|
Name |
Accession |
Description |
Interval |
E-value |
| 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: 717.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVMGMTPADDFCQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 97 LAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVrDKGVNSFLVFMAYKDRCQC 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 177 TDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 257 SKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVTSPPINPDpTTADHLTSLLSSGDLQVTGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 337 TTAQKAVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRA 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 188219524 417 TKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPGAG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| 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 [Multi-domain] Cd Length: 454 Bit Score: 652.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVMGMTPADDFCQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 97 LAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVRDKGVNSFLVFMAYKDRCQC 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 177 TDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 257 SKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWsKNWAKAAAFVTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 337 TTAQK-AVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPR 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 188219524 416 ATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPGAGRFIPR 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-475 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 565.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIVNDDQSFHADLYVEDGLIKQIGENlivpGGIKTIDAHGLMVLPGGVDVHTRLQMPVMGMTPADDFCQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 96 ALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVrDKGVNSFLVFMAYKDRCQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 176 CTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 256 MSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPINPdPTTADHLTSLLSSGDLQVTGSAHCT 335
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 336 FTTAQKA-VGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNP 414
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219524 415 RATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPGAGRFIPRKTFP 475
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-486 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 545.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 12 ITSDRLLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVMGMTPADDFCQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 92 GTKAALAGGTTMILDHVFPDAGvSLLAAYEQWRERADSAaCCDYSLHVDIPRWHESTKEELEALVRDKGVNSFLVFMAYK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAEKS-CMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 172 DRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 252 VTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGSHYWSKNWAKAAAFVTSPPINPdpttADH---LTSLLSSGDLQV 328
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP----AGHgkaLQAALSSGILQL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 329 TGSAHCTFTTAQKAVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDAD 408
Cdd:PLN02942 316 VGTDHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDAD 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219524 409 LVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPGAGRFIPRKTFPdFVYKRIKARN 486
Cdd:PLN02942 396 IIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKAD 472
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-471 |
3.68e-128 |
|
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; Dihydroorotase or related cyclic amidohydrolase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 439814 [Multi-domain] Cd Length: 439 Bit Score: 382.52 E-value: 3.68e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 18 LIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 98 AGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVrDKGVNSFLVFMAYKD-RCQC 176
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 177 TDGQIYEIFSLIRDLGAVAQVHAENGDIVEEeqkRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVM 256
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 257 SKGAADMVAQAKRRGVVVFGE--P----ITAS-LGTDGSHYwsknwakaaafVTSPPINpdptTADHLTSL---LSSGDL 326
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPLR----TEEDREALwegLADGTI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 327 QVTGSAHCTFTTAQKAvgkDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSD 406
Cdd:COG0044 300 DVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGAD 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219524 407 ADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPgAGRFIPR 471
Cdd:COG0044 376 ADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-473 |
2.71e-117 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 355.93 E-value: 2.71e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLivPGGIKTIDAHGLMVLPGGVDVHTRLQMPV-MGMTPADDFCQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 96 ALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHEST-KEELEALVRDkGVNSFLVFMAYkDRC 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 175 QCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 255 VMSKGAADMVAQAKRRGVVVFGEP------ITAS-LGTDGSHywsknwakAAAFVTSPPinpdPTTADHLTSL---LSSG 324
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPP----PRDKANQEAIwngLADG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 325 DLQVTGSAHCTF---TTAQKAVGKDN--FTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRKG 399
Cdd:PRK13404 310 TFEVFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKG 389
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219524 400 RVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPGAGRFIPRKT 473
Cdd:PRK13404 390 AIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-469 |
6.54e-64 |
|
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: 216.00 E-value: 6.54e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 97 LAGGTTMILD---HVFPDA--GVSLLAAYEQWRERadsaaccdysLHVDIPRWHESTK---EELEALVrDKGVNSFLVFM 168
Cdd:cd01315 80 AAGGITTIIDmplNSIPPTttVENLEAKLEAAQGK----------LHVDVGFWGGLVPgnlDQLRPLD-EAGVVGFKCFL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 169 A---YKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQ 245
Cdd:cd01315 149 CpsgVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 246 ANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPINpDPTTADHLT 318
Cdd:cd01315 229 TGCRLHIVHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLW 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 319 SLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRK 398
Cdd:cd01315 297 EALENGDIDMVVSDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQK 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 188219524 399 GRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPgAGRFI 469
Cdd:cd01315 377 GRIAVGYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
63-443 |
4.01e-56 |
|
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: 192.22 E-value: 4.01e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 63 LMVLPGGVDVHTRLQMPVMGMTpADDFCQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIp 142
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTY-KEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 143 rWHESTKEELEaLVRDKGVNSFLVFMAYK--DRCQCTDGQIYEIFSLIRDLGAVAQVHAEngdiveeeqkrlleqgitgp 220
Cdd:cd01302 79 -GPGDVTDELK-KLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE-------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 221 eghvlshpeeveaeavyRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDGShYWSKNWAKaaa 300
Cdd:cd01302 137 -----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW--- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 301 FVTSPPINPdPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDnFTLIPEGVNGIEERMSVVWEKcVASGKMDENEF 380
Cdd:cd01302 196 GKVNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILLTE-GVKRGLSLETL 272
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 188219524 381 VAVTSTNAAKIFNFYPrKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVP 443
Cdd:cd01302 273 VEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-469 |
1.26e-47 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 172.58 E-value: 1.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 97 LAGGTT----MILDHVFPdagVSLLAAYEQWRERADSAACCDYSLhvdiprWHESTKEELEAL--VRDKGVNSFLVFMAY 170
Cdd:PRK06189 82 AAGGCTtyfdMPLNSIPP---TVTREALDAKAELARQKSAVDFAL------WGGLVPGNLEHLreLAEAGVIGFKAFMSN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 171 K--DRCQ-CTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQAN 247
Cdd:PRK06189 153 SgtDEFRsSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 248 CPLYVTKVMSKGAADMVAQAKRRGVVV----------FGEPITASLGTdgshywsknWAKAAafvtsPPINpDPTTADHL 317
Cdd:PRK06189 233 CPLHFVHISSGKAVALIAEAKKRGVDVsvetcphyllFTEEDFERIGA---------VAKCA-----PPLR-SRSQKEEL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 318 TSLLSSGDLQVTGSAHCTFTTAQKAvgKDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFyPR 397
Cdd:PRK06189 298 WRGLLAGEIDMISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQ 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188219524 398 KGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNlLVTPGAGRFI 469
Cdd:PRK06189 375 KGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGE-VFPPPRGQLL 445
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-472 |
1.12e-46 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 169.45 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 97 LAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDI-PRWhestkEELEALVRdKGVNSF-LVFMAYKDRC 174
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVtGNW-----DPLESLWE-RGVFALgEIFMADSTGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 175 QCTDGQIY-EIFSLIRDLGAVAQVHAENGDIVEEEQKRLleQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVT 253
Cdd:PRK02382 156 MGIDEELFeEALAEAARLGVLATVHAEDEDLFDELAKLL--KGDADADAWSAYRPAAAEAAAVERALEVASETGARIHIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 254 KVMSKGAADMvaqAKRRGVVVFGEPITASLGTDgshywskNWAKAAAFV-TSPPINPDPTTaDHLTSLLSSGDLQVTGSA 332
Cdd:PRK02382 234 HISTPEGVDA---ARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRR-EALWERLNDGTIDVVASD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 333 HCTFTTAQKAVG-KDnftlIPEGVNGIEERMSVVWEKcVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVI 411
Cdd:PRK02382 303 HAPHTREEKDADiWD----APSGVPGVETMLPLLLAA-VRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLVL 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 188219524 412 WNPRATKVISAKSHNLNVEYNIFEGVEcrGV-PTVVISQGRVVLEDGNLLVTPGAGRFIPRK 472
Cdd:PRK02382 377 VDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
33-456 |
8.31e-44 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 161.07 E-value: 8.31e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 33 ADLYVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDHVFPDA 112
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPDA-EVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADMPNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 113 GVSLLAAYEQWRERADSAACCDYSLHVDIPRwHESTKEELEAlvrdkgvnSFLVFMAYKDRCQCTDG-QIYEIFSLIRDL 191
Cdd:TIGR00857 83 PIDTPETLEWKLQRLKKVSLVDVHLYGGVTQ-GNQGKELTEA--------YELKEAGAVGRMFTDDGsEVQDILSMRRAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 192 GAVAQ------VHAENGDIVEEEQKRlleQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVA 265
Cdd:TIGR00857 154 EYAAIagvpiaLHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 266 QAKRRGVvvfgePITAS------LGTDGSHYWSKNWAKaaafvTSPPINPdPTTADHLTSLLSSGDLQVTGSAHCTFTTA 339
Cdd:TIGR00857 231 KAKSQGI-----KITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHTLE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 340 QKAVgkdNFTLIPEGVNGIEERMSVVWEKCVAsGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKV 419
Cdd:TIGR00857 300 EKTK---EFAAAPPGIPGLETALPLLLQLLVK-GLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWT 374
|
410 420 430
....*....|....*....|....*....|....*..
gi 188219524 420 ISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLED 456
Cdd:TIGR00857 375 INAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
5.44e-33 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 131.09 E-value: 5.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIVN---DDQsfHADLYVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQG 92
Cdd:PRK09357 2 MILIKNGRVIDpkgLDE--VADVLIDDGKIAAIGENIEAEGA-EVIDATGLVVAPGLVDLHVHLREP--GQEDKETIETG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 93 TKAALAGG---------TTMILDhvfpDAGVsllaaYEQWRERADSAACCDysLHVDIPRWHESTKEEL---EALvRDKG 160
Cdd:PRK09357 77 SRAAAAGGfttvvampnTKPVID----TPEV-----VEYVLDRAKEAGLVD--VLPVGAITKGLAGEELtefGAL-KEAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 161 VNSFlvfmaykdrcqCTDGQIYEIFSLIRdlGAVAQVHAENGDIVE-EEQKRLLEQGITGpEGHVLSH------PEEVEA 233
Cdd:PRK09357 145 VVAF-----------SDDGIPVQDARLMR--RALEYAKALDLLIAQhCEDPSLTEGGVMN-EGEVSARlglpgiPAVAEE 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 234 EAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVvvfgePITA------------SLGTDGSHYwsKnwakaaaf 301
Cdd:PRK09357 211 VMIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY--K-------- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 302 vtsppINPdP--TTADHLTSL--LSSGDLQVTGSAHCTFTTAQKAVGkdnFTLIPEGVNGIEERMSVVWEKCVASGKMDE 377
Cdd:PRK09357 276 -----VNP-PlrTEEDREALIegLKDGTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 378 NEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPRATKVISA-----KSHNlnveyNIFEGVECRGVPTVVISQGRV 452
Cdd:PRK09357 347 EQLLEKMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGedfasKGKN-----TPFIGMKLKGKVVYTIVDGKI 419
|
....
gi 188219524 453 VLED 456
Cdd:PRK09357 420 VYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-470 |
8.34e-32 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 128.05 E-value: 8.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLivPGGIKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 97 LAGG-TTMIldhVFPDAGVSLLAAYEQWRERADSAaccDYSLHVDIPRWHESTKEELEAL--VRDKGVNSFLVFMAY--- 170
Cdd:PRK08044 81 AKGGiTTMI---EMPLNQLPATVDRASIELKFDAA---KGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcgd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 171 ----KDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQA 246
Cdd:PRK08044 155 rgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 247 NCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPINpDPTTADHLTSLLS 322
Cdd:PRK08044 235 GCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIR-DLENQKGMWEKLF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 323 SGDLQVTGSAHCTFTTAQKAvgkDNFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVA 402
Cdd:PRK08044 306 NGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 188219524 403 VGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTPGAGRFIP 470
Cdd:PRK08044 382 PGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
62-450 |
8.95e-32 |
|
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 [Multi-domain] Cd Length: 361 Bit Score: 126.29 E-value: 8.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 62 GLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILD---HVFPdagVSLLAAYEQWRERADSAACCDYSLH 138
Cdd:cd01318 1 GLLILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDmpnTKPP---TTTAEALYEKLRLAAAKSVVDYGLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 139 VDIPRwhESTKEELEALvrdkGVNSFLVFMAykdrcQCT-DGQIYE--IFSLIRDLGAVAQVHAENGDIVEEEQKRLLEQ 215
Cdd:cd01318 76 FGVTG--SEDLEELDKA----PPAGYKIFMG-----DSTgDLLDDEetLERIFAEGSVLVTFHAEDEDRLRENRKELKGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 216 GItgpegHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVV-------VFGEPITASLGTdgs 288
Cdd:cd01318 145 SA-----HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTVevtphhlFLDVEDYDRLGT--- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 289 hywsknWAKaaafvTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNftlIPEGVNGIEERMSVVWEK 368
Cdd:cd01318 217 ------LGK-----VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLTL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 369 cVASGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVIS 448
Cdd:cd01318 282 -VNKGILSLSRVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIV 359
|
..
gi 188219524 449 QG 450
Cdd:cd01318 360 RG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-444 |
2.32e-29 |
|
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: 119.65 E-value: 2.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 54 GIKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTT--MILDHVFPDagVSLLAAYEQWRERADsaa 131
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTtvVCMPNTNPV--IDNPAVVELLKNRAK--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 132 ccDYSLHVDIPrWHESTK----EELE--ALVRDKGVNSFlvfmaYKDRCQCTDGQI-YEIFSLIRDLGAVAQVHAENgdi 204
Cdd:cd01317 74 --DVGIVRVLP-IGALTKglkgEELTeiGELLEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVHPED--- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 205 veeeqKRLLEQGIT--GPEGHVL---SHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKRRGVvvfgePI 279
Cdd:cd01317 143 -----PSLAGGGVMneGKVASRLglpGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGL-----PV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 280 TASLGtdgSHYWSKNWAKAAAFVTSPPINP---DPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGkdnFTLIPEGVN 356
Cdd:cd01317 213 TAEVT---PHHLLLDDEALESYDTNAKVNPplrSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGII 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 357 GIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPrkGRVAVGSDADLVIWNPRATKVISA-----KSHNlnvey 431
Cdd:cd01317 287 GLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEetfrsKSKN----- 359
|
410
....*....|...
gi 188219524 432 NIFEGVECRGVPT 444
Cdd:cd01317 360 TPFDGQKLKGRVL 372
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
2.87e-28 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 117.71 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 97 LAGGTTMILDhvFPDAGVSLL--AAYEQWRERADSAACCDYSLHVDiprwheSTKE---ELEALVRDKGVNSFLVFMA-- 169
Cdd:PRK09060 84 VLGGVTAVFE--MPNTNPLTTtaEALADKLARARHRMHCDFAFYVG------GTRDnadELAELERLPGCAGIKVFMGss 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 170 -----YKDrcqctDGQIYEIFSLIRdlgAVAQVHAEngdivEEEqkRLLEQGITGPEGHVLSHP----EEVEAEAVYRAV 240
Cdd:PRK09060 156 tgdllVED-----DEGLRRILRNGR---RRAAFHSE-----DEY--RLRERKGLRVEGDPSSHPvwrdEEAALLATRRLV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 241 TIAKQANCPLYVTKVMSKGAADMVAQAKRRGVV--------VFGEPITASLGTdgshYWSKNwakaaafvtsPPINpDPT 312
Cdd:PRK09060 221 RLARETGRRIHVLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DAR 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 313 TADHLTSLLSSGDLQVTGSAHCTFTTAQKAvgkDNFTLIPEGVNGIEERMSVVWEKcVASGKMDENEFVAVTSTNAAKIF 392
Cdd:PRK09060 286 HRDGLWRGVRQGVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIF 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219524 393 NFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNlLVTPGAGR 467
Cdd:PRK09060 362 GI-AGKGRIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGE-LVGPPTGE 434
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-459 |
1.86e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 112.08 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 14 SDRLLIKGGKIVNDDQSF-HADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVD--VHTRlqMPvmGMTPADDFC 90
Cdd:PRK07575 2 MMSLLIRNARILLPSGELlLGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDpqVHFR--EP--GLEHKEDLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 91 QGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDiprwheSTKEELEALVRDKGVNSFLVFM-- 168
Cdd:PRK07575 78 TASRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIG------ATPDNLPELLTANPTCGIKIFMgs 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 169 AYKDRCQCTDGQIYEIFSLIRDLGAvaqVHAENGDIVEEEQKRLleQGITGPEGHVLSHPEEVEAEAVYRAVTIAKQANC 248
Cdd:PRK07575 152 SHGPLLVDEEAALERIFAEGTRLIA---VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 249 PLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLGTDgshywskNWAKAAAFV-TSPPINpDPTTADHLTSLLSSGDLQ 327
Cdd:PRK07575 227 RLHILHLSTAIEAELLRQDKPSWVTAEVTPQHLLLNTD-------AYERIGTLAqMNPPLR-SPEDNEALWQALRDGVID 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 328 VTGSAHCTFTTAQKAVGKDNftlIPEGVNGIEERMSVVWEKCVAsGKMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDA 407
Cdd:PRK07575 299 FIATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDA 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 188219524 408 DLVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNL 459
Cdd:PRK07575 374 DLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
4.78e-25 |
|
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 hydrolyses adenine to form hypoxanthine and ammonia. Adenine deaminases reaction is important for adenine utilization 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: 460401 [Multi-domain] Cd Length: 334 Bit Score: 106.05 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 64 MVLPGGVDVHTRLQMPVMGMTPADDFC------QGTKAALAGGTTMILDHVF--PDAGVSLLAAYEQWRE--RADSAACC 133
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELPLglRFLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 134 ---DYSLHVDIPRWHEStKEELEALVRDKGVNSFLVFMAYKDRcQCTDGQIYEIFSLIRDLGAVAQVHAENGDiveEEQK 210
Cdd:pfam01979 81 ldtDGELEGRKALREKL-KAGAEFIKGMADGVVFVGLAPHGAP-TFSDDELKAALEEAKKYGLPVAIHALETK---GEVE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 211 RLLEQGITGPEghVLSHPEEVEAEAVYRAVTIAKQANCPLYVTkvmskGAADMVAQAKRRGVVvfgepitasLGTDGSHY 290
Cdd:pfam01979 156 DAIAAFGGGIE--HGTHLEVAESGGLLDIIKLILAHGVHLSPT-----EANLLAEHLKGAGVA---------HCPFSNSK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 291 WSKNWAKAAAfvtsppinpdpttadhltsLLSSGDLQVTGSAHCtfttaqkaVGKDNFTLIPEGVNGIEERMsvvwekcV 370
Cdd:pfam01979 220 LRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQF-------D 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 371 ASGKMDENEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRatkvisakshnlnvEYNIFEGVECRGVPTVVISQG 450
Cdd:pfam01979 266 PEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLD--------------PLAAFFGLKPDGNVKKVIVKG 331
|
...
gi 188219524 451 RVV 453
Cdd:pfam01979 332 KIV 334
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-463 |
7.42e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 103.69 E-value: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 22 GKIVNDDQSFHADLYVEDGLIKQIGENLIvpGGIKTIDAHGLMVLPGGVDVHTRLQmpvmgmtpadDFCQ--------GT 93
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR----------DFEEsyketiesGT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 94 KAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACCDYSLHVDIprwhESTKEELEALVRDkgvnsflvfmAYKDR 173
Cdd:PRK04250 72 KAALHGGITLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLI----AGNCEKAEEIKAD----------FYKIF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 174 CQCTDGQIY-EIFSL-IRDLGAVAQVHAENGDIVEEEQKRlleqgitgpeghvlshPEEVEAEAVYRAVTIAKQANCPLY 251
Cdd:PRK04250 138 MGASTGGIFsENFEVdYACAPGIVSVHAEDPELIREFPER----------------PPEAEVVAIERALEAGKKLKKPLH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 252 VTKVMSKGAADMVAQAKRRGVVVFGEPitaslgtdgSH--YWSKNWAKAAAFVTSPPINpdptTADHLTSLLSSGD-LQV 328
Cdd:PRK04250 202 ICHISTKDGLKLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR----SEEDRKALWENFSkIPI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 329 TGSAHCTFTTAQKAVGKdnftlipEGVNGIEERMSVVWEkCVASGKMDENEFVAVTSTNAAKIFNFyPRKGrVAVGSDAD 408
Cdd:PRK04250 269 IASDHAPHTLEDKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFGI-KNYG-IEEGNYAN 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 188219524 409 LVIWNPRATKVISAKSHNLNVEYNIFEGVECRGVPTVVISQGRVVLEDGNLLVTP 463
Cdd:PRK04250 339 FAVFDMKKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-458 |
1.36e-23 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 104.47 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 12 ITSDRLLIKGGKIVNDdqsfhadLYVEDGLIKQIGENLIVPG---GIKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADD 88
Cdd:PLN02795 48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 89 FCQGTKAALAGGTTMILDhvFPDAGVSLLAAYEQWRERADSAAccdYSLHVDIPRWHESTKE------ELEALVrDKGVN 162
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVD--MPLNSFPSTTSVETLELKIEAAK---GKLYVDVGFWGGLVPEnahnasVLEELL-DAGAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 163 SFLVFM---AYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQKrlLEQGITGPEGHVLSHPEEVEAEAVYRA 239
Cdd:PLN02795 193 GLKSFMcpsGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSR--LDADPRSYSTYLKSRPPSWEQEAIRQL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 240 VTIAKQAN-------CPLYVTKVM-SKGAADMVAQAKRRGVVVFGEPITaslgtdgsHYWsknwAKAAA--------FVT 303
Cdd:PLN02795 271 LEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKC 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 304 SPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAVGKDNFTLIPEGVNGIEERMSVVWEKCVASGkMDENEFVAV 383
Cdd:PLN02795 339 APPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARW 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 384 TSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISA------KSHNLNVeyniFEGVECRGVPTVVISQGRVVLEDG 457
Cdd:PLN02795 417 WSERPAKLAGL-DSKGAIAPGKDADIVVWDPEAEFVLDEsypiyhKHKSLSP----YLGTKLSGKVIATFVRGNLVFLEG 491
|
.
gi 188219524 458 N 458
Cdd:PLN02795 492 K 492
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
37-471 |
6.32e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 101.09 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 37 VEDGLIKQIGENLivpGGIKTIDAHGLmVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILDHVFPDAGVSL 116
Cdd:PRK01211 20 VEDGKIKSIKKDA---GNIGKKELKGA-ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMDMPNNNIPIKD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 117 LAAYEQWRERADSAACCDYSLHvdiprwheSTKEELEALVRDKGVNSFLVFMAYKDRCQCTDGQIYEIfSLIRDLGAVAQ 196
Cdd:PRK01211 94 YNAFSDKLGRVAPKAYVDFSLY--------SMETGNNALILDERSIGLKVYMGGTTNTNGTDIEGGEI-KKINEANIPVF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 197 VHAENGDIVEE---EQKRLLEqgitgpegHVLSHPEEVEAEAVYRAVTIAKQANCPLYVTKVMSKGaaDMVAQAKRRGVV 273
Cdd:PRK01211 165 FHAELSECLRKhqfESKNLRD--------HDLARPIECEIKAVKYVKNLDLKTKIIAHVSSIDVIG--RFLREVTPHHLL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 274 VFGEpitASLGTDGShywsknwakaaafvTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQKAvgkdNFTLIPE 353
Cdd:PRK01211 235 LNDD---MPLGSYGK--------------VNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ----EFEYAKS 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 354 GVNGIEERMSVVWeKCVASGKMDENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNI 433
Cdd:PRK01211 293 GIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSP 369
|
410 420 430
....*....|....*....|....*....|....*...
gi 188219524 434 FEGVECRgVPTVVISQGRVVLEDGNLLVTPgAGRFIPR 471
Cdd:PRK01211 370 FNGFDAI-FPSHVIMRGEVVIDNYELISER-TGKFVPK 405
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-252 |
1.08e-15 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 79.53 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 15 DRLLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVD--VHTRlqMPvmGMTPADDFCQG 92
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR--EP--GLTHKGDIASE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 93 TKAALAGGTTMILD--HVFPDAgvSLLAAYEQWRERADSAACCDYSLHvdiprwHESTKEELEALVR-DK----GVNsfl 165
Cdd:PRK09236 78 SRAAVAGGITSFMEmpNTNPPT--TTLEALEAKYQIAAQRSLANYSFY------FGATNDNLDEIKRlDPkrvcGVK--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 166 VFMAYK------DRCQCTDgqiyEIFsliRDLGAVAQVHAENGDIVEEEQKRLLEQ-GITGPEGHvlsHPEEVEAEAVYR 238
Cdd:PRK09236 147 VFMGAStgnmlvDNPETLE----RIF---RDAPTLIATHCEDTPTIKANLAKYKEKyGDDIPAEM---HPLIRSAEACYK 216
|
250
....*....|....*...
gi 188219524 239 ----AVTIAKQANCPLYV 252
Cdd:PRK09236 217 ssslAVSLAKKHGTRLHV 234
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-288 |
1.16e-13 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 72.94 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIVNDDQSF----HADLYVEDGLIKQIGENLIVP---GGIKTIDAHGLMVLPGGVDVHTRL-QMPVMGMTPAD 87
Cdd:COG0402 1 DLLIRGAWVLTMDPAGgvleDGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLpQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 88 DFCQ--------------------GTKAA----LAGGTTMILDH--VFPDAGVSLLAAYEQWRERADSA-ACCDYSLHVD 140
Cdd:COG0402 81 PLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAEAGIRAVLGrGLMDRGFPDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 141 IPRWHESTKEELEALVRDkgvnsflVFMAYKDRCQ----------CTDGQIYEIFSLIRDLGAVAQVH-----AENGDIV 205
Cdd:COG0402 161 LREDADEGLADSERLIER-------WHGAADGRIRvalaphapytVSPELLRAAAALARELGLPLHTHlaetrDEVEWVL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 206 EEEQKR----LLEQGITGPeGHVLSH-----PEEVE--AEavyRAVTIakqANCP---LYvtkvMSKGAADmVAQAKRRG 271
Cdd:COG0402 234 ELYGKRpveyLDELGLLGP-RTLLAHcvhltDEEIAllAE---TGASV---AHCPtsnLK----LGSGIAP-VPRLLAAG 301
|
330
....*....|....*..
gi 188219524 272 VVVfgepitaSLGTDGS 288
Cdd:COG0402 302 VRV-------GLGTDGA 311
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-243 |
4.95e-13 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 70.98 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIktIDAHGLMVLPGGVDVHT----RLQMP--------VMGM 83
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVDLHTdnleKHLAPrpgvdwpaDAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 84 TPADdfcqgTKAALAGGTTMiLDHVF----PDAGV-------SLLAAYEQWRERadSAACCDYSLH--VDIPrwHESTKE 150
Cdd:PRK15446 81 AAHD-----AQLAAAGITTV-FDALSvgdeEDGGLrsrdlarKLIDAIEEARAR--GLLRADHRLHlrCELT--NPDALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 151 ELEALVRDKGVnSFLVFMaykDRcqcTDGQiyeifSLIRDLGAVAQVHAENGDIVEEEQKRLLEQGITGPEGHVLSHPEE 230
Cdd:PRK15446 151 LFEALLAHPRV-DLVSLM---DH---TPGQ-----RQFRDLEKYREYYAGKYGLSDEEFDAFVEERIALSARYAPPNRRA 218
|
250
....*....|...
gi 188219524 231 VEAEAVYRAVTIA 243
Cdd:PRK15446 219 IAALARARGIPLA 231
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
56-437 |
9.23e-12 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 67.17 E-value: 9.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 56 KTIDAHGLMVLPGGVDVHT---RLQMPVMGMTPADDFCQGTKAALAG------------------------GTTMILDHV 108
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHThldGGGLNLRELRLPDVLPNAVVKGQAGrtpkgrwlvgegwdeaqfaetrfpYALADLDEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 109 FPDAGVSLLAA--YEQWRERA--DSAaccDYSLHVDIPR----WHESTKEELEALVRDK---------------GVNSFL 165
Cdd:pfam07969 81 APDGPVLLRALhtHAAVANSAalDLA---GITKATEDPPggeiARDANGEGLTGLLREGayalppllareaeaaAVAAAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 166 VFMAyKDRCQCTDGQIYEIFSLIrDLGAVAQVHAENGDIveEEQKRLLEQGITGPEGHV-------------------LS 226
Cdd:pfam07969 158 AALP-GFGITSVDGGGGNVHSLD-DYEPLRELTAAEKLK--ELLDAPERLGLPHSIYELrigamklfadgvlgsrtaaLT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 227 HP---------EEVEAEAVYRAVTIAKQANCPLYV-----TKVMSK-GAADMVAQAK-RRGVVVFG-------------E 277
Cdd:pfam07969 234 EPyfdapgtgwPDFEDEALAELVAAARERGLDVAIhaigdATIDTAlDAFEAVAEKLgNQGRVRIEhaqgvvpytysqiE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 278 PITASLGTDGSHYWSknWAKAAAFVTSPPINPDPTTADHLTSLLSSGDLQVTGS-AHCTFTTAQKAVGkDNFTLIPEG-- 354
Cdd:pfam07969 314 RVAALGGAAGVQPVF--DPLWGDWLQDRLGAERARGLTPVKELLNAGVKVALGSdAPVGPFDPWPRIG-AAVMRQTAGgg 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 355 -VNGIEERMSVvwekcvasgkmdeNEFVAVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAKSHNLNVEYNI 433
Cdd:pfam07969 391 eVLGPDEELSL-------------EEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTV 457
|
....
gi 188219524 434 FEGV 437
Cdd:pfam07969 458 VDGR 461
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-460 |
3.62e-11 |
|
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: 65.30 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQS---FHADLYVEDGLIKQIGENLIVPGGI--KTIDAHGLMVLPGGVDVHTRLQM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAYPadEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 79 --------PVMGMTPADDFCQGTKAALA----GGTTMILDH--VFPDAgvsLLAAYEQ--WReradsaACCDYSLhVDIP 142
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMyfFYPDA---VAEAAEElgIR------AVLGRGI-MDLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 143 R-WHESTKEEL---EALVRdkgvnsflvfmAYKDRCQ--------------CTDGQIYEIFSLIRDLGAVAQVH-AENGD 203
Cdd:cd01298 151 TeDVEETEEALaeaERLIR-----------EWHGAADgrirvalaphapytCSDELLREVAELAREYGVPLHIHlAETED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 204 IVEEEQKR--------LLEQGITGPEGhVLSH-----PEEVE--AEavyRAVTIakqANCPLYVTKVMSkGAADmVAQAK 268
Cdd:cd01298 220 EVEESLEKygkrpveyLEELGLLGPDV-VLAHcvwltDEEIEllAE---TGTGV---AHNPASNMKLAS-GIAP-VPEML 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 269 RRGVVVfgepitaSLGTDGSHywSKNwakaaafvtsppiNPDPTTADHLTSLLssgdlqvtgsahctfttaQKAVGKDNF 348
Cdd:cd01298 291 EAGVNV-------GLGTDGAA--SNN-------------NLDMFEEMRLAALL------------------QKLAHGDPT 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 349 TLIPEgvngieermsvvwekcvasgkmdenEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRATKVISAKSHNLN 428
Cdd:cd01298 331 ALPAE-------------------------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISH 384
|
490 500 510
....*....|....*....|....*....|..
gi 188219524 429 VEYNIFEGVecrgVPTVVISqGRVVLEDGNLL 460
Cdd:cd01298 385 LVYSANGGD----VDTVIVN-GRVVMEDGELL 411
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-437 |
3.78e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.98 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 13 TSDRLLIKGGKIVNDDQS---FHADLYVEDGLIKQIGEN--LIVPGGIKTIDAHGLMVLPGGVDVHTRLqmpVMGMTPAD 87
Cdd:COG1228 6 QAGTLLITNATLVDGTGGgviENGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHL---GLGGGRAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 88 DFCQGT----------------KAALAGGTTMILDHVFPDAGVS------LLAAYEQWR-ERADSAACCDYSLHVDIPrw 144
Cdd:COG1228 83 EFEAGGgitptvdlvnpadkrlRRALAAGVTTVRDLPGGPLGLRdaiiagESKLLPGPRvLAAGPALSLTGGAHARGP-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 145 hestkEELEALVRD---KGVNsFLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVeeeqKRLLEQGITGPE 221
Cdd:COG1228 161 -----EEARAALREllaEGAD-YIKVFAEGGAPDFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 222 gHVLSHPEEVeaeavyravtiakqancplyvtkvmskgaadmVAQAKRRGVVVFGePiTASLGTDGSHYWSKNWAKAAAF 301
Cdd:COG1228 231 -HGTYLDDEV--------------------------------ADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 302 VtsppinpDPTTADHLTSLLSSGdlqvtgsahCTFttaqkAVGKDNFTLIPEGVNgieerMSVVWEKCVASGkMDENE-F 380
Cdd:COG1228 276 V-------REAALANARRLHDAG---------VPV-----ALGTDAGVGVPPGRS-----LHRELALAVEAG-LTPEEaL 328
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 188219524 381 VAVTStNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKVISAkshNLNVEYNIFEGV 437
Cdd:COG1228 329 RAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY---LEDVRAVMKDGR 381
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
32-424 |
7.55e-11 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 64.24 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 32 HADLYVEDGLIKQIGENLI-VPGGIKTIDAHGLMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTT--MILDHV 108
Cdd:PRK07369 21 IADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTrvAILPDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 109 FPdaGVSLLAAYEQWRERADSAAccdySLHVDIprWHESTKE-------ELEALVRdKGVNSFlvfmaykdrcqcTDGQI 181
Cdd:PRK07369 99 FP--PLDNPATLARLQQQAQQIP----PVQLHF--WGALTLGgqgkqltELAELAA-AGVVGF------------TDGQP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 182 YEIFSLIRDLGAVAQVH-------------AENGdiVEEEQKRLLEQGITGpeghvlsHPEEVEAEAVYRAVTIAKQANC 248
Cdd:PRK07369 158 LENLALLRRLLEYLKPLgkpvalwpcdrslAGNG--VMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 249 PLYVTKVMSKGAADMVAQAKRRGVvvfgePITAS-------LGT-DGSHYwSKNWAKAaafvtsPPI-NPDPTTAdhLTS 319
Cdd:PRK07369 229 PVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD------PPLgNPSDRQA--LIE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 320 LLSSGDLQVTGSAHCTFTTAQKAVGkdnFTLIPEGVNGIEERMSVVWEKCVASGKMDENEFVAVTSTNAAKIFNFYPRkg 399
Cdd:PRK07369 295 GVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP-- 369
|
410 420
....*....|....*....|....*
gi 188219524 400 RVAVGSDADLVIWNPRATKVISAKS 424
Cdd:PRK07369 370 SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-457 |
1.61e-10 |
|
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: 63.08 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVndDQS----FHADLYVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQMPVM---GMTPaddf 89
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSAR-EVIDAAGLVVAPGFIDVHTHYDGQVFwdpDLRP---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 90 cqgtkAALAGGTTMILDH-------VFPD---------AGVSLL-----------AAYEQWRERADSA--ACCDYSlHVD 140
Cdd:cd01297 75 -----SSRQGVTTVVLGNcgvspapANPDdlarlimlmEGLVALgeglpwgwatfAEYLDALEARPPAvnVAALVG-HAA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 141 IPRWH------ESTKEELEALVR--DKGVNS----FLVFMAYKDRCQCTDGQIYEIFSLIRDLGAVAQVHAENgdiveee 208
Cdd:cd01297 149 LRRAVmgldarEATEEELAKMREllREALEAgalgISTGLAYAPRLYAGTAELVALARVAARYGGVYQTHVRY------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 209 qkrlleqgitgpeghvlshPEEVEAEAVYRAVTIAKQANCPLYVT--KVMSKG-------AADMVAQAKRRGVVVfgepi 279
Cdd:cd01297 222 -------------------EGDSILEALDELLRLGRETGRPVHIShlKSAGAPnwgkidrLLALIEAARAEGLQV----- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 280 taslgtdgshywsknWAKAAAFVTSPPINPDPTTADHLTSLLSSGDLQvtGSAH----CTFT--TAQKAVGKDNFTLiPE 353
Cdd:cd01297 278 ---------------TADVYPYGAGSEDDVRRIMAHPVVMGGSDGGAL--GKPHprsyGDFTrvLGHYVRERKLLSL-EE 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 354 GVngieERMsvvwekcvasgkmdenefvavtSTNAAKIFNFYPRkGRVAVGSDADLVIWNP-----RATKVisakshNLN 428
Cdd:cd01297 340 AV----RKM----------------------TGLPARVFGLADR-GRIAPGYRADIVVFDPdtladRATFT------RPN 386
|
490 500
....*....|....*....|....*....
gi 188219524 429 VEYNifegvecrGVPTVVISqGRVVLEDG 457
Cdd:cd01297 387 QPAE--------GIEAVLVN-GVPVVRDG 406
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
63-466 |
2.43e-09 |
|
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: 59.00 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 63 LMVLPGGVDVHTRLQMPvmGMTPADDFCQGTKAALAGGTTMILdhVFPDAGVSLL--AAYEQWRERADSAACCDYSLHVD 140
Cdd:cd01316 2 TIRLPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 141 IPRWHESTKEELEalvrDKGVNSFLvfmaykdrcqctdgqiyeifslirdlgavaqvhaengdIVEEEQKRLLEQGITGP 220
Cdd:cd01316 78 ATSTNAATVGELA----SEAVGLKF--------------------------------------YLNETFSTLILDKITAW 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 221 EGHVLSHPEE----VEAEAVYRAVTI--AKQANCPLYVTKVMSKGAADMVAQAKRRGVVVFGEPITASLgtdgshYWSKN 294
Cdd:cd01316 116 ASHFNAWPSTkpivTHAKSQTLAAVLllASLHNRSIHICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQD 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 295 WAKAAAFvtspPINPDPTTADHLTSL---LSSGDLQVTGSAhcTFTTAQKAVGKdnftlIPEGVNGIEERMSVVWeKCVA 371
Cdd:cd01316 190 DLPRGQY----EVRPFLPTREDQEALwenLDYIDCFATDHA--PHTLAEKTGNK-----PPPGFPGVETSLPLLL-TAVH 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 372 SGKMDENEFVAVTSTNAAKIFNFYPRKGrVAVGSDADlVIWNPRATKVISAKShnlnveYNIFEGVECRGVPTVVISQGR 451
Cdd:cd01316 258 EGRLTIEDIVDRLHTNPKRIFNLPPQSD-TYVEVDLD-EEWTIPKNPLQSKKG------WTPFEGKKVKGKVQRVVLRGE 329
|
410
....*....|....*
gi 188219524 452 VVLEDGNLLVTPGAG 466
Cdd:cd01316 330 TAFIDGEIVAPPGFG 344
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
17-113 |
2.58e-09 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 59.41 E-value: 2.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHA--DLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRL--QMPVMGMtPADDFCqg 92
Cdd:COG3964 2 LLIKGGRVIDPANGIDGvmDIAIKDGKIAAVAKDIDAAEAKKVIDASGLYVTPGLIDLHTHVfpGGTDYGV-DPDGVG-- 78
|
90 100
....*....|....*....|.
gi 188219524 93 tkaALAGGTTMIldhvfpDAG 113
Cdd:COG3964 79 ---VRSGVTTVV------DAG 90
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-74 |
3.17e-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: 3.17e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 188219524 17 LLIKGGKIVNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHI 58
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
17-274 |
3.75e-08 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 55.95 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVN--DDQSFHADLYVEDGLIKQIGeNLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVM---GMTPadDFCQ 91
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFIDIHTHYDLQLLwdpRLEP--SLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 92 GTkaalaggTTMIL--DhvfpdaGVSLLAAYEQWRERADSAACCDYSLHVDIPRWHESTKEELEALVRDK-GVN-SFLV- 166
Cdd:COG3653 81 GV-------TTVVMgnC------GVSFAPVRPEDRDRLIDLMEGVEGIPEGLDWDWESFGEYLDALERRGlGVNvASLVg 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 167 -------FMAYKDRcQCTDGQIYEIFSLIR---DLGAV---------AQVHAEngdivEEEQKRLLEqgITGPEGHVL-S 226
Cdd:COG3653 148 hgtlrayVMGLDDR-PPTPEELARMRALLReamEAGALglstgliyvPGTYAS-----TDELVALAK--VVAEYGGVYqS 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 227 HPEEVEA---EAVYRAVTIAKQANCPLYVT--KVMSK-------GAADMVAQAKRRGVVV 274
Cdd:COG3653 220 HMRDEGDgllEAVDELIRIGREAGVPVHIShlKAAGKpnwgkadEVLALIEAARAEGLDV 279
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
62-466 |
6.79e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 54.77 E-value: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 62 GLMVLPGGVDVHTRLQMpvMGMTPADDFCQGTKAALAGGTTMILDhvFPDAgVSLLAAYEQWRERADSAAC---CDYSLH 138
Cdd:PRK00369 42 GTLILPGAIDLHVHLRG--LKLSYKEDVASGTSEAAYGGVTLVAD--MPNT-IPPLNTPEAITEKLAELEYysrVDYFVY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 139 VDIPRwhesTKEELEALvrdkGVNSFLVFMAykdrcqctdgqiyeifslirdlgavaqvhaengDIVEEEQKRLLEqgit 218
Cdd:PRK00369 117 SGVTK----DPEKVDKL----PIAGYKIFPE---------------------------------DLEREETFRVLL---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 219 gpEGHVLS--HPEEVEAEAVYRAVtiakQANCPLYVTKVMS-KGAADM----------VAQAKRRGvvvFGEPITAS-LG 284
Cdd:PRK00369 152 --KSRKLKilHPEVPLALKSNRKL----RRNCWYEIAALYYvKDYQNVhithasnprtVRLAKELG---FTVDITPHhLL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 285 TDG-SHYWSKnwakaaafvTSPPINpDPTTADHLTSLLSSGDLQVtgSAHCTFTTAQKavgKDNFTLIPEGVNGIEERMS 363
Cdd:PRK00369 223 VNGeKDCLTK---------VNPPIR-DINERLWLLQALSEVDAIA--SDHAPHSSFEK---LQPYEVCPPGIAALSFTPP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 364 VVWeKCVASGKMDENEFVAVTSTNAAKIFNFypRKGRVAVGSDADLVIWNPRATKVISAKShnlNVEYNIFEGVECRGVP 443
Cdd:PRK00369 288 FIY-TLVSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWRYSTKYS---KVIETPLDGFELKASV 361
|
410 420
....*....|....*....|...
gi 188219524 444 TVVISQGRVVLEDGNllVTPGAG 466
Cdd:PRK00369 362 YATIVQGKLAYLEGE--VFPVKG 382
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-102 |
7.19e-08 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 55.07 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIVN-----DDQsfhADLYVEDGLIKQIGEnliVPGGI---KTIDAHGLMVLPGGVDVHTRLQMPvmGMTPAD 87
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90
....*....|....*
gi 188219524 88 DFCQGTKAALAGGTT 102
Cdd:PRK07627 74 TLESEMAAAVAGGVT 88
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-74 |
1.41e-07 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 53.70 E-value: 1.41e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVNDDQSFHA--DLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHV 60
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-471 |
2.56e-07 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 53.55 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIVNDDQSFHA--DLYVEDGLIKQIGENLIvpGGIKTIDAHGLMVLPGGVDVHTRlqmpvmGMTPADDFCQgt 93
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH------GQSVAAYRMQ-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 94 kaALAGGTTMiLDHvfpDAGVSLLAAYEQWRER-----------------------ADSAACCDYSLH-VDIPRWHE--S 147
Cdd:PRK09061 90 --AFDGVTTA-LEL---EAGVLPVARWYAEQAGegrplnygasvgwtpariavltgPQAEGTIADFGKaLGDPRWQEraA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 148 TKEELEALVR------DKGVNSFLVFMAYKDrcQCTDGQIYEIFSLIRDLGAVAQVHAENGDIVEeeqkrlleqgitgPE 221
Cdd:PRK09061 164 TPAELAEILElleqglDEGALGIGIGAGYAP--GTGHKEYLELARLAARAGVPTYTHVRYLSNVD-------------PR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 222 GHVlshpeeveaEAVYRAVTIAKQANCPLYVTKVMSKG------AADMVAQAKRRGVVVFGE--PITASLGTDGSHYWSK 293
Cdd:PRK09061 229 SSV---------DAYQELIAAAAETGAHMHICHVNSTSlrdidrCLALVEKAQAQGLDVTTEayPYGAGSTVVGAAFFDP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 294 NWAK---------------------------------AAAFVTSPPINpDPTTADHLTSLLSSGDLQVTGSAHCTFTTAQ 340
Cdd:PRK09061 300 GWLErmglgygslqwvetgerlltreelaklrandpgGLVLIHFLDED-NPRDRALLDRSVLFPGAAIASDAMPWTWSDG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 341 KAVGKDNFTLIPEGV-----NG---------IEERMSVVWEKCVAsgKMdenefvavtSTNAAKIF-NFYP---RKGRVA 402
Cdd:PRK09061 379 TVYEGDAWPLPEDAVshprsAGtfarflreyVRERKALSLLEAIR--KC---------TLMPAQILeDSVPamrRKGRLQ 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 188219524 403 VGSDADLVIWNP-----RATKVISAK-SHnlnveynifegvecrGVPTVVISqGRVVLEDGNLLVTPGAGRFIPR 471
Cdd:PRK09061 448 AGADADIVVFDPetitdRATFEDPNRpSE---------------GVRHVLVN-GVPVVSNGELVRDARPGRPVRR 506
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-74 |
6.45e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 51.64 E-value: 6.45e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 188219524 18 LIKGGKIVNDDQSFH-ADLYVEDGLIKQIGENliVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
16-459 |
7.14e-07 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 51.92 E-value: 7.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIVNDDQS---FHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLqMPVMGMTPADDF--- 89
Cdd:PRK07228 2 TILIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHL-CQTLFRGIADDLell 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 90 -----------------------CQGTKAALAGGTTMILDHVFPDAGVSLLAAYEQWRERADSAACC-DYSlhVDIPR-W 144
Cdd:PRK07228 81 dwlkdriwpleaahdaesmyysaLLGIGELIESGTTTIVDMESVHHTDSAFEAAGESGIRAVLGKVMmDYG--DDVPEgL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 145 HESTKEELEALVRDK----GVNSFLVFMAYKDR--CQCTDGQIYEIFSLIRDLGAVAQVHA-ENGD---IVEEEQKR--- 211
Cdd:PRK07228 159 QEDTEASLAESVRLLekwhGADNGRIRYAFTPRfaVSCTEELLRGVRDLADEYGVRIHTHAsENRGeieTVEEETGMrni 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 212 --LLEQGITGpEGHVLSH---PEEVEAEAVyrAVTIAKQANCPLYVTKVMSkGAADmVAQAKRRGVVVfgepitaSLGTD 286
Cdd:PRK07228 239 hyLDEVGLTG-EDLILAHcvwLDEEEREIL--AETGTHVTHCPSSNLKLAS-GIAP-VPDLLERGINV-------ALGAD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 287 GshywsknwakaaafvtsPPINP--DPTTADHLTSLLssgdlqvtgsahctfttaQKAVGKDNfTLIPegvngieerMSV 364
Cdd:PRK07228 307 G-----------------APCNNtlDPFTEMRQAALI------------------QKVDRLGP-TAMP---------ART 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 365 VWEkcvasgkmdenefvaVTSTNAAKIFNFYPRKGRVAVGSDADLVIWNPRATKviSAKSHNLNVEYNIFEGVECRGVPT 444
Cdd:PRK07228 342 VFE---------------MATLGGAKAAGFEDEIGSLEEGKKADLAILDLDGLH--ATPSHGVDVLSHLVYAAHGSDVET 404
|
490
....*....|....*
gi 188219524 445 VVISqGRVVLEDGNL 459
Cdd:PRK07228 405 TMVD-GKIVMEDGEL 418
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-74 |
1.34e-06 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 50.96 E-value: 1.34e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219524 17 LLIKGGKI------VNDDQsfhADLYVEDGlikQIGENLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHT 60
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-426 |
1.91e-06 |
|
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: 50.02 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 34 DLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRL--QMPVMGMTPadDFCqgtkAALAGGTTMIldhvfpD 111
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVyqGGTRYGDRP--DMI----GVKSGVTTVV------D 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 112 AGvsllaayeqwreradSAACCDyslhVDIPRWH--ESTKEELEALvrdkgVNSFLVFMAYKDrcqctdgQIYEIFSLir 189
Cdd:cd01307 69 AG---------------SAGADN----IDGFRYTviERSATRVYAF-----LNISRVGLVAQD-------ELPDPDNI-- 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 190 DLGAVAQVHAENGDIVEEEQKRlLEQGITGPEGhvlshpeeveAEAVYRAVTIAKQANCPLYVTKVMSKGAADMVAQAKR 269
Cdd:cd01307 116 DEDAVVAAAREYPDVIVGLKAR-ASKSVVGEWG----------IKPLELAKKIAKEADLPLMVHIGSPPPILDEVVPLLR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 270 RGVVVfgepitaslgtdgSHYWSknwAKAAAFVtsppiNPDPTTADHLTSLLSSG---DLQvTGSAHCTFTTAQKAVGKD 346
Cdd:cd01307 185 RGDVL-------------THCFN---GKPNGIV-----DEEGEVLPLVRRARERGvifDVG-HGTASFSFRVARAAIAAG 242
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 347 nftLIPE----------GVNGIEERMSVVWEKCVASGkMDENEFVAVTSTNAAKIFNFyPRKGRVAVGSDADLVIWNPRA 416
Cdd:cd01307 243 ---LLPDtissdihgrnRTNGPVYALATTLSKLLALG-MPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDLKD 317
|
410
....*....|
gi 188219524 417 TKVISAKSHN 426
Cdd:cd01307 318 GRVELVDSEG 327
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-128 |
2.17e-06 |
|
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: 50.32 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 12 ITSDRLLIKGGKIVnddqsfhaDLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRL-QMPVMGMTPADDFC 90
Cdd:cd01293 2 LRNARLADGGTALV--------DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHIHLdKTFTGGRWPNNSGG 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 91 QGTKA--------------------------ALAGGTTMILDHV--FPDAGV----SLLAAYEQWRERAD 128
Cdd:cd01293 74 TLLEAiiaweerkllltaedvkeraeralelAIAHGTTAIRTHVdvDPAAGLkaleALLELREEWADLID 143
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-228 |
4.18e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 49.23 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 15 DRLLIKGGKIVNDDQSFH----ADLYVEDGLIKQIGENlIVPGGIKTIDAHGLMVLPGGVDVHTRL-QMPVMGM------ 83
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIGdlprGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHRHTwQSVLRGIgadwtl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 84 ---------------TPADDFCQ---GTKAALAGGTTMILD--HV-----FPDAGVSLLAayeqwreRADSAACCDYSLH 138
Cdd:PRK08204 81 qtyfreihgnlgpmfRPEDVYIAnllGALEALDAGVTTLLDwsHInnspeHADAAIRGLA-------EAGIRAVFAHGSP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 139 VDIPRWHEST----KEELEAlVRDKGVNS--FLVFMAYKDRCQ--CTDGQIYEIFSLIRDLGAVAQVHAENGDIVEEEQ- 209
Cdd:PRK08204 154 GPSPYWPFDSvphpREDIRR-VKKRYFSSddGLLTLGLAIRGPefSSWEVARADFRLARELGLPISMHQGFGPWGATPRg 232
|
250 260
....*....|....*....|
gi 188219524 210 -KRLLEQGITGPeGHVLSHP 228
Cdd:PRK08204 233 vEQLHDAGLLGP-DLNLVHG 251
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
33-128 |
3.32e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 46.46 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 33 ADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVMGM--------------------------TPA 86
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTFWGDpwypnepgpslrerianerrrraasgHPA 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 188219524 87 DDfcQGTK---AALAGGTTMILDHVFPDAGVSL------LAAYEQWRERAD 128
Cdd:PRK05985 97 AE--RALAlarAAAAAGTTAMRSHVDVDPDAGLrhleavLAARETLRGLID 145
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
25-126 |
2.62e-04 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 43.82 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 25 VNDDQSFHADLYVEDGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQ---------------MPVMGMTPAD-- 87
Cdd:PRK07583 33 DTLEGLVLVDIEIADGKIAAILPAGGAPDELPAVDLKGRMVWPCFVDMHTHLDkghiwprspnpdgtfPGALDAVTADre 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 188219524 88 ------------DFcqGTKAALAGGTTMI---LDHVFPDAGVSlLAAYEQWRER 126
Cdd:PRK07583 113 ahwsaedlyrrmEF--GLRCAYAHGTSAIrthLDSFAPQAAIS-WEVFAELREA 163
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
33-140 |
3.27e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 43.54 E-value: 3.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 33 ADLYVEDGLIKQIG------------ENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvmgmtpaddfcQGTKAALAGG 100
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSA-----------QLVDHALASG 155
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188219524 101 -TTMILDHVFPDAGVS---------LLAAYEQW--------RERADS---------AACCDYSLHVD 140
Cdd:PRK13308 156 iTTMLGGGLGPTVGIDsggpfntgrMLQAAEAWpvnfgflgRGNSSKpaalieqveAGACGLKIHED 222
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
17-74 |
4.45e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 42.86 E-value: 4.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219524 17 LLIKGGKI--VNDDQSFHADLYVEDGLIKQIGEN----LIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:COG1574 10 LLLTNGRIytMDPAQPVAEAVAVRDGRIVAVGSDaevrALAGPATEVIDLGGKTVLPGFIDAHV 73
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-102 |
6.33e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 42.39 E-value: 6.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 17 LLIKGGKIVN--DDQSFHADLYVEDGLIKQIGEnlIVPGGIKTIDAHGLMVLPGGVDVHTRL--QMpvmgMTPAdDFCqg 92
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHIesSM----VTPA-EFA-- 77
|
90
....*....|
gi 188219524 93 tKAALAGGTT 102
Cdd:COG1001 78 -RAVLPHGTT 86
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
19-74 |
6.38e-04 |
|
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 [Multi-domain] Cd Length: 541 Bit Score: 42.40 E-value: 6.38e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 188219524 19 IKGGKIVNDDQSFHA---DLYVEDGlikQIGENLIVPGGIKTIDAHGLMVLPGGVDVHT 74
Cdd:cd01304 1 IKNGTVYDPLNGINGekmDIFIRDG---KIVESSSGAKPAKVIDASGKVVMAGGVDMHS 56
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-78 |
1.02e-03 |
|
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: 41.53 E-value: 1.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 188219524 39 DGLIKQIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQM 78
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSHLGL 40
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-78 |
1.06e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 41.71 E-value: 1.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 188219524 17 LLIKGGKIVNDD--QSFHADLYVEDGLIKQIGENLIVPGGiKTIDAHGLMVLPGGVDVHTRLQM 78
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
17-88 |
1.31e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 41.41 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 188219524 17 LLIKGGKIVNDDQS---FHADLYVEDGLIKQIGEnlIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPVM-GMtpADD 88
Cdd:PRK06380 3 ILIKNAWIVTQNEKreiLQGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTASkGL--FDD 74
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
368-413 |
1.34e-03 |
|
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: 41.14 E-value: 1.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 188219524 368 KCVASGKMDENEFVAVTStNAAKIFNFYPRKGRVAVGSDADLVIWN 413
Cdd:cd01309 294 KAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-119 |
2.11e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.61 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 16 RLLIKGGKIV---NDDQSFHAD--LYVEDGLIKQIGENLIVPGGI-KTIDAHGLMVLPGGVDVH-------TRLQMPVM- 81
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQPAdEVFDARGHVVTPGLVNTHhhfyqtlTRALPAAQd 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 188219524 82 ---------------GMTPaDDFCQGTKAALA----GGTTMILDH--VFPDAGVSLLAA 119
Cdd:PRK08203 82 aelfpwlttlypvwaRLTP-EMVRVATQTALAelllSGCTTSSDHhyLFPNGLRDALDD 139
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
17-89 |
3.59e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 40.12 E-value: 3.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 188219524 17 LLIKGGKIVNDDQS--FHADLYVEDGLIKQIGENliVPGGIKT-IDAHGLMVLPGGVDVHTRLQMPVM-GMtpADDF 89
Cdd:PRK06038 4 IIIKNAYVLTMDAGdlKKGSVVIEDGTITEVSES--TPGDADTvIDAKGSVVMPGLVNTHTHAAMTLFrGY--ADDL 76
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
19-113 |
6.84e-03 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 39.11 E-value: 6.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 188219524 19 IKGGKIVNDDQSFHADLyvEDGlikqIGENLIVPGGIKTIDAHGLMVLPGGVDVHTRLQMPvmgmtpaddfcQGTKAALA 98
Cdd:PRK13985 87 IKDGKIAGIGKGGNKDM--QDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISP-----------QQIPTAFA 149
|
90
....*....|....*.
gi 188219524 99 GG-TTMILDHVFPDAG 113
Cdd:PRK13985 150 SGvTTMIGGGTGPADG 165
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
17-74 |
8.23e-03 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 38.76 E-value: 8.23e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 188219524 17 LLIKGGKIVNDDQSFH----ADLYVEDGLIKQIGENlivpGGIKT-------IDAHGLMVLPGGVDVHT 74
Cdd:PRK07203 2 LLIGNGTAITRDPAKPviedGAIAIEGNVIVEIGTT----DELKAkypdaefIDAKGKLIMPGLINSHN 66
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-76 |
8.76e-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: 8.76e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 188219524 35 LYVEDGLIKQIGE----NLIVPGGIKTIDAHGLMVLPGGVDVHTRL 76
Cdd:cd01296 1 IAIRDGRIAAVGPaaslPAPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| |
