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Conserved domains on  [gi|6681219|ref|NP_033494|]
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dihydropyrimidinase-related protein 3 CRMP4a [Mus musculus]

Protein Classification

D-hydantoinase family protein (domain architecture ID 10797696)

D-hydantoinase family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
17-471 0e+00

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


:

Pssm-ID: 273937  Cd Length: 454  Bit Score: 759.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQV 176
Cdd:TIGR02033  81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    337 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681219    416 ALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
 
Name Accession Description Interval E-value
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
17-471 0e+00

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937  Cd Length: 454  Bit Score: 759.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQV 176
Cdd:TIGR02033  81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    337 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681219    416 ALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
17-466 0e+00

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 734.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:cd01314   1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKeKGVNSFMVYMAYKDLYQV 176
Cdd:cd01314  81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  337 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 6681219  417 LKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
PRK08323 PRK08323
phenylhydantoinase; Validated
16-475 0e+00

phenylhydantoinase; Validated


Pssm-ID: 236240  Cd Length: 459  Bit Score: 569.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    16 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKA 95
Cdd:PRK08323   2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    96 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEkGVNSFMVYMAYKDLYQ 175
Cdd:PRK08323  78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   176 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   256 MSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 332
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   333 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 411
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681219   412 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 475
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];
17-464 6.93e-106

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 223122 [Multi-domain]  Cd Length: 430  Bit Score: 325.05  E-value: 6.93e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:COG0044   3 LLIKNARVVDPGEDEVADILIKDGKIAAIGKNLEPTSGAEIIDAKGLLVLPGLVDLHVHFREP--GFEHKETFETGSRAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEvQSLSKEKGVNSFMVYMAYKdlyqV 176
Cdd:COG0044  81 AAGGVTTVVDMPNTKPPIDTAEALEDKLERAKGKSVVDYAFYGGLTKGNLGKLEL-TERGVEAGFKGFMDDSTGA----L 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARmleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:COG0044 156 DDDVLEEALEYAAELGALILVHAEDDDLIAEGVMN---EGLRAPELGLAGRPPIAEASAIARDLELARATGARVHICHIS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  257 SKSAADLISQARKKGNVVFGEPitaslgidgT-HYWSKN----WAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGS 331
Cdd:COG0044 233 TKESVELIRAAKAEGIRVTAEV---------TpHHLLLDeediEDLGTLAKVNPPLR-DEEDREALWEALKDGVIDVIAS 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  332 AHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNLYPrKGRIAVGSDSDLVI 411
Cdd:COG0044 303 DHAPHTLEEKRLP---FEEAPSGIPGLETALPLLLT-LVKKGRLSLERLVELLSTNPARIFGLPP-KGAIEEGADADLVL 377
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 6681219  412 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQG 464
Cdd:COG0044 378 VDPDEEWTIRAEELYSKAKNSPFEGFELKGRVVATILRGKVVYEDGEVIAKPG 430
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
64-453 9.98e-26

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyzes adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 396526 [Multi-domain]  Cd Length: 335  Bit Score: 107.97  E-value: 9.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     64 MVIPGGIDVHTHFQM-----PYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLT--EAYEKW----REWADGKSC 132
Cdd:pfam01979   1 IVLPGLIDAHVHLEMgllrgIVPPEFAYEALALGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELplglRFLGPGCSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    133 CDYALHVDITHWNDSVKQEVQSLSKEKGVnsFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqEQARM 212
Cdd:pfam01979  81 DGGELEGRKALREKLKAGADFIKGMADGV--VFVGLAPHGAPTFTDDELKAALEEAKKYGLPVAIHALETKG---EVEDA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    213 LEMGITGPEghVLSRPEELEAEAVFRAITVASQTNCPLYVTkvmskSAADLISQARKKGNvvfgepitaslgidgthyws 292
Cdd:pfam01979 156 IAAFGGGIE--HGTHLEVAESLGLLDVIKLILAHGVHLSPT-----EANLLAEHLKGAGV-------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    293 knwakaaAFVTSPPLSPDPTTPDyINSLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERMSViwdkAVAT 372
Cdd:pfam01979 209 -------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGA--------ASGNSLNMLEELRLALKLQRLL----YDEE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    373 GKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALkivsaknhqsvaeyNIFEGMELRGAPLVVICQGKI 452
Cdd:pfam01979 269 GGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIVKGKI 334

                  .
gi 6681219    453 M 453
Cdd:pfam01979 335 V 335
 
Name Accession Description Interval E-value
D-hydantoinase TIGR02033
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ...
17-471 0e+00

D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.


Pssm-ID: 273937  Cd Length: 454  Bit Score: 759.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:TIGR02033   1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQV 176
Cdd:TIGR02033  81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    337 STAQK-AIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681219    416 ALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPC 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
D-HYD cd01314
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ...
17-466 0e+00

D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.


Pssm-ID: 238639 [Multi-domain]  Cd Length: 447  Bit Score: 734.79  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKAA 96
Cdd:cd01314   1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKeKGVNSFMVYMAYKDLYQV 176
Cdd:cd01314  81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  257 SKSAADLISQARKKGNVVFGEPITASLGIDGTHYWsKNWAKAAAFVTSPPLSPDpTTPDYINSLLASGDLQLSGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  337 STAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 6681219  417 LKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
PRK08323 PRK08323
phenylhydantoinase; Validated
16-475 0e+00

phenylhydantoinase; Validated


Pssm-ID: 236240  Cd Length: 459  Bit Score: 569.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    16 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNlivpGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQGTKA 95
Cdd:PRK08323   2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    96 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEkGVNSFMVYMAYKDLYQ 175
Cdd:PRK08323  78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   176 VSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   256 MSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdpttPDYINSL---LASGDLQLSGSA 332
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD----KEHQDALwrgLQDGDLQVVATD 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   333 HCTFSTAQKA-IGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 411
Cdd:PRK08323 313 HCPFCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVI 392
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681219   412 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFS 475
Cdd:PRK08323 393 WDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
PLN02942 PLN02942
dihydropyrimidinase
12-485 0e+00

dihydropyrimidinase


Pssm-ID: 178530  Cd Length: 486  Bit Score: 548.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    12 ITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGMTTVDDFFQ 91
Cdd:PLN02942   2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    92 GTKAALAGGTTMIIDHVVPePESSLTEAYEKWREWADgKSCCDYALHVDITHWNDSVKQEVQSLSKEKGVNSFMVYMAYK 171
Cdd:PLN02942  82 GQAAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   172 DLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   252 VTKVMSKSAADLISQARKKGNVVFGEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSPdPTTPDYINSLLASGDLQLSGS 331
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   332 AHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVI 411
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681219   412 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSPFSdYVYKRIKAR 485
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKA 471
PRK13404 PRK13404
dihydropyrimidinase; Provisional
17-473 6.25e-116

dihydropyrimidinase; Provisional


Pssm-ID: 184033 [Multi-domain]  Cd Length: 477  Bit Score: 352.46  E-value: 6.25e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPY-KGMTTVDDFFQGTKA 95
Cdd:PRK13404   6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    96 ALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSV-KQEVQSLSKEkGVNSFMVYMAYKDLy 174
Cdd:PRK13404  84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   175 QVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   255 VMSKSAADLISQARKKGNVVFGEP------ITAS-LGIDGTHywsknwakAAAFVTSPPLSpDPTTPDYINSLLASGDLQ 327
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   328 LSGSAHCTF---STAQKAIGKDN--FTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 402
Cdd:PRK13404 313 VFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6681219   403 VGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRFIPCSP 473
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
AllB COG0044
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];
17-464 6.93e-106

Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 223122 [Multi-domain]  Cd Length: 430  Bit Score: 325.05  E-value: 6.93e-106
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:COG0044   3 LLIKNARVVDPGEDEVADILIKDGKIAAIGKNLEPTSGAEIIDAKGLLVLPGLVDLHVHFREP--GFEHKETFETGSRAA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEvQSLSKEKGVNSFMVYMAYKdlyqV 176
Cdd:COG0044  81 AAGGVTTVVDMPNTKPPIDTAEALEDKLERAKGKSVVDYAFYGGLTKGNLGKLEL-TERGVEAGFKGFMDDSTGA----L 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  177 SNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARmleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVM 256
Cdd:COG0044 156 DDDVLEEALEYAAELGALILVHAEDDDLIAEGVMN---EGLRAPELGLAGRPPIAEASAIARDLELARATGARVHICHIS 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  257 SKSAADLISQARKKGNVVFGEPitaslgidgT-HYWSKN----WAKAAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGS 331
Cdd:COG0044 233 TKESVELIRAAKAEGIRVTAEV---------TpHHLLLDeediEDLGTLAKVNPPLR-DEEDREALWEALKDGVIDVIAS 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  332 AHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNLYPrKGRIAVGSDSDLVI 411
Cdd:COG0044 303 DHAPHTLEEKRLP---FEEAPSGIPGLETALPLLLT-LVKKGRLSLERLVELLSTNPARIFGLPP-KGAIEEGADADLVL 377
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 6681219  412 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQG 464
Cdd:COG0044 378 VDPDEEWTIRAEELYSKAKNSPFEGFELKGRVVATILRGKVVYEDGEVIAKPG 430
L-HYD_ALN cd01315
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ...
17-469 1.98e-68

L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.


Pssm-ID: 238640 [Multi-domain]  Cd Length: 447  Bit Score: 227.94  E-value: 1.98e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:cd01315   2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   97 LAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQSLSK--EKGV---NSFMVYM 168
Cdd:cd01315  80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGF------WGGLVPGNLDQLRPldEAGVvgfKCFLCPS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  169 AYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 248
Cdd:cd01315 152 GVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGC 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  249 PLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVTSPPLSpDPTTPDYINSLLA 322
Cdd:cd01315 232 RLHIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFtaedvpDG----------GTEFKCAPPIR-DAANQEQLWEALE 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  323 SGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIA 402
Cdd:cd01315 301 NGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIA 380
                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6681219  403 VGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNlHVTQGAGRFI 469
Cdd:cd01315 381 VGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
Cyclic_amidohydrolases cd01302
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ...
63-443 6.74e-62

Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.


Pssm-ID: 238627 [Multi-domain]  Cd Length: 337  Bit Score: 207.24  E-value: 6.74e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   63 KMVIPGGIDVHTHFQMPYKGmTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDIt 142
Cdd:cd01302   1 LLVLPGFIDIHVHLRDPGGT-TYKEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  143 hWNDSVKQEVQSLSkEKGVNSFMVYMAYK--DLYQVSNTELYEIFTCLGELGAIAQVHAEngdiiaqeqarmlemgitgp 220
Cdd:cd01302  79 -GPGDVTDELKKLF-DAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  221 eghvlsrpeeleaeavfRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGIDgTHYWSKNWAKaaa 300
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLD-ESMLRLNGAW--- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  301 FVTSPPLSPdPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDnFTAIPEGTNGVEERMSVIWdKAVATGKMDENQF 380
Cdd:cd01302 196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETL 272
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6681219  381 VAVTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAP 443
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
PRK06189 PRK06189
allantoinase; Provisional
17-460 4.93e-54

allantoinase; Provisional


Pssm-ID: 235732 [Multi-domain]  Cd Length: 451  Bit Score: 189.53  E-value: 4.93e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK06189   5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    97 LAGGTTMIIDHVVPEPESSLT-EAYEKWREWADGKSCCDYALhvdithWNDSVKQEVQSLSK--EKGVNSFMVYMAYK-- 171
Cdd:PRK06189  82 AAGGCTTYFDMPLNSIPPTVTrEALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNSgt 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   172 DLYQVSNTE-LYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPL 250
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   251 YVTKVMSKSAADLISQARKKG-NV---------VFGEPITASLGIdgthywsknWAKAAafvtsPPLSPDPTTPDYINSL 320
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRGvDVsvetcphylLFTEEDFERIGA---------VAKCA-----PPLRSRSQKEELWRGL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   321 LAsGDLQLSGSAH--CTFSTAQKaigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRK 398
Cdd:PRK06189 302 LA-GEIDMISSDHspCPPELKEG----DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQK 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6681219   399 GRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 460
Cdd:PRK06189 376 GRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
PRK02382 PRK02382
dihydroorotase; Provisional
17-470 5.58e-54

dihydroorotase; Provisional


Pssm-ID: 179417  Cd Length: 443  Bit Score: 189.48  E-value: 5.58e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK02382   4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALhvdithwNDSVKQEVQSLSK--EKGVNSF-MVYMA--YK 171
Cdd:PRK02382  82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGI-------NGGVTGNWDPLESlwERGVFALgEIFMAdsTG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   172 DLyQVSNTELYEIFTCLGELGAIAQVHAENGDIIAqEQARMLEmGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLY 251
Cdd:PRK02382 155 GM-GIDEELFEEALAEAARLGVLATVHAEDEDLFD-ELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIH 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   252 VTKVMSKSAADLISqarkkgnvvfGEPITAslgiDGT-HYW---SKNWAKAAAFV-TSPPLSPDPTTPDYINSLlASGDL 326
Cdd:PRK02382 232 IAHISTPEGVDAAR----------REGITC----EVTpHHLflsRRDWERLGTFGkMNPPLRSEKRREALWERL-NDGTI 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   327 QLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSD 406
Cdd:PRK02382 297 DVVASDHAPHTREEKD---ADIWDAPSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYD 371
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6681219   407 SDLVIWDPDALKIVSAKNHQSVAEYNIFEGMElrGA-PLVVICQGKIMLEDGNLHVTQGAGRFIP 470
Cdd:PRK02382 372 ADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
DHOase_IIb cd01318
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ...
62-450 4.45e-38

Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.


Pssm-ID: 238643  Cd Length: 361  Bit Score: 143.63  E-value: 4.45e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   62 GKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIID--HVVPEPESSltEAYEKWREWADGKSCCDYALHV 139
Cdd:cd01318   1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpNTKPPTTTA--EALYEKLRLAAAKSVVDYGLYF 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  140 DIThwndsvKQEVQSLSKEKGVNSFMVYMA--YKDLYQVSNTeLYEIFtclGELGAIAQVHAENGDIIAQEQARMLEMGI 217
Cdd:cd01318  77 GVT------GSEDLEELDKAPPAGYKIFMGdsTGDLLDDEET-LERIF---AEGSVLVTFHAEDEDRLRENRKELKGESA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  218 tgpegHVLSRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGNV-------VFGEPITASLGidgthy 290
Cdd:cd01318 147 -----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLG------ 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  291 wskNWAKaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDkAV 370
Cdd:cd01318 216 ---TLGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKG---YPAAPSGIPGVETALPLMLT-LV 282
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  371 ATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQG 450
Cdd:cd01318 283 NKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
PRK08044 PRK08044
allantoinase AllB;
17-424 4.68e-36

allantoinase AllB;


Pssm-ID: 169193 [Multi-domain]  Cd Length: 449  Bit Score: 139.99  E-value: 4.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLivPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK08044   5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    97 LAGGTTMIIDHVVPE-PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQslskEKGVNSFMVYMAY----- 170
Cdd:PRK08044  81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLDRLHELD----EVGVVGFKCFVATcgdrg 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   171 --KDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQARMLEMGITGPEGHVLSRPEELEAEAVFRAITVASQTNC 248
Cdd:PRK08044 157 idNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGC 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   249 PLYVTKVMSKSAADLISQARKKGNVVFGEPItaslgidgTHYWSKNWAKAAAFVT----SPPLSPDPTTPDYINSLLaSG 324
Cdd:PRK08044 237 RLHVCHISSPEGVEEVTRARQEGQDVTCESC--------PHYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLF-NG 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   325 DLQLSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVG 404
Cdd:PRK08044 308 EIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPG 383
                        410       420
                 ....*....|....*....|
gi 6681219   405 SDSDLVIWDPDALKIVSAKN 424
Cdd:PRK08044 384 KDADFVFIQPNSSYVLKNED 403
pyrC PRK09357
dihydroorotase; Validated
16-456 4.78e-35

dihydroorotase; Validated


Pssm-ID: 236479 [Multi-domain]  Cd Length: 423  Bit Score: 136.86  E-value: 4.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    16 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTK 94
Cdd:PRK09357   2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETGSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    95 AALAGGTTMiidhVV------PEPESSLTEAYEKWRewADGKSCCDyaLHV--DIThwndsVKQEVQSLS-----KEKGV 161
Cdd:PRK09357  79 AAAAGGFTT----VVampntkPVIDTPEVVEYVLDR--AKEAGLVD--VLPvgAIT-----KGLAGEELTefgalKEAGV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   162 NSFMvymayKDLYQVSNTEL-YEIFTCLGELG-AIAQvHAE----NGDIIAQEQARMLEMGITGpeghvlsRPEELEAEA 235
Cdd:PRK09357 146 VAFS-----DDGIPVQDARLmRRALEYAKALDlLIAQ-HCEdpslTEGGVMNEGEVSARLGLPG-------IPAVAEEVM 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   236 VFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPITA------------SLGIDGTHYwsknwaKAAafvt 303
Cdd:PRK09357 213 IARDVLLAEATGARVHICHVSTAGSVELIRWAKALG-----IKVTAevtphhllltdeDLLTYDPNY------KVN---- 277
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   304 sPPLSpdptTPDYINSL---LASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQF 380
Cdd:PRK09357 278 -PPLR----TEEDREALiegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQL 349
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6681219   381 VAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLED 456
Cdd:PRK09357 350 LEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
DHOase_IIa cd01317
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ...
54-444 7.54e-31

Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.


Pssm-ID: 238642 [Multi-domain]  Cd Length: 374  Bit Score: 123.89  E-value: 7.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   54 GVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMII--DHVVPEPESSLTEAYEKWREWADGKS 131
Cdd:cd01317   1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVVcmPNTNPVIDNPAVVELLKNRAKDVGIV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  132 CCDY--ALhvdithwndSVKQEVQSLS-----KEKGVNSFMvymayKDLYQVSNTELyeIFTCLgELGAIAQ----VHAE 200
Cdd:cd01317  79 RVLPigAL---------TKGLKGEELTeigelLEAGAVGFS-----DDGKPIQDAEL--LRRAL-EYAAMLDlpiiVHPE 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  201 NGDIIAQeqARMLEMGITGPEGhVLSRPEELEAEAVFRAITVASQTNCPLYVTKVMSKSAADLISQARKKGnvvfgEPIT 280
Cdd:cd01317 142 DPSLAGG--GVMNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LPVT 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  281 ASLGIdgtHYWS------KNWAkaAAFVTSPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGkdnFTAIPEG 354
Cdd:cd01317 214 AEVTP---HHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPG 284
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  355 TNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPrkGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIF 434
Cdd:cd01317 285 IIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPF 362
                       410
                ....*....|
gi 6681219  435 EGMELRGAPL 444
Cdd:cd01317 363 DGQKLKGRVL 372
PRK07575 PRK07575
dihydroorotase; Provisional
14-459 8.70e-31

dihydroorotase; Provisional


Pssm-ID: 236055  Cd Length: 438  Bit Score: 124.79  E-value: 8.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    14 SDRLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQG 92
Cdd:PRK07575   2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    93 TKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSkekGVNSFMVYMaYKD 172
Cdd:PRK07575  80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPELLTANPTC---GIKIFMGSS-HGP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   173 LYQVSNTELYEIFTCLGELgaIAqVHAENGDIIAQEQARMleMGITGPEGHVLSRPEELEAEAVFRAITVASQTNCPLYV 252
Cdd:PRK07575 156 LLVDEEAALERIFAEGTRL--IA-VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHI 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   253 TKVMSKSAADLISQArkKGNVVFGEPITASLGIDGTHYwsknwAKAAAFV-TSPPLSpDPTTPDYINSLLASGDLQLSGS 331
Cdd:PRK07575 231 LHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAqMNPPLR-SPEDNEALWQALRDGVIDFIAT 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   332 AHCTFSTAQKAIGKDNftaIPEGTNGVEERMSVIWDKAVAtGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVI 411
Cdd:PRK07575 303 DHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADLVL 377
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*...
gi 6681219   412 WDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNL 459
Cdd:PRK07575 378 VDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
PRK09060 PRK09060
dihydroorotase; Validated
17-467 2.77e-30

dihydroorotase; Validated


Pssm-ID: 181632  Cd Length: 444  Bit Score: 123.49  E-value: 2.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAA 96
Cdd:PRK09060   7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    97 LAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNdsvKQEVQSLSKEKGVNSFMVYM--AYKDLY 174
Cdd:PRK09060  84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRDN---ADELAELERLPGCAGIKVFMgsSTGDLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   175 QVSNTELYEIftclgeLGAI---AQVHAEngdiiaqEQARMLEMGITGPEGHVLSRPEELEAEAVFRA----ITVASQTN 247
Cdd:PRK09060 161 VEDDEGLRRI------LRNGrrrAAFHSE-------DEYRLRERKGLRVEGDPSSHPVWRDEEAALLAtrrlVRLARETG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   248 CPLYVTKVMSKSAADLISQARkkgNVVFGEPITASLGIDGTHYWSKNWAKAaafVTSPPLSpDPTTPDYINSLLASGDLQ 327
Cdd:PRK09060 228 RRIHVLHVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVD 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   328 LSGSAHCTFSTAQKAigkDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDS 407
Cdd:PRK09060 301 VLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDA 375
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   408 DLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLhVTQGAGR 467
Cdd:PRK09060 376 DFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
PRK04250 PRK04250
dihydroorotase; Provisional
22-457 1.40e-28

dihydroorotase; Provisional


Pssm-ID: 235265  Cd Length: 398  Bit Score: 117.56  E-value: 1.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    22 GRIVNDDQSFYADIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTH---FQMPYKgmTTVDdffQGTKAALA 98
Cdd:PRK04250   4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHlrdFEESYK--ETIE---SGTKAALH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    99 GGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSLSKEkgvnsFMVyMAYKDLYQVSN 178
Cdd:PRK04250  77 GGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKI-----FMG-ASTGGIFSENF 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   179 TELYEiftclgELGAIAQVHAENGDIIAQEqarmlemgitgPEghvlsRPEELEAEAVFRAITVASQTNCPLYVTKVMSK 258
Cdd:PRK04250 151 EVDYA------CAPGIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTK 208
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   259 SAADLISQARKkgnvvfgEPITASLGIDGTHYWSKNWAKAAAFVTSPPLSpdpTTPDYINSLLASGDLQLSGSAHCTFST 338
Cdd:PRK04250 209 DGLKLILKSNL-------PWVSFEVTPHHLFLTRKDYERNPLLKVYPPLR---SEEDRKALWENFSKIPIIASDHAPHTL 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   339 AQKAIGKdnfTAIPegtnGVEERMSVIWDkAVATGKMDENQFVAVTSTNAAKIFNlYPRKGrIAVGSDSDLVIWDPDALK 418
Cdd:PRK04250 279 EDKEAGA---AGIP----GLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEW 348
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 6681219   419 IVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDG 457
Cdd:PRK04250 349 TIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
PLN02795 PLN02795
allantoinase
12-469 4.24e-28

allantoinase


Pssm-ID: 178392  Cd Length: 505  Bit Score: 117.95  E-value: 4.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    12 ITSDRLLIKGGRIVNDdqsfyadIYMEDGLIKQIGDNLIVPG---GVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDD 88
Cdd:PLN02795  48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    89 FFQGTKAALAGGTTMIIDhvVP---EPESSLTEAYEKWREWADGKsccdyaLHVDITHWNDSVKQEVQSLSKEK------ 159
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPENAHNASVLEelldag 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   160 --GVNSFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIIAQEQarMLEMGITGPEGHVLSRPEELEAEAVF 237
Cdd:PLN02795 191 alGLKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDS--RLDADPRSYSTYLKSRPPSWEQEAIR 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   238 RAITVASQTN-------CPLYVTKVM-SKSAADLISQARKKGNVVFGEPITASLGI------DGthywsknwakAAAFVT 303
Cdd:PLN02795 269 QLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFsaeeipDG----------DTRYKC 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   304 SPPLSpDPTTPDYINSLLASGDLQLSGSAHCTFSTAQKAIGKDNFTAIPEGTNGVEERMSVIWDKAVATGkMDENQFVAV 383
Cdd:PLN02795 339 APPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARW 416
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   384 TSTNAAKIFNLyPRKGRIAVGSDSDLVIWDPDALKIVSAK-----NHQSVAEYnifEGMELRGAPLVVICQGKIMLEDGN 458
Cdd:PLN02795 417 WSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDESypiyhKHKSLSPY---LGTKLSGKVIATFVRGNLVFLEGK 492
                        490
                 ....*....|.
gi 6681219   459 lHVTQGAGRFI 469
Cdd:PLN02795 493 -HAKQACGSPI 502
Amidohydro_1 pfam01979
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ...
64-453 9.98e-26

Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase superfamily. The family includes Adenine deaminase EC:3.5.4.2 that hydrolyzes adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilisation as a purine and also as a nitrogen source. This family also includes dihydroorotase and N-acetylglucosamine-6-phosphate deacetylases, EC:3.5.1.25 These enzymes catalyze the reaction N-acetyl-D-glucosamine 6-phosphate + H2O <=> D-glucosamine 6-phosphate + acetate. This family includes the catalytic domain of urease alpha subunit. Dihydroorotases (EC:3.5.2.3) are also included.


Pssm-ID: 396526 [Multi-domain]  Cd Length: 335  Bit Score: 107.97  E-value: 9.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     64 MVIPGGIDVHTHFQM-----PYKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLT--EAYEKW----REWADGKSC 132
Cdd:pfam01979   1 IVLPGLIDAHVHLEMgllrgIVPPEFAYEALALGITTMLKSGTTTVLDMGATTSTGIEAllEAAEELplglRFLGPGCSL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    133 CDYALHVDITHWNDSVKQEVQSLSKEKGVnsFMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAENGDIiaqEQARM 212
Cdd:pfam01979  81 DGGELEGRKALREKLKAGADFIKGMADGV--VFVGLAPHGAPTFTDDELKAALEEAKKYGLPVAIHALETKG---EVEDA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    213 LEMGITGPEghVLSRPEELEAEAVFRAITVASQTNCPLYVTkvmskSAADLISQARKKGNvvfgepitaslgidgthyws 292
Cdd:pfam01979 156 IAAFGGGIE--HGTHLEVAESLGLLDVIKLILAHGVHLSPT-----EANLLAEHLKGAGV-------------------- 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    293 knwakaaAFVTSPPLSPDPTTPDyINSLLASGDLQLSGSAHCtfstaqkaIGKDNFTAIPEGTNGVEERMSViwdkAVAT 372
Cdd:pfam01979 209 -------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGA--------ASGNSLNMLEELRLALKLQRLL----YDEE 268
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    373 GKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALkivsaknhqsvaeyNIFEGMELRGAPLVVICQGKI 452
Cdd:pfam01979 269 GGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPL--------------AAFFGLKPDGNVKKVIVKGKI 334

                  .
gi 6681219    453 M 453
Cdd:pfam01979 335 V 335
PRK01211 PRK01211
dihydroorotase; Provisional
32-470 4.33e-23

dihydroorotase; Provisional


Pssm-ID: 179247  Cd Length: 409  Bit Score: 101.86  E-value: 4.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    32 YADIYMEDGLIKQIGDNLivpGGVKTIEANGkMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIIDHVVPE 111
Cdd:PRK01211  15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   112 PESSLTEAYEKWREWADGKSCCDYALHVDITHWNDSVKQEVQSlskekgvnSFMVYMAYKDLYQVSNTELYEIfTCLGEL 191
Cdd:PRK01211  89 IPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNNALILDERSI--------GLKVYMGGTTNTNGTDIEGGEI-KKINEA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   192 GAIAQVHAENGDIIAQEQARMLEMgitgpEGHVLSRPEELEAEAVFRAITVASQtncplyvTKVMS-KSAADLISQarkk 270
Cdd:PRK01211 160 NIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIAhVSSIDVIGR---- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   271 gnvvFGEPITASlgidgtHYWSKNWAKAAAF-VTSPPLSPDPTTPDYINSLLaSGDLQLSGSAHCTFSTAQKAigkdNFT 349
Cdd:PRK01211 224 ----FLREVTPH------HLLLNDDMPLGSYgKVNPPLRDRWTQERLLEEYI-SGRFDILSSDHAPHTEEDKQ----EFE 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   350 AIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVA 429
Cdd:PRK01211 289 YAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKC 365
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 6681219   430 EYNIFEGMELRgAPLVVICQGKIMLEDGNLhVTQGAGRFIP 470
Cdd:PRK01211 366 PVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVP 404
PRK09236 PRK09236
dihydroorotase; Reviewed
15-460 3.71e-22

dihydroorotase; Reviewed


Pssm-ID: 181716  Cd Length: 444  Bit Score: 99.17  E-value: 3.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    15 DRLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTK 94
Cdd:PRK09236   2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    95 AALAGGTTMIID--HVVPepeSSLT-EAYEKWREWADGKSCCDYALHVDIThwNDSVkQEVQSLSKEK--GVNSFM---- 165
Cdd:PRK09236  80 AAVAGGITSFMEmpNTNP---PTTTlEALEAKYQIAAQRSLANYSFYFGAT--NDNL-DEIKRLDPKRvcGVKVFMgast 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   166 ----VymaykDLYQVsnteLYEIFTCLGELgaIAqVHAENGDIIAQEQARMLEM---GITgPEGHVLSRpeelEAEAVFR 238
Cdd:PRK09236 154 gnmlV-----DNPET----LERIFRDAPTL--IA-THCEDTPTIKANLAKYKEKygdDIP-AEMHPLIR----SAEACYK 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   239 ----AITVASQTNCPLYVTKVMSKSAADLISQ---ARKKgnvvfgepITASLGIDGTHYWSKNWAKAAAFVTSPPLSPDP 311
Cdd:PRK09236 217 ssslAVSLAKKHGTRLHVLHISTAKELSLFENgplAEKR--------ITAEVCVHHLWFDDSDYARLGNLIKCNPAIKTA 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   312 TTPDYINSLLASGDLQLSGSAHCTFSTAQKaigKDNFTAIPEGTNGVEERMSVIWDKaVATGKMDENQFVAVTSTNAAKI 391
Cdd:PRK09236 289 SDREALRQALADDRIDVIATDHAPHTWEEK---QGPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAIL 364
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6681219   392 FNLyPRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLH 460
Cdd:PRK09236 365 FDI-KERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLV 432
ATZ_TRZ_like cd01298
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ...
17-122 4.70e-13

TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.


Pssm-ID: 238623 [Multi-domain]  Cd Length: 411  Bit Score: 71.08  E-value: 4.70e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPG--GVKTIEANGKMVIPGGIDVHTHFQM------------- 78
Cdd:cd01298   1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681219   79 --------PYKGMTTVDDFFQGTKAALA----GGTTMIIDHVVPEPEsSLTEAYEK 122
Cdd:cd01298  81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPD-AVAEAAEE 135
pyrC PRK00369
dihydroorotase; Provisional
34-468 6.95e-12

dihydroorotase; Provisional


Pssm-ID: 234738  Cd Length: 392  Bit Score: 67.48  E-value: 6.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    34 DIYMEDGlIKQIGDNLIVpgGVKTIEANGK---------MVIPGGIDVHTHF---QMPYKgmttvDDFFQGTKAALAGGT 101
Cdd:PRK00369   8 KAYLGKE-IKEICINFDR--RIKEIKSRCKpdldlpqgtLILPGAIDLHVHLrglKLSYK-----EDVASGTSEAAYGGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   102 TMIIDHVVPEPESSLTEAY-EKWREWADGkSCCDYALHVDIThwnDSVKqEVQSLskekGVNSFMVYMayKDLyqvsntE 180
Cdd:PRK00369  80 TLVADMPNTIPPLNTPEAItEKLAELEYY-SRVDYFVYSGVT---KDPE-KVDKL----PIAGYKIFP--EDL------E 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   181 LYEIFTCLGELGAIAQVHAEngdiiaqeqarmLEMGITGPEGhvLSRPEELEAEAVFRAITVASqtncpLYVTKVmskSA 260
Cdd:PRK00369 143 REETFRVLLKSRKLKILHPE------------VPLALKSNRK--LRRNCWYEIAALYYVKDYQN-----VHITHA---SN 200
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   261 ADLISQARKKGnvvFGEPITAS-LGIDG-THYWSKnwakaaafvTSPPLSpDPTTPDYINSLLASGDLQLSGsaHCTFST 338
Cdd:PRK00369 201 PRTVRLAKELG---FTVDITPHhLLVNGeKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIASD--HAPHSS 265
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   339 AQKaigKDNFTAIPEGTNGVEERMSVIWdKAVATGKMDENQFVAVTSTNAAKIFNLypRKGRIAVGSDSDLVIwdpdaLK 418
Cdd:PRK00369 266 FEK---LQPYEVCPPGIAALSFTPPFIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTV-----IQ 334
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6681219   419 IVSAKNHQ--SVAEYNIFEGMELRGAPLVVICQGKIMLEDGNLHVTQGAGRF 468
Cdd:PRK00369 335 FEDWRYSTkySKVIETPLDGFELKASVYATIVQGKLAYLEGEVFPVKGINPF 386
D-aminoacylase cd01297
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ...
17-467 1.25e-11

D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.


Pssm-ID: 238622 [Multi-domain]  Cd Length: 415  Bit Score: 66.55  E-value: 1.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVndDQS----FYADIYMEDGLIKQIGDNLIVPGgVKTIEANGKMVIPGGIDVHTHfqmpYKGMTTVDDFFqg 92
Cdd:cd01297   2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTH----YDGQVFWDPDL-- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   93 TKAALAGGTTMIIDH-------VVPEPESSLTEAYEKWREWADGK-----SCCDYALHVD------------------IT 142
Cdd:cd01297  73 RPSSRQGVTTVVLGNcgvspapANPDDLARLIMLMEGLVALGEGLpwgwaTFAEYLDALEarppavnvaalvghaalrRA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  143 HWNDSVKQ----EVQSLSK--EKGVNS----FMVYMAYKDLYQVSNTELYEIFTCLGELGAIAQVHAEN-GDIIAQEQAR 211
Cdd:cd01297 153 VMGLDAREateeELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRYeGDSILEALDE 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  212 MLEMGitgpeghvlsrpEELEAEAVFRAITVASQTNCPLYvtkvmsKSAADLISQARKKGNVVFGE--PITASLGidgth 289
Cdd:cd01297 233 LLRLG------------RETGRPVHISHLKSAGAPNWGKI------DRLLALIEAARAEGLQVTADvyPYGAGSE----- 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  290 ywsknwAKAAAFVTSPPlspdpttpdyinsLLASGDLQLSGSAH----CTFStaqKAIGKdnftaipegtnGVEERMSVI 365
Cdd:cd01297 290 ------DDVRRIMAHPV-------------VMGGSDGGALGKPHprsyGDFT---RVLGH-----------YVRERKLLS 336
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  366 WDKAVAtgKMdenqfvavtSTNAAKIFNLYPRkGRIAVGSDSDLVIWDPDALKIVS---AKNHQSvaeynifEGMELrga 442
Cdd:cd01297 337 LEEAVR--KM---------TGLPARVFGLADR-GRIAPGYRADIVVFDPDTLADRAtftRPNQPA-------EGIEA--- 394
                       490       500
                ....*....|....*....|....*
gi 6681219  443 plvVICQGKIMLEDGnLHVTQGAGR 467
Cdd:cd01297 395 ---VLVNGVPVVRDG-AFTGARPGR 415
CAD_DHOase cd01316
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ...
66-466 1.58e-11

The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.


Pssm-ID: 238641 [Multi-domain]  Cd Length: 344  Bit Score: 65.93  E-value: 1.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   66 IPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMIidHVVPEPESSL--TEAYEKWREWADGKSCCDYALHVDITH 143
Cdd:cd01316   5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIvdVASLKLVQSLAQAKARCDYAFSIGATS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  144 WNDSVKQEVQSlskeKGVNSFMVymaykdlyqvsnteLYEIFTCLgELGAIAQVhaengdiiaqeqARMLEmgiTGPEgh 223
Cdd:cd01316  81 TNAATVGELAS----EAVGLKFY--------------LNETFSTL-ILDKITAW------------ASHFN---AWPS-- 124
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  224 vlSRPEELEAEAVFRA--ITVASQTNCPLYVTKVMSKSAADLISQARKKGNVVFGEPITASLGI---DGTHYWSknwaka 298
Cdd:cd01316 125 --TKPIVTHAKSQTLAavLLLASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLsqdDLPRGQY------ 196
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  299 aafvtspPLSPDPTTPDYINSL---LASGDLQLSGSAHCTFstAQKAIGKdnftaIPEGTNGVEERMSVIWdKAVATGKM 375
Cdd:cd01316 197 -------EVRPFLPTREDQEALwenLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRL 261
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  376 DENQFVAVTSTNAAKIFNLYPRkgriavgSDSDLVIwDPDALKIVSAKNHQSVAEYNIFEGMELRGAPLVVICQGKIMLE 455
Cdd:cd01316 262 TIEDIVDRLHTNPKRIFNLPPQ-------SDTYVEV-DLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFI 333
                       410
                ....*....|.
gi 6681219  456 DGNLHVTQGAG 466
Cdd:cd01316 334 DGEIVAPPGFG 344
SsnA COG0402
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ...
14-220 6.19e-10

Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 223479 [Multi-domain]  Cd Length: 421  Bit Score: 61.31  E-value: 6.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   14 SDRLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHF-QMPYKG------- 82
Cdd:COG0402   1 MTMLLIRGDLLLTNDPEgriEDGDLVIEDGKIVAIGANAEGPPDEEVIDAKGKLVLPGFVNAHTHLdQTLLRGladdlpl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   83 --------------MTTVDDFFQGTKAA----LAGGTTMIIDH--VVPEPESSLTEAYEKWRE-WADGKSCCDYAL--HV 139
Cdd:COG0402  81 lewleryvwprearLLTEEDLYARALLAllemLRNGTTTARTHvdVVAESADAAFEAALEVGLrAVLGPVLQDVAFpdPG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  140 DITHWNDSVKQEVQSLSKEKGVNSFMVymAYKDLYQVSNTELYEIFTCLGELGAIAQVH-AENGDiiaqEQARMLEMGIT 218
Cdd:COG0402 161 AETDEELEETEELLREAHGLGRDVVGL--APHFPYTVSPELLESLDELARKYGLPVHIHlAETLD----EVERVLEPYGA 234

                ..
gi 6681219  219 GP 220
Cdd:COG0402 235 RP 236
PRK09237 PRK09237
amidohydrolase/deacetylase family metallohydrolase;
17-413 2.94e-09

amidohydrolase/deacetylase family metallohydrolase;


Pssm-ID: 236423  Cd Length: 380  Bit Score: 59.09  E-value: 2.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFqmpYKGMTtvDDFFQGTK 94
Cdd:PRK09237   1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVHV---YPGST--PYGDEPDE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    95 AALAGGTTMIIDhvvpepesslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQSLSKEKgvnsfmVYmAYKDLY 174
Cdd:PRK09237  76 VGVRSGVTTVVD--------------------AGSAGADNF----------DDFRKLTIEASKTR------VL-AFLNIS 118
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   175 QV---SNTELYEIFTClgELGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEEleaeavfRAITVASQTNCPLY 251
Cdd:PRK09237 119 RIgllAQDELADLEDI--DADAVAEAVKRNPDFIVGIKARM-SSSVVGDNG---IEPLE-------LAKAIAAEANLPLM 185
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   252 VTKVMSKSAADLISQARKKGNVVfgepitaslgidgTHYWSKnwaKAAAFVTspplsPDPTTPDYINSLLASGdLQLS-- 329
Cdd:PRK09237 186 VHIGNPPPSLEEILELLRPGDIL-------------THCFNG---KPNRILD-----EDGELRPSVLEALERG-VRLDvg 243
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   330 -GSAHCTFSTAQKAIGKD-NFTAIpeGT--------NGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKG 399
Cdd:PRK09237 244 hGTASFSFKVAEAAIAAGiLPDTI--STdiycrnriNGPVYSLATVMSKFLALG-MPLEEVIAAVTKNAADALRL-PELG 319
                        410
                 ....*....|....
gi 6681219   400 RIAVGSDSDLVIWD 413
Cdd:PRK09237 320 RLQVGSDADLTLFT 333
PRK07228 PRK07228
5'-deoxyadenosine deaminase;
16-220 2.04e-08

5'-deoxyadenosine deaminase;


Pssm-ID: 180895 [Multi-domain]  Cd Length: 445  Bit Score: 56.55  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    16 RLLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHF-QMPYKGMTtvDDF-- 89
Cdd:PRK07228   2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLcQTLFRGIA--DDLel 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    90 ----------FQGTKAA--------------LAGGTTMIIDHV-VPEPESSLTEAYEKWREWADGKSCCDYALHVDIT-- 142
Cdd:PRK07228  80 ldwlkdriwpLEAAHDAesmyysallgigelIESGTTTIVDMEsVHHTDSAFEAAGESGIRAVLGKVMMDYGDDVPEGlq 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   143 -HWNDSVKQEVQSLSKEKGVNSFMVYMAYKDLYQVSNTElyeifTCLGELGAIAQ-------VHA-EN-GDIIAQEQARM 212
Cdd:PRK07228 160 eDTEASLAESVRLLEKWHGADNGRIRYAFTPRFAVSCTE-----ELLRGVRDLADeygvrihTHAsENrGEIETVEEETG 234
                        250
                 ....*....|....*
gi 6681219   213 L-------EMGITGP 220
Cdd:PRK07228 235 MrnihyldEVGLTGE 249
NagA cd00854
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ...
17-75 3.02e-08

N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.


Pssm-ID: 238434 [Multi-domain]  Cd Length: 374  Bit Score: 55.66  E-value: 3.02e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6681219   17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:cd00854   1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIH 59
PRK09061 PRK09061
D-glutamate deacylase; Validated
16-104 6.15e-08

D-glutamate deacylase; Validated


Pssm-ID: 236369 [Multi-domain]  Cd Length: 509  Bit Score: 55.09  E-value: 6.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    16 RLLIKGGRIVNDDQSFYA--DIYMEDGLIKQIGDNLIvpGGVKTIEANGKMVIPGGIDVHTHfqmpykGMTTVDDFFQgt 93
Cdd:PRK09061  20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH------GQSVAAYRMQ-- 89
                         90
                 ....*....|.
gi 6681219    94 kaALAGGTTMI 104
Cdd:PRK09061  90 --AFDGVTTAL 98
Met_dep_hydrolase_B cd01307
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ...
34-413 1.51e-07

Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238632 [Multi-domain]  Cd Length: 338  Bit Score: 53.49  E-value: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   34 DIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFqmpYKGMTTVDDffQGTKAALAGGTTMIIDhvvpepe 113
Cdd:cd01307   1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHV---YQGGTRYGD--RPDMIGVKSGVTTVVD------- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  114 sslteayekwrewADGKSCCDYalhvdithwnDSVKQEVQSLSKEKgvnsfmVYmAYKDLY---QVSNTELYEIFTClgE 190
Cdd:cd01307  69 -------------AGSAGADNI----------DGFRYTVIERSATR------VY-AFLNISrvgLVAQDELPDPDNI--D 116
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  191 LGAIAQVHAENGDIIAQEQARMlEMGITGPEGhvlSRPEELEAEAvfraitvASQTNCPLYvtkVMSKSAADLISQA--- 267
Cdd:cd01307 117 EDAVVAAAREYPDVIVGLKARA-SKSVVGEWG---IKPLELAKKI-------AKEADLPLM---VHIGSPPPILDEVvpl 182
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  268 RKKGNVVfgepitaslgidgTHYWSknwAKAAAFVTspplsPDPTTPDYINSLLASG---DLQlSGSAHCTFSTAQKAIG 344
Cdd:cd01307 183 LRRGDVL-------------THCFN---GKPNGIVD-----EEGEVLPLVRRARERGvifDVG-HGTASFSFRVARAAIA 240
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6681219  345 KD-NFTAI------PEGTNGVEERMSVIWDKAVATGkMDENQFVAVTSTNAAKIFNLyPRKGRIAVGSDSDLVIWD 413
Cdd:cd01307 241 AGlLPDTIssdihgRNRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
metallo-dependent_hydrolases cd01292
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ...
70-276 1.93e-07

Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.


Pssm-ID: 238617 [Multi-domain]  Cd Length: 275  Bit Score: 52.72  E-value: 1.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   70 IDVHTHFQMP----------------YKGMTTVDDFFQGTKAALAGGTTMIIDHVVPEPESSLTEAYEKWREWADGKSCC 133
Cdd:cd01292   2 IDTHVHLDGSalrgtrlnlelkeaeeLSPEDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  134 DYALHVDITH--------WNDSVKQEVQSLsKEKGVNSFMVYMAYKDlYQVSNTELYEIFTCLGELGAIAQVHAENGDII 205
Cdd:cd01292  82 RVVLGLGIPGvpaavdedAEALLLELLRRG-LELGAVGLKLAGPYTA-TGLSDESLRRVLEEARKLGLPVVIHAGELPDP 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681219  206 AQEQARMLEMGITGPE---GHVLSRPEELEAEAVFRAITVASqTNCPLYVTKVMSKSAADLISQARKKGNVVFG 276
Cdd:cd01292 160 TRALEDLVALLRLGGRvviGHVSHLDPELLELLKEAGVSLEV-CPLSNYLLGRDGEGAEALRRLLELGIRVTLG 232
AdeC COG1001
Adenine deaminase [Nucleotide transport and metabolism];
17-105 2.57e-07

Adenine deaminase [Nucleotide transport and metabolism];


Pssm-ID: 223933 [Multi-domain]  Cd Length: 584  Bit Score: 53.46  E-value: 2.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVN--DDQSFYADIYMEDGLIkqIGDNL-IVPGGVKTIEANGKMVIPGGIDVHTHFQMpykGMTTVDDFfqgT 93
Cdd:COG1001  26 LVLKNGRIVDvvTGEIYKGDIAIAGGRI--VGVIGeYRAEATEVIDAAGRYIVPGFIDAHLHIES---SMLTPSEF---A 97
                        90
                ....*....|..
gi 6681219   94 KAALAGGTTMII 105
Cdd:COG1001  98 RAVLPHGTTTVV 109
Amidohydro_3 pfam07969
Amidohydrolase family;
381-436 5.85e-07

Amidohydrolase family;


Pssm-ID: 400360 [Multi-domain]  Cd Length: 464  Bit Score: 52.15  E-value: 5.85e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6681219    381 VAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALKIVSAKNHQSVAEYNIFEG 436
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
PRK10657 PRK10657
isoaspartyl dipeptidase; Provisional
381-468 6.78e-07

isoaspartyl dipeptidase; Provisional


Pssm-ID: 182623  Cd Length: 388  Bit Score: 51.75  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   381 VAVTSTNAAKIFNLYpRKGRIAVGSDSDLVIWDpDALKIVSaknhqsvaeynifegmelrgaplvVICQGKIMLEDGNLH 460
Cdd:PRK10657 329 LKPLTSNVARFLKLN-GKGEILPGKDADLLVLD-DDLRIEQ------------------------VIAKGKLMVKDGKAL 382

                 ....*...
gi 6681219   461 VTqgaGRF 468
Cdd:PRK10657 383 VK---GTF 387
Bact_CD cd01293
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ...
12-128 7.98e-07

Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.


Pssm-ID: 238618 [Multi-domain]  Cd Length: 398  Bit Score: 51.48  E-value: 7.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   12 ITSDRLLIKGGRIVnddqsfyaDIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH------FQMP------ 79
Cdd:cd01293   2 LRNARLADGGTALV--------DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHldktftGGRWpnnsgg 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   80 -----------YKGMTTVDDFFQ----GTKAALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 128
Cdd:cd01293  74 tlleaiiaweeRKLLLTAEDVKEraerALELAIAHGTTAIRTHVDVDPAAGLKaleallELREEWADLID 143
PRK08204 PRK08204
hypothetical protein; Provisional
15-113 8.79e-07

hypothetical protein; Provisional


Pssm-ID: 181288 [Multi-domain]  Cd Length: 449  Bit Score: 51.54  E-value: 8.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    15 DRLLIKGGRIVNDDQSF----YADIYMEDGLIKQIGDNlIVPGGVKTIEANGKMVIPGGIDVHTH--------------- 75
Cdd:PRK08204   2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHtwqsvlrgigadwtl 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 6681219    76 ---FQMPYKGMTTV---DDFFQGTKA----ALAGGTTMIID--HVVPEPE 113
Cdd:PRK08204  81 qtyFREIHGNLGPMfrpEDVYIANLLgaleALDAGVTTLLDwsHINNSPE 130
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
345-415 9.78e-07

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 224733 [Multi-domain]  Cd Length: 380  Bit Score: 51.11  E-value: 9.78e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6681219  345 KDNFTAIPEGT-NGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWDPD 415
Cdd:COG1820 294 ADGARRLEDGTlAGSTLTMDEAVRNLVEWGGISLAEAVRMASLNPAKALGLDDRLGSIKPGKDADLVVLDDD 365
PRK07369 PRK07369
dihydroorotase; Provisional
33-441 2.04e-06

dihydroorotase; Provisional


Pssm-ID: 236002  Cd Length: 418  Bit Score: 50.37  E-value: 2.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    33 ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQGTKAALAGGTTMI------- 104
Cdd:PRK07369  22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRVailpdtf 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   105 --IDHvvPEPESSL-----TEAYEKWREWADgksccdyalhvdITHwNDSVKQ--EVQSLSkEKGVNSFMVYMAYKDLYQ 175
Cdd:PRK07369 100 ppLDN--PATLARLqqqaqQIPPVQLHFWGA------------LTL-GGQGKQltELAELA-AAGVVGFTDGQPLENLAL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   176 VSNTELYeiftcLGELGAIAQVHAEN----GDIIAQEQARMLEMGITGpeghvlsRPEELEAEAVFRAITVASQTNCPLY 251
Cdd:PRK07369 164 LRRLLEY-----LKPLGKPVALWPCDrslaGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVH 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   252 VTKVMSKSAADLISQARKKGnvvfgEPITASlgidgTHYWSKNWAKAAAFVTSPPLSPDPT--TPDYINSLLA---SGDL 326
Cdd:PRK07369 232 LMRISTARSVELIAQAKARG-----LPITAS-----TTWMHLLLDTEALASYDPNLRLDPPlgNPSDRQALIEgvrTGVI 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   327 QLSGSAHCTFSTAQKAIGkdnFTAIPEGTNGVEERMSVIWDKAVATGKMDENQFVAVTSTNAAKIFNLYPRkgRIAVGSD 406
Cdd:PRK07369 302 DAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQP 376
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 6681219   407 SDLVIWDPDALKIVSAKNHQSVAEYNIFEGMELRG 441
Cdd:PRK07369 377 AELILFDPQKTWTVSAQTLHSLSRNTPWLGQTLKG 411
YtcJ COG1574
Predicted amidohydrolase YtcJ [General function prediction only];
17-88 2.74e-06

Predicted amidohydrolase YtcJ [General function prediction only];


Pssm-ID: 224490 [Multi-domain]  Cd Length: 535  Bit Score: 50.03  E-value: 2.74e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRI--VNDDQSFYADIYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVIPGGIDVHTH--------FQMPYKG 82
Cdd:COG1574   7 LILHNGRIytMDEARPTAEAVAIKDGRIVAVGSdaelKALAGPATEVIDLKGKFVLPGFVDAHLHlisgglslLELNLDG 86

                ....*.
gi 6681219   83 MTTVDD 88
Cdd:COG1574  87 VRSLDD 92
Urease_alpha cd00375
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ...
33-105 3.82e-06

Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.


Pssm-ID: 238221  Cd Length: 567  Bit Score: 49.63  E-value: 3.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:cd00375  83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICP-----------QQIEEALASG 151

                ....*
gi 6681219  101 TTMII 105
Cdd:cd00375 152 ITTMI 156
COG3653 COG3653
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ...
17-128 6.43e-06

N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 226179 [Multi-domain]  Cd Length: 579  Bit Score: 48.79  E-value: 6.43e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVND--DQSFYADIYMEDGLIKQIGDNLIV-PGGVKTIEANGKMVIPGGIDVHTHfqmpYKGMTTVDDFFQgt 93
Cdd:COG3653   8 VVIRDGLIFDGtgNPPFTTDVGIRDGVIAAVAKGALDgTGCPEEVDAAGRIVAPGFIDVHTH----YDAEVLLDPGLR-- 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6681219   94 KAALAGGTTMII-------------DH---------VVPEPESSLTEAYEKWREWAD 128
Cdd:COG3653  82 PSVRHGVTTVVLgncgistapanseDAddlfsrveaVGREFVFGALRDNQTWSTFAE 138
HutI COG1228
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ...
16-75 7.66e-06

Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 224149 [Multi-domain]  Cd Length: 406  Bit Score: 48.52  E-value: 7.66e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6681219   16 RLLIKGGRIVNDDQSFY-ADIYMEDGLIKQIGDNLI-VPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:COG1228  11 MLATLAGRGLPGLGIIEdGAVLIEDGKIVAVGPEEIdIPAGAEVIDAKGKTVTPGLIDAHTH 72
ureC PRK13308
urease subunit alpha; Reviewed
33-104 9.92e-06

urease subunit alpha; Reviewed


Pssm-ID: 183965  Cd Length: 569  Bit Score: 48.16  E-value: 9.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:PRK13308  87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155

                 ....*
gi 6681219   101 -TTMI 104
Cdd:PRK13308 156 iTTML 160
PRK08393 PRK08393
N-ethylammeline chlorohydrolase; Provisional
17-78 1.21e-05

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 181411 [Multi-domain]  Cd Length: 424  Bit Score: 47.87  E-value: 1.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681219    17 LLIKGGRIVNDD--QSFYADIYMEDGLIKQIGDNLIVPGGvKTIEANGKMVIPGGIDVHTHFQM 78
Cdd:PRK08393   3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
PRK15446 PRK15446
phosphonate metabolism protein PhnM; Provisional
16-74 1.23e-05

phosphonate metabolism protein PhnM; Provisional


Pssm-ID: 237967  Cd Length: 383  Bit Score: 47.48  E-value: 1.23e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6681219    16 RLLIKGGRIVNDDQSFYADIYMEDGLIKQIGDNLIVPGGvkTIEANGKMVIPGGIDVHT 74
Cdd:PRK15446   3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHT 59
PRK06380 PRK06380
metal-dependent hydrolase; Provisional
17-93 1.59e-05

metal-dependent hydrolase; Provisional


Pssm-ID: 180548 [Multi-domain]  Cd Length: 418  Bit Score: 47.57  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQS---FYADIYMEDGLIKQIGDnlIVPGGVKTIEANGKMVIPGGIDVHTHFQMP-YKGM---TTVDDF 89
Cdd:PRK06380   3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTaSKGLfddVDLEEF 80

                 ....
gi 6681219    90 FQGT 93
Cdd:PRK06380  81 LMKT 84
FMDH_A cd01304
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ...
19-75 1.93e-05

Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.


Pssm-ID: 238629  Cd Length: 541  Bit Score: 47.41  E-value: 1.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   19 IKGGRIVNDDQSFYA---DIYMEDGlikQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:cd01304   1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
PRK09356 PRK09356
imidazolonepropionase; Validated
13-76 2.51e-05

imidazolonepropionase; Validated


Pssm-ID: 236478 [Multi-domain]  Cd Length: 406  Bit Score: 46.70  E-value: 2.51e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6681219    13 TSDRLLIKGGRIV---NDDQSFY-----ADIYMEDGLIKQIGDNLIVPGGV--KTIEANGKMVIPGGIDVHTHF 76
Cdd:PRK09356   1 MMADLLWTNAQLAtmdGGGMGELgiiedGAIAIEDGKIVWVGPEADLPAAYaaEVIDAGGKLVTPGLIDCHTHL 74
UreC COG0804
Urease alpha subunit [Amino acid transport and metabolism];
17-104 5.30e-05

Urease alpha subunit [Amino acid transport and metabolism];


Pssm-ID: 223875  Cd Length: 568  Bit Score: 45.79  E-value: 5.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   17 LLIKGGRIVNDDQSFYADIYMEDGLIKQIG--------DNLIVPGGVKT--IEANGKMVIPGGIDVHTHFQMPykgmttv 86
Cdd:COG0804  69 LVITNALIIDYWGIVKADIGIKDGRIAGIGkagnpdimDGVTIIIGPSTeiIAGEGKIVTAGGIDTHIHFICP------- 141
                        90
                ....*....|....*....
gi 6681219   87 ddffQGTKAALAGG-TTMI 104
Cdd:COG0804 142 ----QQIEEALASGiTTMI 156
PRK07203 PRK07203
putative aminohydrolase SsnA;
17-76 8.80e-05

putative aminohydrolase SsnA;


Pssm-ID: 235963 [Multi-domain]  Cd Length: 442  Bit Score: 44.93  E-value: 8.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6681219    17 LLIKGGRIV-NDDQSFY---ADIYMEDGLIKQIGDNlivpGGVKT-------IEANGKMVIPGGIDVHTHF 76
Cdd:PRK07203   2 LLIGNGTAItRDPAKPViedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHNHI 68
ureC PRK13206
urease subunit alpha; Reviewed
33-105 1.04e-04

urease subunit alpha; Reviewed


Pssm-ID: 237304  Cd Length: 573  Bit Score: 45.09  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    33 ADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG 100
Cdd:PRK13206  89 ADVGIRDGRIVAIGkagnpdimdgvhPDLVIGPSTEIIAGNGRILTAGAIDCHVHFICP-----------QIVDEALAAG 157

                 ....*
gi 6681219   101 TTMII 105
Cdd:PRK13206 158 ITTLI 162
ureB PRK13985
urease subunit alpha;
5-101 1.36e-04

urease subunit alpha;


Pssm-ID: 184438  Cd Length: 568  Bit Score: 44.50  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219     5 GKKNIPRITSDRLLIKGGRIVNDDQSFYADIYMEDGLIKQIG------------DNLIVPGGVKTIEANGKMVIPGGIDV 72
Cdd:PRK13985  55 SQSNNPSKEELDLIITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqdgvkNNLSVGPATEALAGEGLIVTAGGIDT 134
                         90       100
                 ....*....|....*....|....*....
gi 6681219    73 HTHFQMPYKGMTTvddFFQGTKAALAGGT 101
Cdd:PRK13985 135 HIHFISPQQIPTA---FASGVTTMIGGGT 160
ureC PRK13207
urease subunit alpha; Reviewed
33-104 1.55e-04

urease subunit alpha; Reviewed


Pssm-ID: 237305  Cd Length: 568  Bit Score: 44.40  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    33 ADIYMEDGLIKQIG--------DNLIVPGGVKT--IEANGKMVIPGGIDVHTHFQMPykgmttvddffQGTKAALAGG-T 101
Cdd:PRK13207  85 ADIGIKDGRIVAIGkagnpdiqDGVDIIIGPGTevIAGEGLIVTAGGIDTHIHFICP-----------QQIEEALASGvT 153

                 ...
gi 6681219   102 TMI 104
Cdd:PRK13207 154 TMI 156
PRK10657 PRK10657
isoaspartyl dipeptidase; Provisional
17-76 1.90e-04

isoaspartyl dipeptidase; Provisional


Pssm-ID: 182623  Cd Length: 388  Bit Score: 44.04  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIvnddqsfYA-------DIYMEDGLIKQIGDNLIVPGG---VKTIEANGKMVIPGGIDVHTHF 76
Cdd:PRK10657   3 TLLKNAHV-------YApedlgkkDILIAGGKIIAIADNINIPDIvpdIEVIDASGKILVPGFIDQHVHI 65
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
35-76 2.10e-04

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 43.79  E-value: 2.10e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 6681219   35 IYMEDGLIKQIGD----NLIVPGGVKTIEANGKMVIPGGIDVHTHF 76
Cdd:cd01296   1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
39-75 2.64e-04

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 43.45  E-value: 2.64e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6681219   39 DGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:cd01309   1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
NagA COG1820
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
18-75 3.05e-04

N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];


Pssm-ID: 224733 [Multi-domain]  Cd Length: 380  Bit Score: 43.41  E-value: 3.05e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219   18 LIKGGRIVnDDQSFYADIYM--EDGLIKQIGDNLIvPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:COG1820   3 ALKNGRIF-TGHGVLDGGAVviEDGKIEAVVPAEL-PADAEIIDLKGALLVPGFIDLHIH 60
PRK05985 PRK05985
cytosine deaminase; Provisional
33-128 3.37e-04

cytosine deaminase; Provisional


Pssm-ID: 180337 [Multi-domain]  Cd Length: 391  Bit Score: 43.00  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    33 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPYKGM--------TTVDDFFQGTK---------- 94
Cdd:PRK05985  17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgPSLRERIANERrrraasghpa 96
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 6681219    95 ---------AALAGGTTMIIDHVVPEPESSLT------EAYEKWREWAD 128
Cdd:PRK05985  97 aeralalarAAAAAGTTAMRSHVDVDPDAGLRhleavlAARETLRGLID 145
FwdA COG1229
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
34-75 3.92e-04

Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];


Pssm-ID: 224150  Cd Length: 575  Bit Score: 43.24  E-value: 3.92e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 6681219   34 DIYMEDGlikQIGDNLIVPG-GVKTIEANGKMVIPGGIDVHTH 75
Cdd:COG1229  25 DICVKDG---KIVEESEVSEsKAKVIDASGKLVMPGGVDSHSH 64
Met_dep_hydrolase_C cd01309
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ...
368-421 3.98e-04

Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.


Pssm-ID: 238634 [Multi-domain]  Cd Length: 359  Bit Score: 42.68  E-value: 3.98e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 6681219  368 KAVATGKMDENQFVAVTStNAAKIFNLYPRKGRIAVGSDSDLVIWDPDALKIVS 421
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTS 346
Isoaspartyl-dipeptidase cd01308
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ...
383-462 4.92e-04

Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.


Pssm-ID: 238633  Cd Length: 387  Bit Score: 42.76  E-value: 4.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219  383 VTSTNAAKIFNLYPrKGRIAVGSDSDLVIWDPDaLKIVSaknhqsvaeynifegmelrgaplvVICQGKIMLEDGNLHVT 462
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD-LDINS------------------------VIAKGQIMVRNGKLLVK 383
PRK09059 PRK09059
dihydroorotase; Validated
17-105 7.53e-04

dihydroorotase; Validated


Pssm-ID: 181631  Cd Length: 429  Bit Score: 41.94  E-value: 7.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6681219    17 LLIKGGRIVNDDQSF--YADIYMEDGLIKQIGD---NLIVPGGVKTIEANGKMVIPGGIDVHTHFQMPykGMTTVDDFFQ 91
Cdd:PRK09059   5 ILLANARIIDPSRGLdeIGTVLIEDGVIVAAGKgagNQGAPEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIAS 82
                         90
                 ....*....|....
gi 6681219    92 GTKAALAGGTTMII 105
Cdd:PRK09059  83 ASRAAAAGGVTSII 96
PRK07583 PRK07583
cytosine deaminase;
33-75 1.90e-03

cytosine deaminase;


Pssm-ID: 236062  Cd Length: 438  Bit Score: 40.74  E-value: 1.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 6681219    33 ADIYMEDGLIKQIGDNLIVPGGVKTIEANGKMVIPGGIDVHTH 75
Cdd:PRK07583  41 VDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTH 83
PRK08203 PRK08203
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
16-76 3.31e-03

hydroxydechloroatrazine ethylaminohydrolase; Reviewed


Pssm-ID: 236184 [Multi-domain]  Cd Length: 451  Bit Score: 40.22  E-value: 3.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6681219    16 RLLIKGGRIV---NDDQSFYAD--IYMEDGLIKQIGDNLIVPG-GVKTIEANGKMVIPGGIDVHTHF 76
Cdd:PRK08203   2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHF 68
YtcJ_like cd01300
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ...
34-76 5.15e-03

YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for photochrome A signalling.


Pssm-ID: 238625 [Multi-domain]  Cd Length: 479  Bit Score: 39.60  E-value: 5.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6681219   34 DIYMEDGLIKQIGDN----LIVPGGVKTIEANGKMVIPGGIDVHTHF 76
Cdd:cd01300   1 AVAVRDGRIVAVGSDaeakALKGPATEVIDLKGKTVLPGFIDSHSHL 47
Imidazolone-5PH cd01296
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ...
369-413 7.50e-03

Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.


Pssm-ID: 238621 [Multi-domain]  Cd Length: 371  Bit Score: 38.78  E-value: 7.50e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 6681219  369 AVATGKMDENQFVAVTSTNAAKIFNLYPRKGRIAVGSDSDLVIWD 413
Cdd:cd01296 304 ACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
PRK06038 PRK06038
N-ethylammeline chlorohydrolase; Provisional
17-89 8.42e-03

N-ethylammeline chlorohydrolase; Provisional


Pssm-ID: 180363 [Multi-domain]  Cd Length: 430  Bit Score: 38.58  E-value: 8.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6681219    17 LLIKGGRIVNDDQSFY--ADIYMEDGLIKQIGDNliVPGGVKT-IEANGKMVIPGGIDVHTHFQMP-YKGMTtvDDF 89
Cdd:PRK06038   4 IIIKNAYVLTMDAGDLkkGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTlFRGYA--DDL 76
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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