|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
10-459 |
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: 626.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAA 89
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 90 LVGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGITWWAPKVKAEMETLVrEKGVNSFQMFMTYKDLYML 169
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 170 RDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 250 SISAGDVIAAAKMQGKVVLAETTNAHATLTGlHYYHQDWSHAAAYVTVPPLRLDTnTSTYLMSLLANDTLNIVASDHRPF 329
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDD-SDYWKDWFEGAKYVCSPPLRPKE-DQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 330 TTKQKAMGKEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVVWDPEA 409
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 12746424 410 TKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTG 459
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
9-463 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 547.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 9 RILIKGGKVVNDDCTHEADVYIESGIIQQVGRelmiPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKA 88
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGA----NLGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 89 ALVGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGITWWAPKVKAEMETLVREkGVNSFQMFMTYKDLYM 168
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 169 LRDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLVNV 248
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 249 SSISAGDVIAAAKMQGKVVLAETTNAHATLTGLHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRP 328
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLR-DKEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 329 FTTKQKAM-GKEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVVWDP 407
Cdd:PRK08323 316 FCFEQKKQlGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 12746424 408 EATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCP 463
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLK 451
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
10-463 |
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: 544.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAA 89
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 90 LVGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGITWWAPKVKAEMETLVREKGVNSFQMFMTYKDLYML 169
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 170 RDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 250 SISAGDVIAAAKMQGKVVLAETTNAHATLTGlHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRPF 329
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDD-THYDKPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 330 -TTKQKAMGKEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVVWDPE 408
Cdd:TIGR02033 319 nFAQKKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 12746424 409 ATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCP 463
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVK 453
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
7-468 |
3.85e-172 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 496.29 E-value: 3.85e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 7 SVRILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGT 86
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 87 KAALVGGTTMIIGHVLPdKETSLVEAYEKCRALADpKVCCDYALHVGITWWAPKVKAEMETLVREKGVNSFQMFMTYKDL 166
Cdd:PLN02942 84 AAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 167 YMLRDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLV 246
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 247 NVSSISAGDVIAAAKMQGKVVLAETTNAHATLTGLHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDH 326
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIR-PAGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 327 RPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVVWD 406
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12746424 407 PEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCPLRSFP 468
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
11-461 |
4.45e-127 |
|
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: 379.44 E-value: 4.45e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 11 LIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTKAAL 90
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 91 VGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGITWWAPKVKAEMETLVrEKGVNSFQMFMTYKD-LYML 169
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 170 RDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEAldlGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNE---GKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 250 SISAGDVIAAAKMQGKVVLAETTNAHATLTGLHYYHQDwshaAAYVTVPPLRLDTNTSTyLMSLLANDTLNIVASDHRPF 329
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYG----TNFKVNPPLRTEEDREA-LWEGLADGTIDVIATDHAPH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 330 TTKQKAmgkEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLyPRKGRIIPGADADVVVWDPEA 409
Cdd:COG0044 310 TLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 12746424 410 TKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFmCAEGTGKF 461
Cdd:COG0044 386 EWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRF 436
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
12-469 |
1.87e-116 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 353.62 E-value: 1.87e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 12 IKGGKVVNDDCTHEADVYIESGIIQQVGRELmiPGGAKVIDATGKLVIPGGIDTSTHFHQ-TFMNATCVDDFYHGTKAAL 90
Cdd:PRK13404 8 IRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQpSGDGIMMADDFYTGTVSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 91 VGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGITWWAPKV-KAEMETLVREkGVNSFQMFMTYKDLyML 169
Cdd:PRK13404 86 FGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL-KL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 170 RDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:PRK13404 164 DDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 250 SISAGDVIAAAKMQGKVVLAETTNAHATLTGlHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRPF 329
Cdd:PRK13404 244 GREAAEQIRRARGRGLKIFAETCPQYLFLTA-EDLDRPGMEGAKYICSPPPR-DKANQEAIWNGLADGTFEVFSSDHAPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 330 ---TTKQKAMGKED--FTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVV 404
Cdd:PRK13404 322 rfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAI 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12746424 405 WDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCPlRSFPD 469
Cdd:PRK13404 402 WDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLA-RSLPD 465
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
11-450 |
2.79e-71 |
|
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: 235.26 E-value: 2.79e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 11 LIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAAL 90
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINE--PGRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 91 VGGTTMIIGHVL---PdkETSLVEAYEKCRALADPKVCCDYALHVGITwwaPKVKAEMETLVrEKGVNSFQMFMT---YK 164
Cdd:cd01315 81 AGGITTIIDMPLnsiP--PTTTVENLEAKLEAAQGKLHVDVGFWGGLV---PGNLDQLRPLD-EAGVVGFKCFLCpsgVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 165 DLYMLRDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIY 244
Cdd:cd01315 155 EFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 245 LVNVSSISAGDVIAAAKMQGKVVLAETTNAHATLTglhyyHQDWSHAAAYVTV-PPLRLDTNTSTyLMSLLANDTLNIVA 323
Cdd:cd01315 235 IVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFT-----AEDVPDGGTEFKCaPPIRDAANQEQ-LWEALENGDIDMVV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 324 SDHRPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVV 403
Cdd:cd01315 309 SDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 12746424 404 VWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENG 450
Cdd:cd01315 389 VWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
56-439 |
2.91e-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: 2.91e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 56 KLVIPGGIDTstHFHQTFMNATCV-DDFYHGTKAALVGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGI 134
Cdd:cd01302 1 LLVLPGFIDI--HVHLRDPGGTTYkEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 135 TwwaPKVKAEMETLVREKGVNSFQMFMTYK--DLYMLRDSELYQVFHACRDIGAIPRVHAEngelvaegakealdlgitg 212
Cdd:cd01302 79 G---PGDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 213 pegieishpeeleaeathRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTNAHatltgLHYYHQDWSHAA 292
Cdd:cd01302 137 ------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHH-----LFLDESMLRLNG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 293 AYVTV-PPLRlDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKAMGKeDFTKIPHGVSGVQDRMSVVWERGVVGGkMDEN 371
Cdd:cd01302 194 AWGKVnPPLR-SKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPILLTEGVKRG-LSLE 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12746424 372 RFVAVTSSNAAKILNLYPrKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVT 439
Cdd:cd01302 271 TLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
10-465 |
7.93e-54 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 188.71 E-value: 7.93e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAA 89
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFRE--PGYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 90 LVGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGIT-WWAPkvkaeMETLVREkGVNSF-QMFMTYKDLY 167
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgNWDP-----LESLWER-GVFALgEIFMADSTGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 168 MLRDSELY-QVFHACRDIGAIPRVHAENGELVAEGAKEaLDlGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLV 246
Cdd:PRK02382 156 MGIDEELFeEALAEAARLGVLATVHAEDEDLFDELAKL-LK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIHIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 247 NVSSISAGDVIAAAKMQgkvvlAETTNAHATLTglhyyHQDWSHAAAYVTV-PPLRLDTNTSTyLMSLLANDTLNIVASD 325
Cdd:PRK02382 234 HISTPEGVDAARREGIT-----CEVTPHHLFLS-----RRDWERLGTFGKMnPPLRSEKRREA-LWERLNDGTIDVVASD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 326 HRPFTTKQKAMgkeDFTKIPHGVSGVQDRMSVVWErGVVGGKMDENRFVAVTSSNAAKILNLyPRKGRIIPGADADVVVW 405
Cdd:PRK02382 303 HAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLVLV 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12746424 406 DPEATKTISASTQVQGGDFNLYENMRchGV-PLVTISRGRVVYENGVFMCAEGTGKFCPLR 465
Cdd:PRK02382 378 DPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
10-452 |
1.98e-53 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 187.99 E-value: 1.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGgAKVIDATGKLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKAA 89
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPA-REIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 90 LVGGTT----MIIGHVLPdkeTSLVEAYEKCRALADPKVCCDYALHVGITwwaPKVKAEMETLVrEKGVNSFQMFMTYKD 165
Cdd:PRK06189 82 AAGGCTtyfdMPLNSIPP---TVTREALDAKAELARQKSAVDFALWGGLV---PGNLEHLRELA-EAGVIGFKAFMSNSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 166 LYMLR---DSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIANRTHCP 242
Cdd:PRK06189 155 TDEFRssdDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 243 IYLVNVSSISAGDVIAAAKMQGKVVLAETTNAHatltgLHYYHQDWSH-AAAYVTVPPLRlDTNTSTYLMSLLANDTLNI 321
Cdd:PRK06189 235 LHFVHISSGKAVALIAEAKKRGVDVSVETCPHY-----LLFTEEDFERiGAVAKCAPPLR-SRSQKEELWRGLLAGEIDM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 322 VASDHRPFTTKQKAmgKEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLyPRKGRIIPGADAD 401
Cdd:PRK06189 309 ISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADAD 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 12746424 402 VVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVF 452
Cdd:PRK06189 386 FVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV 436
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
47-439 |
1.55e-41 |
|
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: 153.55 E-value: 1.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 47 GAKVIDATGKLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKAALVGGTTMIIghVLPDKETSL--VEAYEKCRALADPK- 123
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPNTNPVIdnPAVVELLKNRAKDVg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 124 VCCDY---ALHVGItwwAPKVKAEMETLvREKGVNSFQmfmtyKDLYMLRDSELyqVFHAC---RDIGAIPRVHAENGEL 197
Cdd:cd01317 77 IVRVLpigALTKGL---KGEELTEIGEL-LEAGAVGFS-----DDGKPIQDAEL--LRRALeyaAMLDLPIIVHPEDPSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 198 VAEGA----KEALDLGITGpegieisHPEELEAEATHRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTN 273
Cdd:cd01317 146 AGGGVmnegKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 274 AHATLTGLHYYHQDwshAAAYVTvPPLRLDTNTStYLMSLLANDTLNIVASDHRPFTTKQKamgKEDFTKIPHGVSGVQD 353
Cdd:cd01317 219 HHLLLDDEALESYD---TNAKVN-PPLRSEEDRE-ALIEALKDGTIDAIASDHAPHTDEEK---DLPFAEAPPGIIGLET 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 354 RMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPrkGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCH 433
Cdd:cd01317 291 ALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLK 368
|
....*.
gi 12746424 434 GVPLVT 439
Cdd:cd01317 369 GRVLAT 374
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
11-450 |
3.42e-37 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 143.14 E-value: 3.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 11 LIKGGKVVNDDCTHEADVYIESGIIQQVGrELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTKAAL 90
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGL--EHKEDLETGSRAAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 91 VGGTTMIIGhvLPDKE--TSLVEAYEKCRALADPKVCCDYALHVGITwwaPKVKAEMETLVREKGVNSFQMFM--TYKDL 166
Cdd:PRK09060 85 LGGVTAVFE--MPNTNplTTTAEALADKLARARHRMHCDFAFYVGGT---RDNADELAELERLPGCAGIKVFMgsSTGDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 167 YMLRDSELYQVFHACRDIGAiprVHAENGELVAEGAKEALdlgitgpEGIEISHP----EELEAEATHRVITIANRTHCP 242
Cdd:PRK09060 160 LVEDDEGLRRILRNGRRRAA---FHSEDEYRLRERKGLRV-------EGDPSSHPvwrdEEAALLATRRLVRLARETGRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 243 IYLVNVSSISAGDVIAAAKmqgKVVLAETTNAHATLTGLHYYHQDWSHAaayVTVPPLRlDTNTSTYLMSLLANDTLNIV 322
Cdd:PRK09060 230 IHVLHVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVDVL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 323 ASDHRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVVWERgVVGGKMDENRFVAVTSSNAAKILNLyPRKGRIIPGADADV 402
Cdd:PRK09060 303 GSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADF 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 12746424 403 VVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENG 450
Cdd:PRK09060 378 TIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDG 425
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
55-443 |
1.58e-36 |
|
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: 139.39 E-value: 1.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 55 GKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAALVGGTTMIIGhvLPDKE--TSLVEAYEKCRALADPKVCCDYALHV 132
Cdd:cd01318 1 GLLILPGVIDIHVHFRE--PGLTYKEDFVSGSRAAAAGGVTTVMD--MPNTKppTTTAEALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 133 GITwwaPKVKAEMetlVREKGVNSFQMFMTYKDLYMLRDSElyqvfHACRDIGAIPR---VHAENGELVAEGAKEALDLG 209
Cdd:cd01318 77 GVT---GSEDLEE---LDKAPPAGYKIFMGDSTGDLLDDEE-----TLERIFAEGSVlvtFHAEDEDRLRENRKELKGES 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 210 ItgpegIEISHPEELEAEATHRVITIANRTHCPIYLVNVSSisaGDVIAAAKMQGKVVLAETTNAHATLTglhyyHQDWS 289
Cdd:cd01318 146 A-----HPRIRDAEAAAVATARALKLARRHGARLHICHVST---PEELKLIKKAKPGVTVEVTPHHLFLD-----VEDYD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 290 HAAAYVTV-PPLRlDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKAMGKEDftkIPHGVSGVQDRMSVV---WERGVVG 365
Cdd:cd01318 213 RLGTLGKVnPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILS 288
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12746424 366 GKmdenRFVAVTSSNAAKILNLyPRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRG 443
Cdd:cd01318 289 LS----RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
9-449 |
3.66e-36 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 139.95 E-value: 3.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 9 RILIKGGKVVNDDCTHE-ADVYIESGIIQQVGRELmIPGGAKVIDATGKLVIPGGIDTSTHF------HQtfmnatcvDD 81
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENI-EAEGAEVIDATGLVVAPGLVDLHVHLrepgqeDK--------ET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 82 FYHGTKAALVGGTTMIigHVLPDkeTSLV----EAYEKCRALADPKVCCDY----ALHVGItwwAPKVKAEMETLvREKG 153
Cdd:PRK09357 73 IETGSRAAAAGGFTTV--VAMPN--TKPVidtpEVVEYVLDRAKEAGLVDVlpvgAITKGL---AGEELTEFGAL-KEAG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 154 VnsfQMF------MTYKDLyMLRDSEL---YQVFHAcrdigaiprVHAE-----NGELVAEGAKEALdLGITG-PEgiei 218
Cdd:PRK09357 145 V---VAFsddgipVQDARL-MRRALEYakaLDLLIA---------QHCEdpsltEGGVMNEGEVSAR-LGLPGiPA---- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 219 shpeelEAEATH--RVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTNAHATLTglhyyHQDWSHAAAYVT 296
Cdd:PRK09357 207 ------VAEEVMiaRDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLT-----DEDLLTYDPNYK 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 297 V-PPLRLDTNTSTyLMSLLANDTLNIVASDHRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVA 375
Cdd:PRK09357 276 VnPPLRTEEDREA-LIEGLKDGTIDAIATDHAPHAREEKE---CEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLE 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12746424 376 VTSSNAAKILNLYPrkGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYEN 449
Cdd:PRK09357 352 KMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PLN02795 |
PLN02795 |
allantoinase |
15-450 |
9.97e-31 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 125.66 E-value: 9.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 15 GKVVNDDCTHEADVYIESGIIQQVGRELMIPG---GAKVIDATGKLVIPGGIDTstHFHQTFMNATCVDDFYHGTKAALV 91
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDV--HVHLNEPGRTEWEGFPTGTKAAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 92 GGTTMIIGHVL-PDKETSLVEAYEKCRALADPKvccdyaLHVGITWWAPKV------KAEMETLVrEKGVNSFQMFMT-- 162
Cdd:PLN02795 129 GGITTLVDMPLnSFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVpenahnASVLEELL-DAGALGLKSFMCps 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 163 -YKDLYMLRDSELYQVFHACRDIGAIPRVHAENGELVAEGAKEALDLgiTGPEGIEISHPEELEAEATHRVITIANRTH- 240
Cdd:PLN02795 202 gINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAIRQLLEVAKDTRp 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 241 ------CPIYLVNVS-SISAGDVIAAAKMQGKVVLAETTNahatltglHYYhqdwSHAAA--------YVTVPPLRLDTN 305
Cdd:PLN02795 280 ggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKCAPPIRDAAN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 306 TSTyLMSLLANDTLNIVASDHRPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVVWERGVVGGkMDENRFVAVTSSNAAKIL 385
Cdd:PLN02795 348 REL-LWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLA 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12746424 386 NLyPRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNL--YENMRCHGVPLVTISRGRVVYENG 450
Cdd:PLN02795 426 GL-DSKGAIAPGKDADIVVWDPEAEFVLDESYPIYHKHKSLspYLGTKLSGKVIATFVRGNLVFLEG 491
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
10-463 |
7.97e-30 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 122.27 E-value: 7.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELmiPGGAKVIDATGKLVIPGGIDTstHFHQTFMNATCVDDFYHGTKAA 89
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDA--HTHISEPGRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 90 LVGGTTMIIGHVLPD-----KETSLVEAYEKcralADPKVCCDYALHVGITWWAPKVKAEMEtlvrEKGVNSFQMFM-TY 163
Cdd:PRK08044 81 AKGGITTMIEMPLNQlpatvDRASIELKFDA----AKGKLTIDAAQLGGLVSYNLDRLHELD----EVGVVGFKCFVaTC 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 164 KDLYM---LRDSELYQVFHACRDIGAIPR---VHAENGELVAEGAKEALDLGITGPEGIEISHPEELEAEATHRVITIAN 237
Cdd:PRK08044 153 GDRGIdndFRDVNDWQFYKGAQKLGELGQpvlVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 238 RTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTNahatltglHYYHQDWSHAAAYVTV----PPLRlDTNTSTYLMSL 313
Cdd:PRK08044 233 VAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTLakcsPPIR-DLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 314 LANDTLNIVASDHRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLyPRKGR 393
Cdd:PRK08044 304 LFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 394 IIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCP 463
Cdd:PRK08044 380 IAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
9-452 |
1.44e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 112.46 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 9 RILIKGGKVVNDDCTHE-ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTK 87
Cdd:PRK07575 4 SLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGL--EHKEDLFTASR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 88 AALVGGTTMIIGHVLPDKETSLVEAYEKCRALADPKVCCDYALHVGITwwaPKVKAEMETLVREKGVNSFQMFMTyKDLY 167
Cdd:PRK07575 82 ACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT---PDNLPELLTANPTCGIKIFMGSSH-GPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 168 MLRDSELYQVFHACRDIGAiprVHAENGELVAEGAKEAldLGITGPEGIEISHPEELEAEATHRVITIANRTHCPIYLVN 247
Cdd:PRK07575 158 VDEEAALERIFAEGTRLIA---VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHILH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 248 VSSISAGDVIAAAKmqGKVVLAETTNAHATLTglhyyhqdwshAAAYVTV-------PPLRlDTNTSTYLMSLLANDTLN 320
Cdd:PRK07575 233 LSTAIEAELLRQDK--PSWVTAEVTPQHLLLN-----------TDAYERIgtlaqmnPPLR-SPEDNEALWQALRDGVID 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 321 IVASDHRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVVWERgVVGGKMDENRFVAVTSSNAAKILNLyPRKGRIIPGADA 400
Cdd:PRK07575 299 FIATDHAPHTLEEKA---QPYPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDA 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 12746424 401 DVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVF 452
Cdd:PRK07575 374 DLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
15-450 |
1.28e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 103.31 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 15 GKVVNDDCTHEADVYIESGIIQQVGRELMipGGAKVIDATGKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAALVGGT 94
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLRD--FEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 95 TMIIGhvLPDKETSLV--EAYEKCRALADPKVCCDYALHVGITWWAPKVKAEMETLvrekgvnsfqmfmtYKDLYMLRDS 172
Cdd:PRK04250 80 TLVFD--MPNTKPPIMdeKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF--------------YKIFMGASTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 173 ELY----QVFHACrdIGAIPRVHAENGELVAEgakealdlgitGPEgieisHPEELEAEATHRVITIANRTHCPIYLVNV 248
Cdd:PRK04250 144 GIFsenfEVDYAC--APGIVSVHAEDPELIRE-----------FPE-----RPPEAEVVAIERALEAGKKLKKPLHICHI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 249 SSISAGDVIAAAKMQgkVVLAETTNAHATLTglhyyHQDWSHAAAYVTVPPLRldtnTSTYLMSLLAN-DTLNIVASDHR 327
Cdd:PRK04250 206 STKDGLKLILKSNLP--WVSFEVTPHHLFLT-----RKDYERNPLLKVYPPLR----SEEDRKALWENfSKIPIIASDHA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 328 PFTTKQKAMGKEdftkiphGVSGVQDRMSVVWErGVVGGKMDENRFVAVTSSNAAKILNlYPRKGrIIPGADADVVVWDP 407
Cdd:PRK04250 275 PHTLEDKEAGAA-------GIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDM 344
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 12746424 408 EATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENG 450
Cdd:PRK04250 345 KKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
9-450 |
5.99e-20 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 92.63 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 9 RILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKA 88
Cdd:PRK09236 3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 89 ALVGGTT--MIIGHVLPdkETSLVEAYEKCRALADPKVCCDYALHVGITwwapkvKAEMETLVR--EKGVNSFQMFMTYK 164
Cdd:PRK09236 81 AVAGGITsfMEMPNTNP--PTTTLEALEAKYQIAAQRSLANYSFYFGAT------NDNLDEIKRldPKRVCGVKVFMGAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 165 DLYMLRDSE--LYQVFhacRDIGAIPRVHAENGELVAegAKEALDLGITGpEGIEIS-HPEELEAEA----THRVITIAN 237
Cdd:PRK09236 153 TGNMLVDNPetLERIF---RDAPTLIATHCEDTPTIK--ANLAKYKEKYG-DDIPAEmHPLIRSAEAcyksSSLAVSLAK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 238 RTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTNAHatltgLHYYHQDWSHAAAYVTVPPLRLDTNTSTYLMSLLAND 317
Cdd:PRK09236 227 KHGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHH-----LWFDDSDYARLGNLIKCNPAIKTASDREALRQALADD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 318 TLNIVASDHRPFTTKQKAMGkedFTKIPHGVSGVQDRMSVVWERgVVGGKMDENRFVAVTSSNAAKILNLyPRKGRIIPG 397
Cdd:PRK09236 302 RIDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILFDI-KERGFIREG 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12746424 398 ADADVVVWDPEATKTISAstqvqggDFNLYenmRCHGVPLV----------TISRGRVVYENG 450
Cdd:PRK09236 377 YWADLVLVDLNSPWTVTK-------ENILY---KCGWSPFEgrtfrsrvatTFVNGQLVYHNG 429
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
25-463 |
1.72e-19 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 90.69 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 25 EADVYIESGIIQQVGRELmipGGAKVIDATGkLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKAALVGGTTMIIGhvLPD 104
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMD--MPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 105 KETSL--VEAYEKCRALADPKVCCDYALHvgitwwapkvkaEMET----LVREKGVNSFQMFM---TYKDLYMLRDSELY 175
Cdd:PRK01211 87 NNIPIkdYNAFSDKLGRVAPKAYVDFSLY------------SMETgnnaLILDERSIGLKVYMggtTNTNGTDIEGGEIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 176 QVfhacRDIGAIPRVHAENGELVAEGAKEALDLgitgpEGIEISHPEELEAEATHRVITIANRTHcpiYLVNVSSIsagD 255
Cdd:PRK01211 155 KI----NEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLKTK---IIAHVSSI---D 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 256 VIAAakmqgkvVLAETTNAHATLtglhyyHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKA 335
Cdd:PRK01211 220 VIGR-------FLREVTPHHLLL------NDDMPLGSYGKVNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 336 mgkeDFTKIPHGVSGVQDRMSVVWERgVVGGKMDENRFVAVTSSNAAKILNLypRKGRIIPGADADVVVWDPEATKTISA 415
Cdd:PRK01211 286 ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKIND 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 12746424 416 STQVQGGDFNLYENMRCHgVPLVTISRGRVVYENGVFMcAEGTGKFCP 463
Cdd:PRK01211 359 KRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYELI-SERTGKFVP 404
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
9-449 |
2.49e-15 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 78.18 E-value: 2.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 9 RILIKGGKVVNDDCTHE--ADVYIESGIIQQVGRelmIPGG---AKVIDATGKLVIPGGIDTSTHFHQTFMNatcvddfY 83
Cdd:PRK07627 2 KIHIKGGRLIDPAAGTDrqADLYVAAGKIAAIGQ---APAGfnaDKTIDASGLIVCPGLVDLSARLREPGYE-------Y 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 84 HGT-----KAALVGGTTMIIghVLPDK-----ETSLVEAYE-KCRALADPKVCCDYALHVGItwwAPKVKAEMETLVrEK 152
Cdd:PRK07627 72 KATlesemAAAVAGGVTSLV--CPPDTdpvldEPGLVEMLKfRARNLNQAHVYPLGALTVGL---KGEVLTEMVELT-EA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 153 GVNSF-QMFMTYKDLYML-RDSELYQVFHACRDIGAIPRVHAENGelVAEGAKEALDLGITGPegieishPEELEAEATH 230
Cdd:PRK07627 146 GCVGFsQANVPVVDTQVLlRALQYASTFGFTVWLRPLDAFLGRGG--VAASGAVASRLGLSGV-------PVAAETIALH 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 231 RVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTNAHATLTGLHYYHQDwshaAAYVTVPPLRLDTNTSTyL 310
Cdd:PRK07627 217 TIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFD----SQFRLDPPLRSQRDREA-I 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 311 MSLLANDTLNIVASDHRPFTTKQKAMgkeDFTKIPHGVSGVQDRMS--VVWERGVvggKMDENRFVAVTSSNAAKILNLy 388
Cdd:PRK07627 292 RAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPltLKWADEA---KVPLARALARITSAPARVLGL- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12746424 389 pRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYEN 449
Cdd:PRK07627 365 -PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFER 424
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-419 |
2.79e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 77.69 E-value: 2.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 3 ANSASVRILIKGGKVV---NDDCTHEADVYIESGIIQQVGR--ELMIPGGAKVIDATGKLVIPGGIDTSTH--------- 68
Cdd:COG1228 3 APAQAGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHlglgggrav 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 69 -FHQTFMNATCVDDFYHGTK---AALVGGTTMIigHVLPDKETSLVEAYE--KCRALADPKV-CCDYALHVGITWWApKV 141
Cdd:COG1228 83 eFEAGGGITPTVDLVNPADKrlrRALAAGVTTV--RDLPGGPLGLRDAIIagESKLLPGPRVlAAGPALSLTGGAHA-RG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 142 KAEMETLVRE---KGVNSFQMFMTYKDLYMLRDsELYQVFHACRDIGAIPRVHAENgelvAEGAKEALDLGITGpegieI 218
Cdd:COG1228 160 PEEARAALREllaEGADYIKVFAEGGAPDFSLE-ELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEAGVDS-----I 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 219 SHPEELEAEathrvitianrthcpiylvnvssisagdVIAAAKMQGKVVLaeTTNAHATLTGLHYYHQDWSHAAAYV--- 295
Cdd:COG1228 230 EHGTYLDDE----------------------------VADLLAEAGTVVL--VPTLSLFLALLEGAAAPVAAKARKVrea 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 296 TVPPLRLdtntstylmsLLANDTLNIVASDHrpfttkqkamgkedFTKIPHGVS-------GVQDRMSV--VWErgvvgg 366
Cdd:COG1228 280 ALANARR----------LHDAGVPVALGTDA--------------GVGVPPGRSlhrelalAVEAGLTPeeALR------ 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 12746424 367 kmdenrfvAVTsSNAAKILNLYPRKGRIIPGADADVVVWDPEATKTISASTQV 419
Cdd:COG1228 330 --------AAT-INAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAYLEDV 373
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
27-448 |
8.07e-14 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 73.53 E-value: 8.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 27 DVYIESGIIQQVGRELM---IPGGAKVIDATGKLVIPGGIDTSTHF------H-QTFMNATcvddfyhgtKAALVGGTTM 96
Cdd:PRK09059 24 TVLIEDGVIVAAGKGAGnqgAPEGAEIVDCAGKAVAPGLVDARVFVgepgaeHrETIASAS---------RAAAAGGVTS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 97 IIghVLPDKE-----TSLVEaYEKCRALadpkvccDYALhVGITWWAPKVK----AEMET--LVREKGVNSF-QMFMTYK 164
Cdd:PRK09059 95 II--MMPDTDpviddVALVE-FVKRTAR-------DTAI-VNIHPAAAITKglagEEMTEfgLLRAAGAVAFtDGRRSVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 165 DLYMLRDSELYqvfhaCRDIGAIPRVHAENGELVAEGA-KEALDLGITGPEGIeishPEELEAEATHRVITIANRTHCPI 243
Cdd:PRK09059 164 NTQVMRRALTY-----ARDFDAVIVHETRDPDLGGNGVmNEGLFASWLGLSGI----PREAEVIPLERDLRLAALTRGRY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 244 YLVNVSSISAGDVIAAAKMQGKVVLAETTNAHATLtglhyyhqDWSHAAAYVT----VPPLRLDTNTSTyLMSLLANDTL 319
Cdd:PRK09059 235 HAAQISCAESAEALRRAKDRGLKVTAGVSINHLSL--------NENDIGEYRTffklSPPLRTEDDRVA-MVEAVASGTI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 320 NIVASDHRPFTTKQKAMgkeDFTKIPHGVSGVQDRMSVVWeRGVVGGKMDENRFVAVTSSNAAKILNLypRKGRIIPGAD 399
Cdd:PRK09059 306 DIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALSTRPAEIFGL--PAGTLKPGAP 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 12746424 400 ADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYE 448
Cdd:PRK09059 380 ADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
26-417 |
1.18e-13 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 73.10 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 26 ADVYIESGIIQQVGRELM-IPGGAKVIDATGKLVIPGGIDTSTHFHQ-------TFMNATcvddfyhgtKAALVGGTTMI 97
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEpgfeereTLASLA---------AAAAAGGFTRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 98 IghVLPDKE-----TSLVEAYEKcRALADPKVCCDyalhvgitWWAP---KVKAEMETLVRE---KGVNSFQMFMTYKDL 166
Cdd:PRK07369 93 A--ILPDTFppldnPATLARLQQ-QAQQIPPVQLH--------FWGAltlGGQGKQLTELAElaaAGVVGFTDGQPLENL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 167 YMLRDSELY-QVFHacRDIGAIPRVHAENGELVAEGAKEALDLGITGpegieisHPEELEAEATHRVITIANRTHCPIYL 245
Cdd:PRK07369 162 ALLRRLLEYlKPLG--KPVALWPCDRSLAGNGVMREGLLALRLGLPG-------DPASAETTALAALLELVAAIGTPVHL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 246 VNVSSISAGDVIAAAKMQGKVVLAETTNAHATLT--GLHYYHqdwshaaayvtvPPLRLDT---NTS--TYLMSLLANDT 318
Cdd:PRK07369 233 MRISTARSVELIAQAKARGLPITASTTWMHLLLDteALASYD------------PNLRLDPplgNPSdrQALIEGVRTGV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 319 LNIVASDHRPFTTKQKAMGkedFTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLYPRkgRIIPGA 398
Cdd:PRK07369 301 IDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLAPGQ 375
|
410
....*....|....*....
gi 12746424 399 DADVVVWDPEATKTISAST 417
Cdd:PRK07369 376 PAELILFDPQKTWTVSAQT 394
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-446 |
3.34e-13 |
|
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: 70.99 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 57 LVIPGGIDTSTHFHQTFMNATCVDDFY------HGTKAALVGGTTMIIGH--VLPDKETSLVEAYEKCRA-----LADPK 123
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMgaTTSTGIEALLEAAEELPLglrflGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 124 VCCDYALHVGITWWaPKVKAEMETLVREKGVNSFQMFMTYKDlYMLRDSELYQVFHACRDIGAIPRVHAENGELVAEGAK 203
Cdd:pfam01979 81 LDTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 204 EALDLGItgpegIEISHPEELEAEATHRVITIAnRTHCpIYLVnvssisagdviaaakmqgkVVLAETTNAHATLTGLhy 283
Cdd:pfam01979 159 AAFGGGI-----EHGTHLEVAESGGLLDIIKLI-LAHG-VHLS-------------------PTEANLLAEHLKGAGV-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 284 yhqdwshaaAYVTVPPLRLDTNTSTyLMSLLANDTLNIVASDHRpfttkqkAMGkedftkiphGVSGVQDRMSV-VWERG 362
Cdd:pfam01979 211 ---------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGA-------GSG---------NSLNMLEELRLaLELQF 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 363 VVGGKMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVVWDPEATKTISASTqvqggdfnlyenmrCHGVPLVTISR 442
Cdd:pfam01979 265 DPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLK--------------PDGNVKKVIVK 330
|
....
gi 12746424 443 GRVV 446
Cdd:pfam01979 331 GKIV 334
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
30-448 |
2.83e-12 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 68.58 E-value: 2.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 30 IESGIIQQVGRELmipGGAKVIDATGKLVIPGGIDTSTHFHQTFMNAtcvDDFYHGTKAALVGGttmiIGHVL--PDKET 107
Cdd:PRK08417 3 IKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVSLKNDSLSS---KNLKSLENECLKGG----VGSIVlyPDSTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 108 SLVEAYE---KCRALADPKVCCDYALHVgitwWAPKVK-AEMETLVReKGVNSFQMFMTYKDLYMLRDSELYQ-----VF 178
Cdd:PRK08417 73 AIDNEIAlelINSAQRELPMQIFPSIRA----LDEDGKlSNIATLLK-KGAKALELSSDLDANLLKVIAQYAKmldvpIF 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 179 HAC-----RDIGAIprvhaENGELVAEgakealdLGITG-PEGIEISHpeeleaeaTHRVITIANRTHCPIYLVNVSSIS 252
Cdd:PRK08417 148 CRCedssfDDSGVM-----NDGELSFE-------LGLPGiPSIAETKE--------VAKMKELAKFYKNKVLFDTLALPR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 253 AGDVIAAAKMQGKVVLAETTnahatltgLHYYHQDWSHAAAYVTV----PPLRlDTNTSTYLMSLLANDTLNIVASDHRP 328
Cdd:PRK08417 208 SLELLDKFKSEGEKLLKEVS--------IHHLILDDSACENFNTAaklnPPLR-SKEDRLALLEALKEGKIDFLTSLHSA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 329 fttkqKAMGKED--FTKIPHGVSGVQDRMSVVWERGVVGGKMDENRFVAVTSSNAAKILNLypRKGRIIPGADADVVVWD 406
Cdd:PRK08417 279 -----KSNSKKDlaFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFD 351
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 12746424 407 PEATKTISASTQVQGGDfNLYENMRCHgvplvtISRGRVVYE 448
Cdd:PRK08417 352 PNESTIIDDNFSLYSGD-ELYGKIEAV------IIKGKLYLE 386
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
10-120 |
1.47e-10 |
|
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: 63.38 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDDCTHE---ADVYIESGIIQQVGR--ELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFM---------- 74
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPalPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLrgladdlplm 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12746424 75 -----------NATCVDDFYHGTKAALV----GGTTMIIGHVLPDKETsLVEAYEKC--RALA 120
Cdd:cd01298 81 ewlkdliwpleRLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDA-VAEAAEELgiRAVL 142
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
10-452 |
2.62e-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: 62.70 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVndDCT----HEADVYIESGIIQQVGRELmIPGGAKVIDATGKLVIPGGIDTSTHFHQTFmnatcvddFYHG 85
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPIL-STSAREVIDAAGLVVAPGFIDVHTHYDGQV--------FWDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 86 TKAALV--GGTTMIIGhvlpdkETSLVEAYEKCRALADPK--VCCDYALHVGITWWAPKVKAEMETLVRE-KGVNSFQMF 160
Cdd:cd01297 71 DLRPSSrqGVTTVVLG------NCGVSPAPANPDDLARLImlMEGLVALGEGLPWGWATFAEYLDALEARpPAVNVAALV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 161 ----MTYKDLYMLR----DSELYQV---FHACRDIGAI---------PRVHAENGELV--AEGAKEAldlgitgpEGIEI 218
Cdd:cd01297 145 ghaaLRRAVMGLDAreatEEELAKMrelLREALEAGALgistglayaPRLYAGTAELValARVAARY--------GGVYQ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 219 SHPE---ELEAEATHRVITIANRTHCPiylVNVSSISAGDVIAAAKMQGKVVLAEttnaHATLTGlhyyHQDWSHAAAYV 295
Cdd:cd01297 217 THVRyegDSILEALDELLRLGRETGRP---VHISHLKSAGAPNWGKIDRLLALIE----AARAEG----LQVTADVYPYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 296 TvpplrldtntstylmsLLANDTLNIVASDHRPFTTKQKAMGKedftkiPH-GVSGVQDRMSVVWERGvvGGKMDENRFV 374
Cdd:cd01297 286 A----------------GSEDDVRRIMAHPVVMGGSDGGALGK------PHpRSYGDFTRVLGHYVRE--RKLLSLEEAV 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12746424 375 AVTSSNAAKILNLYPRkGRIIPGADADVVVWDPeATKTISASTQvqggDFNLYENmrchGVPLVTISrGRVVYENGVF 452
Cdd:cd01297 342 RKMTGLPARVFGLADR-GRIAPGYRADIVVFDP-DTLADRATFT----RPNQPAE----GIEAVLVN-GVPVVRDGAF 408
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
9-151 |
2.84e-10 |
|
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: 62.54 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 9 RILIKGGKVVNDDCTHE----ADVYIESGIIQQVGRELMIP---GGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVD- 80
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 81 --------------------DFYHGTKAALV----GGTTMI--IGHVLPDKETSLVEAYEKC--RALAdPKVCCDYALHV 132
Cdd:COG0402 81 plldwleeyiwplearldpeDVYAGALLALAemlrSGTTTVadFYYVHPESADALAEAAAEAgiRAVL-GRGLMDRGFPD 159
|
170
....*....|....*....
gi 12746424 133 GITWWAPKVKAEMETLVRE 151
Cdd:COG0402 160 GLREDADEGLADSERLIER 178
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
10-68 |
4.37e-10 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 61.79 E-value: 4.37e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12746424 10 ILIKGGKVVNDDCTHEA--DVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
11-461 |
8.92e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 60.93 E-value: 8.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 11 LIKGGKVVNDDCtheadVYIESGIIQQVgRELMiPGGAKVIDAT-GKLVIPGGIDTstHFHQTFMNATCVDDFYHGTKAA 89
Cdd:PRK00369 4 WIKGKAYLGKEI-----KEICINFDRRI-KEIK-SRCKPDLDLPqGTLILPGAIDL--HVHLRGLKLSYKEDVASGTSEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 90 LVGGTTMIIGhvLPDKETSL--VEAY-EKCRALADpKVCCDYALHVGItwwaPKVKAEMETLvrekGVNSFQMFMtyKDL 166
Cdd:PRK00369 75 AYGGVTLVAD--MPNTIPPLntPEAItEKLAELEY-YSRVDYFVYSGV----TKDPEKVDKL----PIAGYKIFP--EDL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 167 ymlrdselyqvfhacrdigaiprVHAENGELVAEGAKealdlgitgpegIEISHPEELEAEATHRvitiANRTHC----- 241
Cdd:PRK00369 142 -----------------------EREETFRVLLKSRK------------LKILHPEVPLALKSNR----KLRRNCwyeia 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 242 PIYL------VNVSSISAGDVIAAAKMQGKVVlaETTNAHATLTGLhyyhqdwSHAAAYVTvPPLRlDTNTSTYLMSLLA 315
Cdd:PRK00369 183 ALYYvkdyqnVHITHASNPRTVRLAKELGFTV--DITPHHLLVNGE-------KDCLTKVN-PPIR-DINERLWLLQALS 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 316 N-DTlniVASDHRPFTTKQKAMgkeDFTKIPHGVSGVQDRMSVVWERgVVGGKMDENRFVAVTSSNAAKILNLypRKGRI 394
Cdd:PRK00369 252 EvDA---IASDHAPHSSFEKLQ---PYEVCPPGIAALSFTPPFIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEI 322
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12746424 395 IPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRChgvPLVTISRGRVVYENGVFMCAEGTGKF 461
Cdd:PRK00369 323 KEGYRANFTVIQFEDWRYSTKYSKVIETPLDGFELKAS---VYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-450 |
1.64e-08 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 57.01 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 1 MLANSASVRILIKGGKVVNDDCTHEA--DVYIESGIIQQVGRELMipGGAKVIDATGKLVIPGGIDTSTHfhqtfmnATC 78
Cdd:PRK09061 12 MPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH-------GQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 79 VDDfyHGTKaALVGGTTMI---IGhVLPdketsLVEAYEKCRALADPkvccdyaLHVGI-TWWAPKVKAEMETLVREKGV 154
Cdd:PRK09061 83 VAA--YRMQ-AFDGVTTALeleAG-VLP-----VARWYAEQAGEGRP-------LNYGAsVGWTPARIAVLTGPQAEGTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 155 NSFQMFMTYKDLYM--LRDSELYQVFHACR---DIGAIPrVHAENGELVAEGAKEALDLGITG-----PEGIEISHPEEL 224
Cdd:PRK09061 147 ADFGKALGDPRWQEraATPAELAEILELLEqglDEGALG-IGIGAGYAPGTGHKEYLELARLAaragvPTYTHVRYLSNV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 225 E----AEATHRVITIANRTHCPIYLVNVSSISAGDV------IAAAKMQGKVVLAETT--NAHATLTGLHYYHQDWSH-- 290
Cdd:PRK09061 226 DprssVDAYQELIAAAAETGAHMHICHVNSTSLRDIdrclalVEKAQAQGLDVTTEAYpyGAGSTVVGAAFFDPGWLErm 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 291 -----AAAYV----------TVPPLRLDTNTSTYLMSLLAND--------------TLNIVASDHRPFTTKQKAMGKEDF 341
Cdd:PRK09061 306 glgygSLQWVetgerlltreELAKLRANDPGGLVLIHFLDEDnprdralldrsvlfPGAAIASDAMPWTWSDGTVYEGDA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 342 TKIPHGV------SGVQDRMSVVW--ERGVVGgkMDENrfVAVTSSNAAKILNLY----PRKGRIIPGADADVVVWDPEa 409
Cdd:PRK09061 386 WPLPEDAvshprsAGTFARFLREYvrERKALS--LLEA--IRKCTLMPAQILEDSvpamRRKGRLQAGADADIVVFDPE- 460
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 12746424 410 tkTISastqvqggDFNLYENMR--CHGVPLVTISrGRVVYENG 450
Cdd:PRK09061 461 --TIT--------DRATFEDPNrpSEGVRHVLVN-GVPVVSNG 492
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
9-81 |
1.04e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 54.62 E-value: 1.04e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12746424 9 RILIKGGKVVNDDCTH----EADVYIESGIIQQVGRELMiPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDD 81
Cdd:PRK08204 3 RTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPSIE-APDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADW 78
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
9-72 |
1.57e-07 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 53.85 E-value: 1.57e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12746424 9 RILIKGGKVVNDDCTHE---ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK07228 2 TILIKNAGIVTMNAKREivdGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQT 68
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
11-95 |
2.17e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.18 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 11 LIKGGKVVNDDCTHE-ADVYIESGIIQQVGRelMIPGGAKVIDATGKLVIPGGIDtsTHFH----QTFMNATcVDDFYHG 85
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFID--LHVHggggVDFMDGT-PEALRTI 75
|
90
....*....|
gi 12746424 86 TKAALVGGTT 95
Cdd:COG1820 76 ARAHARHGTT 85
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
10-68 |
2.80e-07 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 53.27 E-value: 2.80e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 12746424 10 ILIKGGKVVndDCTHE-----ADVYIESG-IIQQVGRelmiPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:COG1229 3 LIIKNGRVY--DPANGidgevMDIAIKDGkIVEEPSD----PKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
10-68 |
4.27e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 52.50 E-value: 4.27e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12746424 10 ILIKGGKVVNDDCTH--EADVYIESGIIQQVGRELMIPGGaKVIDATGKLVIPGGIDTSTH 68
Cdd:PRK08393 3 ILIKNGYVIYGENLKviRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTH 62
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
10-77 |
2.04e-06 |
|
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: 50.27 E-value: 2.04e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH--FHQTFMNAT 77
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHggGGADFMDGT 70
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
374-408 |
2.23e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 50.10 E-value: 2.23e-06
10 20 30
....*....|....*....|....*....|....*
gi 12746424 374 VAVTSSNAAKILNLYPRKGRIIPGADADVVVWDPE 408
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
9-72 |
3.30e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 49.85 E-value: 3.30e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 9 RILIKGGKVV---NDDCTHEAD--VYIESGIIQQVGRELMIPG-GAKVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHFYQT 71
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
27-71 |
6.69e-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: 48.48 E-value: 6.69e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 12746424 27 DVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQ 71
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQ 45
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
59-135 |
8.69e-06 |
|
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: 48.22 E-value: 8.69e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12746424 59 IPGGIDTSTHFHQtfMNATCVDDFYHGTKAALVGGTTMIigHVLPDKETSLV--EAYEKCRALADPKVCCDYALHVGIT 135
Cdd:cd01316 5 LPGLIDVHVHLRE--PGATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVdvASLKLVQSLAQAKARCDYAFSIGAT 79
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
10-74 |
1.17e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 47.96 E-value: 1.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12746424 10 ILIKGGKVVNDDCTHE---ADVYIESGIIQQVGRelMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:PRK06380 3 ILIKNAWIVTQNEKREilqGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTAS 68
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
10-98 |
4.42e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 46.25 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVNDdCTHE---ADVYIESGIIQQVGRElmIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNatcVDDFYhgt 86
Cdd:COG1001 7 LVIKNGRLVNV-FTGEileGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFIDGHVHIESSMVT---PAEFA--- 77
|
90
....*....|..
gi 12746424 87 KAALVGGTTMII 98
Cdd:COG1001 78 RAVLPHGTTTVI 89
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
10-72 |
4.57e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 45.90 E-value: 4.57e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12746424 10 ILIKGGKVVNDDC--THEADVYIESGIIQQVGRElmIPGGA-KVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK06038 4 IIIKNAYVLTMDAgdLKKGSVVIEDGTITEVSES--TPGDAdTVIDAKGSVVMPGLVNTHTHAAMT 67
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
10-73 |
4.65e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 46.08 E-value: 4.65e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12746424 10 ILIKGGKVVNDDCTH----EADVYIESGIIQQVGRELMIPG---GAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:PRK07203 2 LLIGNGTAITRDPAKpvieDGAIAIEGNVIVEIGTTDELKAkypDAEFIDAKGKLIMPGLINSHNHIYSGL 72
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
33-68 |
5.09e-05 |
|
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: 45.77 E-value: 5.09e-05
10 20 30
....*....|....*....|....*....|....*.
gi 12746424 33 GIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:cd01309 2 GKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
374-407 |
5.25e-05 |
|
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: 45.65 E-value: 5.25e-05
10 20 30
....*....|....*....|....*....|....
gi 12746424 374 VAVTSSNAAKILNLYPRKGRIIPGADADVVVWDP 407
Cdd:cd00854 330 VRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD 363
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
1-80 |
1.09e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 44.79 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 1 MLANSASVRILIKGGKV--VNDDC-THEAdVYIESGIIQQVG--RELM--IPGGAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:COG1574 1 MKLAAAAADLLLTNGRIytMDPAQpVAEA-VAVRDGRIVAVGsdAEVRalAGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
....*..
gi 12746424 74 MNATCVD 80
Cdd:COG1574 80 LALLGVD 86
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
355-447 |
1.36e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 44.44 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 355 MSVVWERGVVGGKMDENRF---VAVTSSNAAKILNLYPRKGRIIPGADADVVVWDPEATkTISASTqvqggdfnlyenmR 431
Cdd:pfam07969 383 MRQTAGGGEVLGPDEELSLeeaLALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPL-TVDPPA-------------I 448
|
90
....*....|....*.
gi 12746424 432 CHGVPLVTISRGRVVY 447
Cdd:pfam07969 449 ADIRVRLTVVDGRVVY 464
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
12-68 |
1.61e-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: 44.33 E-value: 1.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12746424 12 IKGGKVVndDCTHE-----ADVYIESGIIQQvgrELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:cd01304 1 IKNGTVY--DPLNGingekMDIFIRDGKIVE---SSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
24-74 |
2.62e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 43.64 E-value: 2.62e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 12746424 24 HEAD--VYIESGIIQQVG--RELM--IPGGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:PRK09228 28 YIEDglLLVEDGRIVAAGpyAELRaqLPADAEVTDYRGKLILPGFIDTHIHYPQTDM 84
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
376-408 |
4.69e-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 [Multi-domain] Cd Length: 387 Bit Score: 42.76 E-value: 4.69e-04
10 20 30
....*....|....*....|....*....|...
gi 12746424 376 VTSSNAAKILNLYPrKGRIIPGADADVVVWDPE 408
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD 361
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
26-73 |
5.92e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 42.23 E-value: 5.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 12746424 26 ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTF 64
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
375-419 |
8.00e-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: 41.91 E-value: 8.00e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 12746424 375 AVTSsNAAKILNLYPRKGRIIPGADADVVVWDPEATKTISASTQV 419
Cdd:cd01309 308 AITI-NPAKILGIEDRVGSLEPGKDADLVVWNGDPLEPTSKPEQV 351
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
28-69 |
8.43e-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: 41.86 E-value: 8.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 12746424 28 VYIESGIIQQVGRELMIPG----GAKVIDATGKLVIPGGIDTSTHF 69
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPApgpaAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
26-70 |
1.47e-03 |
|
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: 41.08 E-value: 1.47e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 12746424 26 ADVYIESGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDtsTHFH 70
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVD--PHIH 57
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
376-460 |
2.23e-03 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 40.95 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 376 VTSSNAAKILNLyPRKGRIIPGADADVVVWDPeatktisastQVQGGDFNLYENMrcHGVPLVTISRGRVVYENGVFMcA 455
Cdd:COG1229 437 MTRAGPAKALGL-ADRGHLGVGADADIAIYDI----------NPDDKDYEDIEKM--FSKPAYVIKDGEVVVKDGEIV-A 502
|
....*
gi 12746424 456 EGTGK 460
Cdd:COG1229 503 TPQGR 507
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
11-126 |
2.57e-03 |
|
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 [Multi-domain] Cd Length: 387 Bit Score: 40.45 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 11 LIKGGKVVNDDCTHEADVYIESGIIQQVGRELMIPGGAK--VIDATGKLVIPGGIDtsTHFHQT-------FMNATCVDD 81
Cdd:cd01308 3 LIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENvtVVDLHGKILVPGFID--QHVHIIggggeggPSTRTPEVT 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 12746424 82 FYHGTKAalvgGTTMIIGHVLPDKET-SLVEAYEKCRALADPKVCC 126
Cdd:cd01308 81 LSDLTTA----GVTTVVGCLGTDGISrSMEDLLAKARALEEEGITC 122
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
10-452 |
7.88e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 39.00 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 10 ILIKGGKVVndDCTH----EADVYIESGIIQQVGReLMIPGGAKVIDATGKLVIPGGIDTSTHFH-QTFMNATCVDDFYH 84
Cdd:COG3653 4 LLIRGGTVV--DGTGappfRADVAIKGGRIVAVGD-LAAAEAARVIDATGLVVAPGFIDIHTHYDlQLLWDPRLEPSLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 85 GTkaalvggTTMIIG-------HVLPDKETSLVEAYEKC------------------RALADPKVCCDYALHV------- 132
Cdd:COG3653 81 GV-------TTVVMGncgvsfaPVRPEDRDRLIDLMEGVegipegldwdwesfgeylDALERRGLGVNVASLVghgtlra 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 133 ---GITWWAPKVK--AEMETLVREkgvnsfqmfmtykdlymlrdselyqvfhACRDiGA---------IPRVHAENGELV 198
Cdd:COG3653 154 yvmGLDDRPPTPEelARMRALLRE----------------------------AMEA-GAlglstgliyVPGTYASTDELV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 199 AEgAKEALDLGitgpeGIEISHPEELEAEATHRV---ITIANRTHCP--IYLVNVS-------SISAGDVIAAAKMQGKV 266
Cdd:COG3653 205 AL-AKVVAEYG-----GVYQSHMRDEGDGLLEAVdelIRIGREAGVPvhISHLKAAgkpnwgkADEVLALIEAARAEGLD 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 267 VLAETTNAHATLTGLHYYHQDWSHA------AAYVTVPPLR------LDTNTSTYLMSLLANDTLNIVAS-DHRPFTTK- 332
Cdd:COG3653 279 VTADVYPYPAGSTGLGALLPPWAAAgglderLARLRDPATRariraeIEEGLPDNLLGRGGWDNILISDSpPNEPLVGKs 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 333 --------------------------------------QKAMGKEDFTKI---------PH-GVSGVQDRM--SVVWERG 362
Cdd:COG3653 359 laeiaaergvdpadaaldllleedgrvlivyfimseedVRELLRHPWVMIgsdgglggkAHpRAYGTFPRVlgHYVRERG 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12746424 363 VvggkMDENRFVAVTSSNAAKILNLYPRkGRIIPGADADVVVWDPEA---TKTISASTQvqggdfnlyenmRCHGVPLVT 439
Cdd:COG3653 439 V----LSLEEAVRKLTSLPADRLGLKDR-GLLRPGYRADLVVFDPATladRATFDLPAQ------------RADGIRAVI 501
|
570
....*....|...
gi 12746424 440 ISrGRVVYENGVF 452
Cdd:COG3653 502 VN-GVVVVEDGKP 513
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
367-406 |
9.46e-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: 38.39 E-value: 9.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 12746424 367 KMDENRFVAVTSSNAAKILNLYPRKGRIIPGADADVVVWD 406
Cdd:cd01296 309 RMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
|
| |
