|
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: 630.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAA 89
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 90 LVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITWWAPKVKAEMETLVrEKGVNSFQMFMTYKDLYML 169
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELV-KKGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 170 RDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 250 SISAGDVIAAAKMQGKVVLAETTTAHATLTGlHYYHQDWSHAAAYVTVPPLRLDTnTSTYLMSLLANDTLNIVASDHRPF 329
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDD-SDYWKDWFEGAKYVCSPPLRPKE-DQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 330 TTKQKAMGKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDPEA 409
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1370478292 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: 553.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 9 RILIKGGKVVNDDCTHEADVYIENGIIQQVGRelmiPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKA 88
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGA----NLGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 89 ALVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITWWAPKVKAEMETLVREkGVNSFQMFMTYKDLYM 168
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELVEE-GITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 169 LRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVNV 248
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 249 SSISAGDVIAAAKMQGKVVLAETTTAHATLTGLHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRP 328
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLR-DKEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 329 FTTKQKAM-GKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDP 407
Cdd:PRK08323 316 FCFEQKKQlGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478292 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: 552.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAA 89
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 90 LVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITWWAPKVKAEMETLVREKGVNSFQMFMTYKDLYML 169
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 170 RDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 250 SISAGDVIAAAKMQGKVVLAETTTAHATLTGlHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRPF 329
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDD-THYDKPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 330 -TTKQKAMGKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDPE 408
Cdd:TIGR02033 319 nFAQKKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1370478292 409 ATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCP 463
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVK 453
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
7-481 |
2.18e-173 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 499.37 E-value: 2.18e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 7 SVRILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGT 86
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 87 KAALVGGTTMIIGHVLPdKETSLVDAYEKCRGLADpKVCCDYALHVGITWWAPKVKAEMETLVREKGVNSFQMFMTYKDL 166
Cdd:PLN02942 84 AAALAGGTTMHIDFVIP-VNGNLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 167 YMLRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLV 246
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 247 NVSSISAGDVIAAAKMQGKVVLAETTTAHATLTGLHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDH 326
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIR-PAGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 327 RPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVVWD 406
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370478292 407 PEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCPLRSFPdTVYKKLVQREKT 481
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS-YLFDGIQKADAA 474
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
11-461 |
1.05e-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: 383.67 E-value: 1.05e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 11 LIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTKAAL 90
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREPGL--EHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 91 VGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITWWAPKVKAEMETLVrEKGVNSFQMFMTYKD-LYML 169
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 170 RDSELYQVLHACKDIGAIARVHAENGELVAEGAKEAldlGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMNE---GKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 250 SISAGDVIAAAKMQGKVVLAETTTAHATLTGLHYYHQDwshaAAYVTVPPLRLDTNTSTyLMSLLANDTLNIVASDHRPF 329
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYG----TNFKVNPPLRTEEDREA-LWEGLADGTIDVIATDHAPH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 330 TTKQKAmgkEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLyPRKGRIIPGADADVVVWDPEA 409
Cdd:COG0044 310 TLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDA 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1370478292 410 TKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFmCAEGTGKF 461
Cdd:COG0044 386 EWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRF 436
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
12-470 |
2.44e-117 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 355.93 E-value: 2.44e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 12 IKGGKVVNDDCTHEADVYIENGIIQQVGRELmiPGGAKVIDATGKLVIPGGIDTSTHFHQ-TFMNATCVDDFYHGTKAAL 90
Cdd:PRK13404 8 IRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQpSGDGIMMADDFYTGTVSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 91 VGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITWWAPKV-KAEMETLVREkGVNSFQMFMTYKDLyML 169
Cdd:PRK13404 86 FGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTYDDL-KL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 170 RDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVNVS 249
Cdd:PRK13404 164 DDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 250 SISAGDVIAAAKMQGKVVLAETTTAHATLTGlHYYHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRPF 329
Cdd:PRK13404 244 GREAAEQIRRARGRGLKIFAETCPQYLFLTA-EDLDRPGMEGAKYICSPPPR-DKANQEAIWNGLADGTFEVFSSDHAPF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 330 ---TTKQKAMGKED--FTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVV 404
Cdd:PRK13404 322 rfdDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAI 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478292 405 WDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCPlRSFPDT 470
Cdd:PRK13404 402 WDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLA-RSLPDR 466
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
11-450 |
7.43e-74 |
|
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: 242.19 E-value: 7.43e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 11 LIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAAL 90
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINE--PGRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 91 VGGTTMIIGHVL---PdkETSLVDAYEKCRGLADPKVCCDYALHVGITwwaPKVKAEMETLVrEKGVNSFQMFMT---YK 164
Cdd:cd01315 81 AGGITTIIDMPLnsiP--PTTTVENLEAKLEAAQGKLHVDVGFWGGLV---PGNLDQLRPLD-EAGVVGFKCFLCpsgVD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 165 DLYMLRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIY 244
Cdd:cd01315 155 EFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 245 LVNVSSISAGDVIAAAKMQGKVVLAETTTAHATLTglhyyHQDWSHAAAYVTV-PPLRLDTNTSTyLMSLLANDTLNIVA 323
Cdd:cd01315 235 IVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFT-----AEDVPDGGTEFKCaPPIRDAANQEQ-LWEALENGDIDMVV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 324 SDHRPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVV 403
Cdd:cd01315 309 SDHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFV 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1370478292 404 VWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENG 450
Cdd:cd01315 389 VWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDG 435
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
10-452 |
1.89e-59 |
|
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ring-opening hydrolysis. The seed members of this model are all in the vicinity of other genes involved in the processes of xanthine/urate/allantoin catabolism. Although not included in the seed, many eukaryotic homologs of this family are included above the trusted cutoff. Below the noise cutoff are related hydantoinases.
Pssm-ID: 163175 [Multi-domain] Cd Length: 443 Bit Score: 203.77 E-value: 1.89e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHEADVYIENGIIQQVGRElMIPGGAKVIDATGKLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKAA 89
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 90 LVGGTTMIIG---HVLPdkETSLVDAYEKCRGLADPKVCCDYALHVGITwwaPKVKAEMETLvREKGVNSFQMFMTYKDL 166
Cdd:TIGR03178 79 AAGGITTYIDmplNSIP--ATTTRASLEAKFEAAKGKLAVDVGFWGGLV---PYNLDDLREL-DEAGVVGFKAFLSPSGD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 167 YMLRDSELYQVLHACKDI---GAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCPI 243
Cdd:TIGR03178 153 DEFPHVDDWQLYKGMRELarlGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 244 YLVNVSSISAGDVIAAAKMQGKVVLAETTTAHatltgLHYYHQDWSH-AAAYVTVPPLRLDTNTSTyLMSLLANDTLNIV 322
Cdd:TIGR03178 233 HVVHLSSAEAVELITEAKQEGLDVTVETCPHY-----LTLTAEEVPDgGTLAKCAPPIRDLANQEG-LWEALLNGLIDCV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 323 ASDHRPFTTKQKAMGkeDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLyPRKGRIIPGADADV 402
Cdd:TIGR03178 307 VSDHSPCTPDLKRAG--DFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDADF 383
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1370478292 403 VVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVF 452
Cdd:TIGR03178 384 VFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQF 433
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
10-465 |
1.68e-57 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 198.72 E-value: 1.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAA 89
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFRE--PGYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 90 LVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGIT-WWAPkvkaeMETLVREkGVNSF-QMFMTYKDLY 167
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgNWDP-----LESLWER-GVFALgEIFMADSTGG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 168 MLRDSELY-QVLHACKDIGAIARVHAENGELVAEGAKEaLDlGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLV 246
Cdd:PRK02382 156 MGIDEELFeEALAEAARLGVLATVHAEDEDLFDELAKL-LK-GDADADAWSAYRPAAAEAAAVERALEVASETGARIHIA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 247 NVSSISAGDVIAAAKMQgkvvlAETTTAHATLTglhyyHQDWSHAAAYVTV-PPLRLDTNTSTyLMSLLANDTLNIVASD 325
Cdd:PRK02382 234 HISTPEGVDAARREGIT-----CEVTPHHLFLS-----RRDWERLGTFGKMnPPLRSEKRREA-LWERLNDGTIDVVASD 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 326 HRPFTTKQKAMgkeDFTKIPHGVSGVQDRMSVIWErGVVGGKMDENRFVAVTSSNAAKLLNLyPRKGRIIPGADADVVVW 405
Cdd:PRK02382 303 HAPHTREEKDA---DIWDAPSGVPGVETMLPLLLA-AVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDADLVLV 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370478292 406 DPEATKTISASTQVQGGDFNLYENMRchGV-PLVTISRGRVVYENGVFMCAEGTGKFCPLR 465
Cdd:PRK02382 378 DPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
56-439 |
3.85e-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: 191.84 E-value: 3.85e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 56 KLVIPGGIDTstHFHQTFMNATCV-DDFYHGTKAALVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGI 134
Cdd:cd01302 1 LLVLPGFIDI--HVHLRDPGGTTYkEDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 135 TwwaPKVKAEMETLVREKGVNSFQMFMTYK--DLYMLRDSELYQVLHACKDIGAIARVHAEngelvaegakealdlgitg 212
Cdd:cd01302 79 G---PGDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 213 pegieisrpeeleaeathRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHatltgLHYYHQDWSHAA 292
Cdd:cd01302 137 ------------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHH-----LFLDESMLRLNG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 293 AYVTV-PPLRlDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKAMGKeDFTKIPHGVSGVQDRMSVIWERGVVGGkMDEN 371
Cdd:cd01302 194 AWGKVnPPLR-SKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPILLTEGVKRG-LSLE 270
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370478292 372 RFVAVTSSNAAKLLNLYPrKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVT 439
Cdd:cd01302 271 TLVEILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
10-452 |
1.37e-55 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 193.76 E-value: 1.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGgAKVIDATGKLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKAA 89
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPA-REIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 90 LVGGTT----MIIGHVLPdkeTSLVDAYEKCRGLADPKVCCDYALHVGITwwaPKVKAEMETLVrEKGVNSFQMFMTYKD 165
Cdd:PRK06189 82 AAGGCTtyfdMPLNSIPP---TVTREALDAKAELARQKSAVDFALWGGLV---PGNLEHLRELA-EAGVIGFKAFMSNSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 166 LYMLR---DSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIANRTHCP 242
Cdd:PRK06189 155 TDEFRssdDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 243 IYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHatltgLHYYHQDWSH-AAAYVTVPPLRlDTNTSTYLMSLLANDTLNI 321
Cdd:PRK06189 235 LHFVHISSGKAVALIAEAKKRGVDVSVETCPHY-----LLFTEEDFERiGAVAKCAPPLR-SRSQKEELWRGLLAGEIDM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 322 VASDHRPFTTKQKAmgKEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLyPRKGRIIPGADAD 401
Cdd:PRK06189 309 ISSDHSPCPPELKE--GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADAD 385
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1370478292 402 VVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVF 452
Cdd:PRK06189 386 FVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEV 436
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
47-439 |
7.62e-43 |
|
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: 157.40 E-value: 7.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 47 GAKVIDATGKLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKAALVGGTTMIIghVLPD-----KETSLVDAY-EKCRGLA 120
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPNtnpviDNPAVVELLkNRAKDVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 121 DPKVCCDYALHVGItwwAPKVKAEMETLvREKGVNSFQmfmtyKDLYMLRDSE-LYQVLHACKDIGAIARVHAENGELVA 199
Cdd:cd01317 77 IVRVLPIGALTKGL---KGEELTEIGEL-LEAGAVGFS-----DDGKPIQDAElLRRALEYAAMLDLPIIVHPEDPSLAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 200 EGA----KEALDLGITGpegieisRPEELEAEATHRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAH 275
Cdd:cd01317 148 GGVmnegKVASRLGLPG-------IPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAEVTPHH 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 276 ATLTGLHYYHQDwshAAAYVTvPPLRlDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKamgKEDFTKIPHGVSGVQDRM 355
Cdd:cd01317 221 LLLDDEALESYD---TNAKVN-PPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEK---DLPFAEAPPGIIGLETAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 356 SVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPrkGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGV 435
Cdd:cd01317 293 PLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGR 370
|
....
gi 1370478292 436 PLVT 439
Cdd:cd01317 371 VLAT 374
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
9-449 |
1.27e-37 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 143.80 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 9 RILIKGGKVVNDDCTHE-ADVYIENGIIQQVGRELmIPGGAKVIDATGKLVIPGGIDTSTHF------HQtfmnatcvDD 81
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENI-EAEGAEVIDATGLVVAPGLVDLHVHLrepgqeDK--------ET 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 82 FYHGTKAALVGG-TTMII-GHVLPDKETSLVDAY--EKCRGLADPKVCCDYALHVGItwwAPKVKAEMETLvREKGVnsf 157
Cdd:PRK09357 73 IETGSRAAAAGGfTTVVAmPNTKPVIDTPEVVEYvlDRAKEAGLVDVLPVGAITKGL---AGEELTEFGAL-KEAGV--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 158 QMFMTykDLYMLRDSEL-YQVLHACKDIGAIARVHAE-----NGELVAEGAKEALdLGITGpegieisRPEELEAEATHR 231
Cdd:PRK09357 146 VAFSD--DGIPVQDARLmRRALEYAKALDLLIAQHCEdpsltEGGVMNEGEVSAR-LGLPG-------IPAVAEEVMIAR 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 232 VITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHATLTglhyyHQDWSHAAAYVTV-PPLRLDTNTSTyL 310
Cdd:PRK09357 216 DVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLT-----DEDLLTYDPNYKVnPPLRTEEDREA-L 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 311 MSLLANDTLNIVASDHRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPr 390
Cdd:PRK09357 290 IEGLKDGTIDAIATDHAPHAREEKE---CEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA- 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1370478292 391 kGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYEN 449
Cdd:PRK09357 366 -GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
55-443 |
1.61e-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: 1.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 55 GKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAALVGGTTMIIGhvLPDKETSLVD--AYEKCRGLADPKVCCDYALHV 132
Cdd:cd01318 1 GLLILPGVIDIHVHFRE--PGLTYKEDFVSGSRAAAAGGVTTVMD--MPNTKPPTTTaeALYEKLRLAAAKSVVDYGLYF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 133 GITwwaPKVKAEMetlVREKGVNSFQMFM--TYKDLyMLRDSELYQVLHACKDIGAiarVHAENGELVAEGAKEALDLGI 210
Cdd:cd01318 77 GVT---GSEDLEE---LDKAPPAGYKIFMgdSTGDL-LDDEETLERIFAEGSVLVT---FHAEDEDRLRENRKELKGESA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 211 tgpegIEISRPEELEAEATHRVITIANRTHCPIYLVNVSSisaGDVIAAAKMQGKVVLAETTTAHATLTglhyyHQDWSH 290
Cdd:cd01318 147 -----HPRIRDAEAAAVATARALKLARRHGARLHICHVST---PEELKLIKKAKPGVTVEVTPHHLFLD-----VEDYDR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 291 AAAYVTV-PPLRlDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKAMGKEDftkIPHGVSGVQDRMSVI---WERGVVGG 366
Cdd:cd01318 214 LGTLGKVnPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILSL 289
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478292 367 KmdenRFVAVTSSNAAKLLNLyPRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRG 443
Cdd:cd01318 290 S----RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
11-450 |
4.56e-36 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 140.06 E-value: 4.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 11 LIKGGKVVNDDCTHEADVYIENGIIQQVGrELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTKAAL 90
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIG-DLSGASAGEVIDCRGLHVLPGVIDSQVHFREPGL--EHKEDLETGSRAAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 91 VGGTTMIIGhvLPDKE--TSLVDAYEKCRGLADPKVCCDYALHVGITwwaPKVKAEMETLVREKGVNSFQMFM--TYKDL 166
Cdd:PRK09060 85 LGGVTAVFE--MPNTNplTTTAEALADKLARARHRMHCDFAFYVGGT---RDNADELAELERLPGCAGIKVFMgsSTGDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 167 YMLRDSELYQVLhacKDIGAIARVHAENGELVAEGAKEAldlgITG-PEGIEISRPEELEAEATHRVITIANRTHCPIYL 245
Cdd:PRK09060 160 LVEDDEGLRRIL---RNGRRRAAFHSEDEYRLRERKGLR----VEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIHV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 246 VNVSSISAGDVIAAAKmqgKVVLAETTTAHATLTGLHYYHQDWSHAaayVTVPPLRlDTNTSTYLMSLLANDTLNIVASD 325
Cdd:PRK09060 233 LHVSTAEEIDFLADHK---DVATVEVTPHHLTLAAPECYERLGTLA---QMNPPIR-DARHRDGLWRGVRQGVVDVLGSD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 326 HRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVIWERgVVGGKMDENRFVAVTSSNAAKLLNLyPRKGRIIPGADADVVVW 405
Cdd:PRK09060 306 HAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADFTIV 380
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1370478292 406 DPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENG 450
Cdd:PRK09060 381 DLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDG 425
|
|
| PLN02795 |
PLN02795 |
allantoinase |
15-450 |
6.40e-34 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 134.90 E-value: 6.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 15 GKVVNDDCTHEADVYIENGIIQQVGRELMIPG---GAKVIDATGKLVIPGGIDTstHFHQTFMNATCVDDFYHGTKAALV 91
Cdd:PLN02795 51 KRVVTPAGVIPGAVEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDV--HVHLNEPGRTEWEGFPTGTKAAAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 92 GGTTMIIGHVL-PDKETSLVDAYEKCRGLADPKvccdyaLHVGITWWAPKV------KAEMETLVrEKGVNSFQMFMT-- 162
Cdd:PLN02795 129 GGITTLVDMPLnSFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVpenahnASVLEELL-DAGALGLKSFMCps 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 163 -YKDLYMLRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLgiTGPEGIEISRPEELEAEATHRVITIANRTH- 240
Cdd:PLN02795 202 gINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAIRQLLEVAKDTRp 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 241 ------CPIYLVNVS-SISAGDVIAAAKMQGKVVLAETTTahatltglHYYhqdwSHAAA--------YVTVPPLRLDTN 305
Cdd:PLN02795 280 ggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYKCAPPIRDAAN 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 306 TSTyLMSLLANDTLNIVASDHRPFTTKQKAMGKEDFTKIPHGVSGVQDRMSVIWERGVVGGkMDENRFVAVTSSNAAKLL 385
Cdd:PLN02795 348 REL-LWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLA 425
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478292 386 NLyPRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNL--YENMRCHGVPLVTISRGRVVYENG 450
Cdd:PLN02795 426 GL-DSKGAIAPGKDADIVVWDPEAEFVLDESYPIYHKHKSLspYLGTKLSGKVIATFVRGNLVFLEG 491
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
10-463 |
1.52e-31 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 127.28 E-value: 1.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHEADVYIENGIIQQVGRELmiPGGAKVIDATGKLVIPGGIDTstHFHQTFMNATCVDDFYHGTKAA 89
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDA--HTHISEPGRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 90 LVGGTTMIIGHVLPD-----KETSLVDAYEKCRGladpKVCCDYALHVGITWWAPKVKAEMEtlvrEKGVNSFQMFMTY- 163
Cdd:PRK08044 81 AKGGITTMIEMPLNQlpatvDRASIELKFDAAKG----KLTIDAAQLGGLVSYNLDRLHELD----EVGVVGFKCFVATc 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 164 ------KDLYMLRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGPEGIEISRPEELEAEATHRVITIAN 237
Cdd:PRK08044 153 gdrgidNDFRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 238 RTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTahatltglHYYHQDWSHAAAYVTV----PPLRlDTNTSTYLMSL 313
Cdd:PRK08044 233 VAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTLakcsPPIR-DLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 314 LANDTLNIVASDHRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLyPRKGR 393
Cdd:PRK08044 304 LFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGR 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 394 IIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVFMCAEGTGKFCP 463
Cdd:PRK08044 380 IAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFIL 449
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
15-450 |
3.26e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 110.63 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 15 GKVVNDDCTHEADVYIENGIIQQVGRELMipGGAKVIDATGKLVIPGGIDTSTHFHQtfMNATCVDDFYHGTKAALVGGT 94
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLRD--FEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 95 TMIIGhvLPDKETSLVDA--YEKCRGLADPKVCCDYALHVGITWWAPKVKAEMETLvrekgvnsfqmfmtYKDLYMLRDS 172
Cdd:PRK04250 80 TLVFD--MPNTKPPIMDEktYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADF--------------YKIFMGASTG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 173 ELY----QVLHACkdIGAIARVHAENGELVAEgakealdlgitGPEgieisRPEELEAEATHRVITIANRTHCPIYLVNV 248
Cdd:PRK04250 144 GIFsenfEVDYAC--APGIVSVHAEDPELIRE-----------FPE-----RPPEAEVVAIERALEAGKKLKKPLHICHI 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 249 SSISAGDVIAAAKMQgkVVLAETTTAHATLTglhyyHQDWSHAAAYVTVPPLRldtnTSTYLMSLLAN-DTLNIVASDHR 327
Cdd:PRK04250 206 STKDGLKLILKSNLP--WVSFEVTPHHLFLT-----RKDYERNPLLKVYPPLR----SEEDRKALWENfSKIPIIASDHA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 328 PFTTKQKAMGKEdftkiphGVSGVQDRMSVIWErGVVGGKMDENRFVAVTSSNAAKLLNlYPRKGrIIPGADADVVVWDP 407
Cdd:PRK04250 275 PHTLEDKEAGAA-------GIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDM 344
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1370478292 408 EATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENG 450
Cdd:PRK04250 345 KKEWTIKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDD 387
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
9-452 |
1.78e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 109.38 E-value: 1.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 9 RILIKGGKVVNDDCTHE-ADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMnaTCVDDFYHGTK 87
Cdd:PRK07575 4 SLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREPGL--EHKEDLFTASR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 88 AALVGGTTMIIGHVLPDKETSLVDAYEKCRGLADPKVCCDYALHVGITwwaPKVKAEMETLVREKGVNSFQMFMTyKDLY 167
Cdd:PRK07575 82 ACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT---PDNLPELLTANPTCGIKIFMGSSH-GPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 168 MLRDSELYQVLHACKDIgaIArVHAENGELVAEGAKEAldLGITGPEGIEISRPEELEAEATHRVITIANRTHCPIYLVN 247
Cdd:PRK07575 158 VDEEAALERIFAEGTRL--IA-VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQRRLHILH 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 248 VSSISAGDVIAAAKmqGKVVLAETTTAHATLTglhyyhqdwshAAAYVTV-------PPLRlDTNTSTYLMSLLANDTLN 320
Cdd:PRK07575 233 LSTAIEAELLRQDK--PSWVTAEVTPQHLLLN-----------TDAYERIgtlaqmnPPLR-SPEDNEALWQALRDGVID 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 321 IVASDHRPFTTKQKAmgkEDFTKIPHGVSGVQDRMSVIWERgVVGGKMDENRFVAVTSSNAAKLLNLyPRKGRIIPGADA 400
Cdd:PRK07575 299 FIATDHAPHTLEEKA---QPYPNSPSGMPGVETSLPLMLTA-AMRGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDA 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1370478292 401 DVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYENGVF 452
Cdd:PRK07575 374 DLVLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
25-463 |
8.98e-23 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 100.70 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 25 EADVYIENGIIQQVGRELmipGGAKVIDATGkLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKAALVGGTTMIIGhvLPD 104
Cdd:PRK01211 15 YLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMD--MPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 105 KETSLVD--AYEKCRGLADPKVCCDYALHvgitwwapkvkaEMET----LVREKGVNSFQMFM---TYKDLYMLRDSELY 175
Cdd:PRK01211 87 NNIPIKDynAFSDKLGRVAPKAYVDFSLY------------SMETgnnaLILDERSIGLKVYMggtTNTNGTDIEGGEIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 176 QVlhacKDIGAIARVHAENGELVAEGAKEALDLgitgpEGIEISRPEELEAEATHRVITIANRTHcpiYLVNVSSIsagD 255
Cdd:PRK01211 155 KI----NEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLKTK---IIAHVSSI---D 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 256 VIAAakmqgkvVLAETTTAHATLtglhyyHQDWSHAAAYVTVPPLRlDTNTSTYLMSLLANDTLNIVASDHRPFTTKQKA 335
Cdd:PRK01211 220 VIGR-------FLREVTPHHLLL------NDDMPLGSYGKVNPPLR-DRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 336 mgkeDFTKIPHGVSGVQDRMSVIWERgVVGGKMDENRFVAVTSSNAAKLLNLypRKGRIIPGADADVVVWDPEATKTISA 415
Cdd:PRK01211 286 ----EFEYAKSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKIND 358
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1370478292 416 STQVQGGDFNLYENMRCHgVPLVTISRGRVVYENGVFMcAEGTGKFCP 463
Cdd:PRK01211 359 KRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYELI-SERTGKFVP 404
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
9-450 |
1.19e-19 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 91.86 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 9 RILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTfmNATCVDDFYHGTKA 88
Cdd:PRK09236 3 RILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESRA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 89 ALVGGTT--MIIGHVLPdkETSLVDAYEKCRGLADPKVCCDYALHVGITwwapkvKAEMETLVR--EKGVNSFQMFMTYK 164
Cdd:PRK09236 81 AVAGGITsfMEMPNTNP--PTTTLEALEAKYQIAAQRSLANYSFYFGAT------NDNLDEIKRldPKRVCGVKVFMGAS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 165 DLYMLRDSElyQVLHAC-KDIGAIARVHAENGELVAEGAKEAL-----DLGITGPEGIeisRPEELEAEATHRVITIANR 238
Cdd:PRK09236 153 TGNMLVDNP--ETLERIfRDAPTLIATHCEDTPTIKANLAKYKekygdDIPAEMHPLI---RSAEACYKSSSLAVSLAKK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 239 THCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHatltgLHYYHQDWSHAAAYVTVPPLRLDTNTSTYLMSLLANDT 318
Cdd:PRK09236 228 HGTRLHVLHISTAKELSLFENGPLAEKRITAEVCVHH-----LWFDDSDYARLGNLIKCNPAIKTASDREALRQALADDR 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 319 LNIVASDHRPFTTKQKAMGkedFTKIPHGVSGVQDRMSVIWERgVVGGKMDENRFVAVTSSNAAKLLNLyPRKGRIIPGA 398
Cdd:PRK09236 303 IDVIATDHAPHTWEEKQGP---YFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILFDI-KERGFIREGY 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370478292 399 DADVVVWDPEATKTISAstqvqggDFNLYenmRCHGVPLV----------TISRGRVVYENG 450
Cdd:PRK09236 378 WADLVLVDLNSPWTVTK-------ENILY---KCGWSPFEgrtfrsrvatTFVNGQLVYHNG 429
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-419 |
2.40e-16 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 81.16 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 3 ANSASVRILIKGGKVV---NDDCTHEADVYIENGIIQQVGR--ELMIPGGAKVIDATGKLVIPGGIDTSTH--------- 68
Cdd:COG1228 3 APAQAGTLLITNATLVdgtGGGVIENGTVLVEDGKIAAVGPaaDLAVPAGAEVIDATGKTVLPGLIDAHTHlglgggrav 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 69 -FHQTFMNATCVDDFYHGTK---AALVGGTTMIigHVLPDKETSLVDAYE--KCRGLADPKV-CCDYALHVGITWWApKV 141
Cdd:COG1228 83 eFEAGGGITPTVDLVNPADKrlrRALAAGVTTV--RDLPGGPLGLRDAIIagESKLLPGPRVlAAGPALSLTGGAHA-RG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 142 KAEMETLVRE---KGVNSFQMFMTYKDLYMLRDsELYQVLHACKDIGAIARVHAENgelvAEGAKEALDLGITgpeGIEi 218
Cdd:COG1228 160 PEEARAALREllaEGADYIKVFAEGGAPDFSLE-ELRAILEAAHALGLPVAAHAHQ----ADDIRLAVEAGVD---SIE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 219 srpeeleaeathrvitianrtHCpIYLVNvssisagDVIAAAKMQGKVVLaeTTTAHATLTGLHYYHQDWSHAAAYV--- 295
Cdd:COG1228 231 ---------------------HG-TYLDD-------EVADLLAEAGTVVL--VPTLSLFLALLEGAAAPVAAKARKVrea 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 296 TVPPLRLdtntstylmsLLANDTLNIVASDHrpfttkqkamgkedFTKIPHGVS-------GVQDRMS---VIWergvvg 365
Cdd:COG1228 280 ALANARR----------LHDAGVPVALGTDA--------------GVGVPPGRSlhrelalAVEAGLTpeeALR------ 329
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1370478292 366 gkmdenrfvAVTsSNAAKLLNLYPRKGRIIPGADADVVVWDPEATKTISASTQV 419
Cdd:COG1228 330 ---------AAT-INAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAYLEDV 373
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
9-449 |
1.27e-14 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 75.87 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 9 RILIKGGKVVNDDCTHE--ADVYIENGIIQQVGRelmIPGG---AKVIDATGKLVIPGGIDTSTHFHQTFMNatcvddfY 83
Cdd:PRK07627 2 KIHIKGGRLIDPAAGTDrqADLYVAAGKIAAIGQ---APAGfnaDKTIDASGLIVCPGLVDLSARLREPGYE-------Y 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 84 HGT-----KAALVGGTTMIIghVLPDK-----ETSLVDAYE-KCRGLADPKVCCDYALHVGItwwAPKVKAEMETLVrEK 152
Cdd:PRK07627 72 KATlesemAAAVAGGVTSLV--CPPDTdpvldEPGLVEMLKfRARNLNQAHVYPLGALTVGL---KGEVLTEMVELT-EA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 153 GVNSFqmfmTYKDLYMLRDSELYQVLHACKDIGAIARVHAE-----NGELVAEGAKeALDLGITGPegieisrPEELEAE 227
Cdd:PRK07627 146 GCVGF----SQANVPVVDTQVLLRALQYASTFGFTVWLRPLdaflgRGGVAASGAV-ASRLGLSGV-------PVAAETI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 228 ATHRVITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHATLTGLHYYHQDwshaAAYVTVPPLRLDTNTS 307
Cdd:PRK07627 214 ALHTIFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDIGYFD----SQFRLDPPLRSQRDRE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 308 TyLMSLLANDTLNIVASDHRPFTTKQKAMgkeDFTKIPHGVSGVQDRMS--VIWERGVvggKMDENRFVAVTSSNAAKLL 385
Cdd:PRK07627 290 A-IRAALADGTIDAICSDHTPVDDDEKLL---PFAEATPGATGLELLLPltLKWADEA---KVPLARALARITSAPARVL 362
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370478292 386 NLypRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYEN 449
Cdd:PRK07627 363 GL--PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFER 424
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
26-417 |
5.12e-14 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 74.25 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 26 ADVYIENGIIQQVGRELM-IPGGAKVIDATGKLVIPGGIDTSTHFHQ-------TFMNATcvddfyhgtKAALVGGTTMI 97
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEpgfeereTLASLA---------AAAAAGGFTRV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 98 IghVLPDKE-----TSLVDAYEKcRGLADPKVCCDyalhvgitWWAP---KVKAEMETLVRE---KGVNSFQMFMTYKDL 166
Cdd:PRK07369 93 A--ILPDTFppldnPATLARLQQ-QAQQIPPVQLH--------FWGAltlGGQGKQLTELAElaaAGVVGFTDGQPLENL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 167 YMLRdselyQVLHACKDIGAIARVHAENGELVAEG-AKE---ALDLGITGpegieisRPEELEAEATHRVITIANRTHCP 242
Cdd:PRK07369 162 ALLR-----RLLEYLKPLGKPVALWPCDRSLAGNGvMREgllALRLGLPG-------DPASAETTALAALLELVAAIGTP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 243 IYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHATLT--GLHYYHqdwshaaayvtvPPLRLDT---NTS--TYLMSLLA 315
Cdd:PRK07369 230 VHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDteALASYD------------PNLRLDPplgNPSdrQALIEGVR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 316 NDTLNIVASDHRPFTTKQKAMGkedFTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLYPRkgRII 395
Cdd:PRK07369 298 TGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP--SLA 372
|
410 420
....*....|....*....|..
gi 1370478292 396 PGADADVVVWDPEATKTISAST 417
Cdd:PRK07369 373 PGQPAELILFDPQKTWTVSAQT 394
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
27-448 |
8.59e-14 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 73.53 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 27 DVYIENGIIQQVGRELM---IPGGAKVIDATGKLVIPGGIDTSTHF------H-QTFMNATcvddfyhgtKAALVGGTTM 96
Cdd:PRK09059 24 TVLIEDGVIVAAGKGAGnqgAPEGAEIVDCAGKAVAPGLVDARVFVgepgaeHrETIASAS---------RAAAAGGVTS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 97 IIghVLPD------------------KETSLVDAYEKC---RGLADpkvccdyalhvgitwwapkvkAEMET--LVREKG 153
Cdd:PRK09059 95 II--MMPDtdpviddvalvefvkrtaRDTAIVNIHPAAaitKGLAG---------------------EEMTEfgLLRAAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 154 VNSF-QMFMTYKDLYMLRDSELYqvlhaCKDIGAIARVHAENGELVAEGA-KEALDLGITGPEGIeisrPEELEAEATHR 231
Cdd:PRK09059 152 AVAFtDGRRSVANTQVMRRALTY-----ARDFDAVIVHETRDPDLGGNGVmNEGLFASWLGLSGI----PREAEVIPLER 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 232 VITIANRTHCPIYLVNVSSISAGDVIAAAKMQGKVVLAETTTAHATLtglhyyhqDWSHAAAYVT----VPPLRLDTNTS 307
Cdd:PRK09059 223 DLRLAALTRGRYHAAQISCAESAEALRRAKDRGLKVTAGVSINHLSL--------NENDIGEYRTffklSPPLRTEDDRV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 308 TyLMSLLANDTLNIVASDHRPFTTKQKAMgkeDFTKIPHGVSGVQDRMSVIWeRGVVGGKMDENRFVAVTSSNAAKLLNL 387
Cdd:PRK09059 295 A-MVEAVASGTIDIIVSSHDPQDVDTKRL---PFSEAAAGAIGLETLLAAAL-RLYHNGEVPLLRLIEALSTRPAEIFGL 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370478292 388 ypRKGRIIPGADADVVVWDPEATKTISASTQVQGGDFNLYENMRCHGVPLVTISRGRVVYE 448
Cdd:PRK09059 370 --PAGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVYE 428
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
30-448 |
4.08e-13 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 71.27 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 30 IENGIIQQVGRELmipGGAKVIDATGKLVIPGGIDTSTHFHQTFMNAtcvDDFYHGTKAALVGGttmiIGHVL--PDKET 107
Cdd:PRK08417 3 IKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVSLKNDSLSS---KNLKSLENECLKGG----VGSIVlyPDSTP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 108 SLVDAYE---KCRGLADPKVCCDYALHVgitwWAPKVK-AEMETLVReKGVNSFQMFMTYKDLYMLRDSELYQVLHA--- 180
Cdd:PRK08417 73 AIDNEIAlelINSAQRELPMQIFPSIRA----LDEDGKlSNIATLLK-KGAKALELSSDLDANLLKVIAQYAKMLDVpif 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 181 --CKDIGAIARVHAENGELVAEgakealdLGITGpegieISRPEELEAEAthRVITIANRTHCPIYLVNVSSISAGDVIA 258
Cdd:PRK08417 148 crCEDSSFDDSGVMNDGELSFE-------LGLPG-----IPSIAETKEVA--KMKELAKFYKNKVLFDTLALPRSLELLD 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 259 AAKMQGKVVLAETTTAHATLtglhyyhqDWSHAAAYVTV----PPLRlDTNTSTYLMSLLANDTLNIVASDHRPfttkqK 334
Cdd:PRK08417 214 KFKSEGEKLLKEVSIHHLIL--------DDSACENFNTAaklnPPLR-SKEDRLALLEALKEGKIDFLTSLHSA-----K 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 335 AMGKED--FTKIPHGVSGVQDRMSVIWERGVVGGKMDENRFVAVTSSNAAKLLNLypRKGRIIPGADADVVVWDPEATKT 412
Cdd:PRK08417 280 SNSKKDlaFDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPNESTI 357
|
410 420 430
....*....|....*....|....*....|....*.
gi 1370478292 413 ISASTQVQGGDfNLYENMRCHgvplvtISRGRVVYE 448
Cdd:PRK08417 358 IDDNFSLYSGD-ELYGKIEAV------IIKGKLYLE 386
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
57-446 |
1.15e-12 |
|
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: 69.07 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 57 LVIPGGIDTSTHFHQTFMNATCVDDFY------HGTKAALVGGTTMIIGH--VLPDKETSLVDAYEKCR-----GLADPK 123
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEFayealrLGITTMLKSGTTTVLDMgaTTSTGIEALLEAAEELPlglrfLGPGCS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 124 VCCDYALHVGITWWaPKVKAEMETLVREKGVNSFQMFMTYKDlYMLRDSELYQVLHACKDIGAIARVHAENGELVAEGAK 203
Cdd:pfam01979 81 LDTDGELEGRKALR-EKLKAGAEFIKGMADGVVFVGLAPHGA-PTFSDDELKAALEEAKKYGLPVAIHALETKGEVEDAI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 204 EAldlgitgpegieisrpeeleaeathrvitIANRTHCPIYLVNVSSISAGDVIAAAKMQG---KVVLAETTTAHATLTG 280
Cdd:pfam01979 159 AA-----------------------------FGGGIEHGTHLEVAESGGLLDIIKLILAHGvhlSPTEANLLAEHLKGAG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 281 LhyyhqdwshaaAYVTVPPLRLDTNTSTyLMSLLANDTLNIVASDHRpfttkqkAMGkedftkiphGVSGVQDRMSV-IW 359
Cdd:pfam01979 210 V-----------AHCPFSNSKLRSGRIA-LRKALEDGVKVGLGTDGA-------GSG---------NSLNMLEELRLaLE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 360 ERGVVGGKMDENRFVAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDPEATKTISASTqvqggdfnlyenmrCHGVPLVT 439
Cdd:pfam01979 262 LQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGLK--------------PDGNVKKV 327
|
....*..
gi 1370478292 440 ISRGRVV 446
Cdd:pfam01979 328 IVKGKIV 334
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
10-121 |
4.74e-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: 64.92 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHE---ADVYIENGIIQQVGR--ELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFM---------- 74
Cdd:cd01298 1 ILIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPalPLPAYPADEVIDAKGKVVMPGLVNTHTHLAMTLLrgladdlplm 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370478292 75 -----------NATCVDDFYHGTKAALV----GGTTMIIGHVLPDKETsLVDAYEK-------CRGLAD 121
Cdd:cd01298 81 ewlkdliwpleRLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDA-VAEAAEElgiravlGRGIMD 148
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
10-68 |
9.54e-11 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 63.72 E-value: 9.54e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370478292 10 ILIKGGKVVNDDCTHEA--DVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVH 61
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
9-151 |
2.32e-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: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 9 RILIKGGKVVNDDCTHE----ADVYIENGIIQQVGRELMIP---GGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVD- 80
Cdd:COG0402 1 DLLIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGLADDl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 81 --------------------DFYHGTKAALV----GGTTMI--IGHVLPDKETSLVDAYEKC--RGLAdPKVCCDYALHV 132
Cdd:COG0402 81 plldwleeyiwplearldpeDVYAGALLALAemlrSGTTTVadFYYVHPESADALAEAAAEAgiRAVL-GRGLMDRGFPD 159
|
170
....*....|....*....
gi 1370478292 133 GITWWAPKVKAEMETLVRE 151
Cdd:COG0402 160 GLREDADEGLADSERLIER 178
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
11-461 |
6.66e-10 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 61.32 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 11 LIKGGKVVNDDCtheadVYIENGIIQQVgRELMiPGGAKVIDAT-GKLVIPGGIDTstHFHQTFMNATCVDDFYHGTKAA 89
Cdd:PRK00369 4 WIKGKAYLGKEI-----KEICINFDRRI-KEIK-SRCKPDLDLPqGTLILPGAIDL--HVHLRGLKLSYKEDVASGTSEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 90 LVGGTTMIIGH-----VLPDKETslvdAYEKCRGLADpKVCCDYALHVGItwwaPKVKAEMETLvrekGVNSFQMFMtyK 164
Cdd:PRK00369 75 AYGGVTLVADMpntipPLNTPEA----ITEKLAELEY-YSRVDYFVYSGV----TKDPEKVDKL----PIAGYKIFP--E 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 165 DLymLRDSELYQVLHACKdigaIARVHAENGELVAEGAKEAldlgitgpegieisRPEELEAEATHRVITIANrthcpiy 244
Cdd:PRK00369 140 DL--EREETFRVLLKSRK----LKILHPEVPLALKSNRKLR--------------RNCWYEIAALYYVKDYQN------- 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 245 lVNVSSISAGDVIAAAKMQGKVVlaETTTAHATLTGLhyyhqdwSHAAAYVTvPPLRlDTNTSTYLMSLLAN-DTlniVA 323
Cdd:PRK00369 193 -VHITHASNPRTVRLAKELGFTV--DITPHHLLVNGE-------KDCLTKVN-PPIR-DINERLWLLQALSEvDA---IA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 324 SDHRPFTTKQKAMgkeDFTKIPHGVSGVQDRMSVIWERgVVGGKMDENRFVAVTSSNAAKLLNLypRKGRIIPGADADVV 403
Cdd:PRK00369 258 SDHAPHSSFEKLQ---PYEVCPPGIAALSFTPPFIYTL-VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFT 331
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1370478292 404 VWDPEATKTISASTQVQGGDFNLYENMRChgvPLVTISRGRVVYENGVFMCAEGTGKF 461
Cdd:PRK00369 332 VIQFEDWRYSTKYSKVIETPLDGFELKAS---VYATIVQGKLAYLEGEVFPVKGINPF 386
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-450 |
4.41e-09 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 58.94 E-value: 4.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 1 MLANSASVRILIKGGKVVNDDCTHEA--DVYIENGIIQQVGRELMipGGAKVIDATGKLVIPGGIDTSTHfhqtfmnATC 78
Cdd:PRK09061 12 MPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHAH-------GQS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 79 VDDfyHGTKaALVGGTTMI---IGhVLPdketsLVDAYEKCRGLADPkvccdyaLHVGI-TWWAPKVKAEMETLVREKGV 154
Cdd:PRK09061 83 VAA--YRMQ-AFDGVTTALeleAG-VLP-----VARWYAEQAGEGRP-------LNYGAsVGWTPARIAVLTGPQAEGTI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 155 NSFQMFMTYKDLYM--LRDSELYQVLHACK---DIGAIArVHAENGELVAEGAKEALDLG-ITGPEGI-------EISRP 221
Cdd:PRK09061 147 ADFGKALGDPRWQEraATPAELAEILELLEqglDEGALG-IGIGAGYAPGTGHKEYLELArLAARAGVptythvrYLSNV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 222 E-ELEAEATHRVITIANRTHCPIYLVNVSSISAGDV------IAAAKMQGKVVLAETT--TAHATLTGLHYYHQDWSH-- 290
Cdd:PRK09061 226 DpRSSVDAYQELIAAAAETGAHMHICHVNSTSLRDIdrclalVEKAQAQGLDVTTEAYpyGAGSTVVGAAFFDPGWLErm 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 291 -----AAAYV----------TVPPLRLDTNTSTYLMSLLAND--------------TLNIVASDHRPFTTKQKAMGKEDF 341
Cdd:PRK09061 306 glgygSLQWVetgerlltreELAKLRANDPGGLVLIHFLDEDnprdralldrsvlfPGAAIASDAMPWTWSDGTVYEGDA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 342 TKIPHGV------SGVQDRMSVIW--ERGVVGgkMDENrfVAVTSSNAAKLLNLY----PRKGRIIPGADADVVVWDPEa 409
Cdd:PRK09061 386 WPLPEDAvshprsAGTFARFLREYvrERKALS--LLEA--IRKCTLMPAQILEDSvpamRRKGRLQAGADADIVVFDPE- 460
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1370478292 410 tkTISastqvqggDFNLYENMR--CHGVPLVTISrGRVVYENG 450
Cdd:PRK09061 461 --TIT--------DRATFEDPNrpSEGVRHVLVN-GVPVVSNG 492
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
10-452 |
4.49e-09 |
|
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: 58.85 E-value: 4.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVndDCT----HEADVYIENGIIQQVGRELmIPGGAKVIDATGKLVIPGGIDTSTHFHQTFmnatcvddFYHG 85
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPIL-STSAREVIDAAGLVVAPGFIDVHTHYDGQV--------FWDP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 86 TKAALV--GGTTMIIGhvlpdkETSLVDAYEKCRGLADPK--VCCDYALHVGITWWAPKVKAEMETLVRE-KGVNSFQMF 160
Cdd:cd01297 71 DLRPSSrqGVTTVVLG------NCGVSPAPANPDDLARLImlMEGLVALGEGLPWGWATFAEYLDALEARpPAVNVAALV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 161 ----MTYKDLYMLR----DSELYQV---LHACKDIGAIA---------RVHAENGELV--AEGAKEAldlgiTGPEGIEI 218
Cdd:cd01297 145 ghaaLRRAVMGLDAreatEEELAKMrelLREALEAGALGistglayapRLYAGTAELValARVAARY-----GGVYQTHV 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 219 SRPEELEAEATHRVITIANRTHCPiylVNVSSISAGDVIAAAKMQGKVVLAEtttaHATLTGlhyyHQDWSHAAAYVTvp 298
Cdd:cd01297 220 RYEGDSILEALDELLRLGRETGRP---VHISHLKSAGAPNWGKIDRLLALIE----AARAEG----LQVTADVYPYGA-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 299 plrldtntstylmsLLANDTLNIVASDHRPFTTKQKAMGKedftkiPH-GVSGVQDRMSVIWERGvvGGKMDENRFVAVT 377
Cdd:cd01297 287 --------------GSEDDVRRIMAHPVVMGGSDGGALGK------PHpRSYGDFTRVLGHYVRE--RKLLSLEEAVRKM 344
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370478292 378 SSNAAKLLNLYPRkGRIIPGADADVVVWDPeATKTISASTQvqggDFNLYENmrchGVPLVTISrGRVVYENGVF 452
Cdd:cd01297 345 TGLPARVFGLADR-GRIAPGYRADIVVFDP-DTLADRATFT----RPNQPAE----GIEAVLVN-GVPVVRDGAF 408
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
9-81 |
4.01e-08 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 55.78 E-value: 4.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478292 9 RILIKGGKVVNDDCTH----EADVYIENGIIQQVGRELMiPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNATCVDD 81
Cdd:PRK08204 3 RTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPSIE-APDAEVVDARGMIVMPGLVDTHRHTWQSVLRGIGADW 78
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
11-95 |
4.59e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 55.11 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 11 LIKGGKVVNDDCTHE-ADVYIENGIIQQVGRelMIPGGAKVIDATGKLVIPGGIDtsTHFH----QTFMNATcVDDFYHG 85
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGP--GAEPDAEVIDLGGGYLAPGFID--LHVHggggVDFMDGT-PEALRTI 75
|
90
....*....|
gi 1370478292 86 TKAALVGGTT 95
Cdd:COG1820 76 ARAHARHGTT 85
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
10-68 |
7.89e-08 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 55.20 E-value: 7.89e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370478292 10 ILIKGGKVVndDCTHE-----ADVYIENG-IIQQVGRelmiPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:COG1229 3 LIIKNGRVY--DPANGidgevMDIAIKDGkIVEEPSD----PKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
9-72 |
1.25e-07 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 54.24 E-value: 1.25e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478292 9 RILIKGGKVVNDDCTHE---ADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK07228 2 TILIKNAGIVTMNAKREivdGDVLIEDDRIAAVGDRLDLEDYDDHIDATGKVVIPGLIQGHIHLCQT 68
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
10-68 |
3.98e-07 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 52.50 E-value: 3.98e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370478292 10 ILIKGGKVVNDDCTH--EADVYIENGIIQQVGRELMIPGGaKVIDATGKLVIPGGIDTSTH 68
Cdd:PRK08393 3 ILIKNGYVIYGENLKviRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTH 62
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
10-77 |
6.09e-07 |
|
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: 51.81 E-value: 6.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH--FHQTFMNAT 77
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHIHggGGADFMDGT 70
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
27-71 |
9.87e-07 |
|
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238632 [Multi-domain] Cd Length: 338 Bit Score: 50.79 E-value: 9.87e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1370478292 27 DVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQ 71
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQ 45
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
9-72 |
1.21e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 51.01 E-value: 1.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 9 RILIKGGKVV---NDDCTHEAD--VYIENGIIQQVGRELMIPG-GAKVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK08203 2 TLWIKNPLAIvtmDAARREIADggLVVEGGRIVEVGPGGALPQpADEVFDARGHVVTPGLVNTHHHFYQT 71
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
374-408 |
1.53e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 50.48 E-value: 1.53e-06
10 20 30
....*....|....*....|....*....|....*
gi 1370478292 374 VAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDPE 408
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
59-135 |
2.35e-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: 49.76 E-value: 2.35e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370478292 59 IPGGIDTSTHFHQtfMNATCVDDFYHGTKAALVGGTTMIigHVLPDKETSLVD--AYEKCRGLADPKVCCDYALHVGIT 135
Cdd:cd01316 5 LPGLIDVHVHLRE--PGATHKEDFASGTKAALAGGFTMV--RAMPNTNPSIVDvaSLKLVQSLAQAKARCDYAFSIGAT 79
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
10-74 |
1.21e-05 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 47.96 E-value: 1.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370478292 10 ILIKGGKVVNDDCTHE---ADVYIENGIIQQVGRelMIPGGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:PRK06380 3 ILIKNAWIVTQNEKREilqGNVYIEGNKIVYVGD--VNEEADYIIDATGKVVMPGLINTHAHVGMTAS 68
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
32-68 |
1.23e-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: 47.69 E-value: 1.23e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1370478292 32 NGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHSH 37
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
10-72 |
1.27e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 47.82 E-value: 1.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478292 10 ILIKGGKVVNDDC--THEADVYIENGIIQQVGRElmIPGGA-KVIDATGKLVIPGGIDTSTHFHQT 72
Cdd:PRK06038 4 IIIKNAYVLTMDAgdLKKGSVVIEDGTITEVSES--TPGDAdTVIDAKGSVVMPGLVNTHTHAAMT 67
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
10-73 |
1.47e-05 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 47.62 E-value: 1.47e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370478292 10 ILIKGGKVVNDDCTH----EADVYIENGIIQQVGRELMIPG---GAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:PRK07203 2 LLIGNGTAITRDPAKpvieDGAIAIEGNVIVEIGTTDELKAkypDAEFIDAKGKLIMPGLINSHNHIYSGL 72
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
10-98 |
1.89e-05 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 47.40 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 10 ILIKGGKVVNDdCTHE---ADVYIENGIIQQVGRElmIPGGAKVIDATGKLVIPGGIDTSTHFHQTFMNatcVDDFYhgt 86
Cdd:COG1001 7 LVIKNGRLVNV-FTGEileGDIAIAGGRIAGVGDY--IGEATEVIDAAGRYLVPGFIDGHVHIESSMVT---PAEFA--- 77
|
90
....*....|..
gi 1370478292 87 KAALVGGTTMII 98
Cdd:COG1001 78 RAVLPHGTTTVI 89
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
1-80 |
2.23e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 47.10 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 1 MLANSASVRILIKGGKV--VNDDC-THEAdVYIENGIIQQVG--RELM--IPGGAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:COG1574 1 MKLAAAAADLLLTNGRIytMDPAQpVAEA-VAVRDGRIVAVGsdAEVRalAGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
....*..
gi 1370478292 74 MNATCVD 80
Cdd:COG1574 80 LALLGVD 86
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
374-407 |
4.18e-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: 46.03 E-value: 4.18e-05
10 20 30
....*....|....*....|....*....|....
gi 1370478292 374 VAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDP 407
Cdd:cd00854 330 VRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDD 363
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
24-74 |
4.64e-05 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 45.95 E-value: 4.64e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1370478292 24 HEAD--VYIENGIIQQVG--RELM--IPGGAKVIDATGKLVIPGGIDTSTHFHQTFM 74
Cdd:PRK09228 28 YIEDglLLVEDGRIVAAGpyAELRaqLPADAEVTDYRGKLILPGFIDTHIHYPQTDM 84
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
12-68 |
5.43e-05 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 45.87 E-value: 5.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370478292 12 IKGGKVVndDCTHE-----ADVYIENGIIQQvgrELMIPGGAKVIDATGKLVIPGGIDTSTH 68
Cdd:cd01304 1 IKNGTVY--DPLNGingekMDIFIRDGKIVE---SSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
26-73 |
1.25e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 44.54 E-value: 1.25e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1370478292 26 ADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDTSTHFHQTF 73
Cdd:PRK05985 17 VDILIRDGRIAAIGPALAAPPGAEVEDGGGALALPGLVDGHIHLDKTF 64
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
28-69 |
1.70e-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: 44.17 E-value: 1.70e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1370478292 28 VYIENGIIQQVGRELMIPG----GAKVIDATGKLVIPGGIDTSTHF 69
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPApgpaAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
26-70 |
2.11e-04 |
|
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: 43.77 E-value: 2.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1370478292 26 ADVYIENGIIQQVGRELMIPGGAKVIDATGKLVIPGGIDtsTHFH 70
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVD--PHIH 57
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
49-447 |
3.55e-04 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 43.29 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 49 KVIDATGKLVIPGGIDTSTHFHQTFMNATCVDDFYHGTKAALVG------GTTMIIGH---------------------V 101
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLDGGGLNLRELRLPDVLPNAVVKGqagrtpKGRWLVGEgwdeaqfaetrfpyaladldeV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 102 LPDKE---------TSLVD--AYEKCRGLADPKVCCDYALHVGITWWAP------------------KVKAEMETLVRE- 151
Cdd:pfam07969 81 APDGPvllralhthAAVANsaALDLAGITKATEDPPGGEIARDANGEGLtgllregayalppllareAEAAAVAAALAAl 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 152 -----KGVNSFQMFMTYKDLY-MLRDSELYQVLHACKDIGAIARVHAENGELVAEGAKEALDLGITGP-----EGIEISR 220
Cdd:pfam07969 161 pgfgiTSVDGGGGNVHSLDDYePLRELTAAEKLKELLDAPERLGLPHSIYELRIGAMKLFADGVLGSRtaaltEPYFDAP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 221 ---PEELEAEATHRVITIANRTHCPIYLVnvsSISAGDVIAAAKMQGKVVLAETTTAHATLTglhyyHQDWSHAAAYVTV 297
Cdd:pfam07969 241 gtgWPDFEDEALAELVAAARERGLDVAIH---AIGDATIDTALDAFEAVAEKLGNQGRVRIE-----HAQGVVPYTYSQI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 298 PPLRldtntstylmSLLANDTLNIV-----ASDHRPFTTKQKAMGKED-FTKIPHGVS---------GVQDRMSVIW--- 359
Cdd:pfam07969 313 ERVA----------ALGGAAGVQPVfdplwGDWLQDRLGAERARGLTPvKELLNAGVKvalgsdapvGPFDPWPRIGaav 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 360 -----ERGVVGGKMDENRF---VAVTSSNAAKLLNLYPRKGRIIPGADADVVVWDPEATkTISASTqvqggdfnlyenmR 431
Cdd:pfam07969 383 mrqtaGGGEVLGPDEELSLeeaLALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPL-TVDPPA-------------I 448
|
490
....*....|....*.
gi 1370478292 432 CHGVPLVTISRGRVVY 447
Cdd:pfam07969 449 ADIRVRLTVVDGRVVY 464
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
376-408 |
1.45e-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: 41.22 E-value: 1.45e-03
10 20 30
....*....|....*....|....*....|...
gi 1370478292 376 VTSSNAAKLLNLYPrKGRIIPGADADVVVWDPE 408
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKD 361
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
9-64 |
2.53e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.55 E-value: 2.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1370478292 9 RILIKGGKVVNDDCTHEADVYIENGIIQQVGRELMIPGGAkvIDATGKLVIPGGID 64
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPGA--IDAEGDYLLPGLVD 56
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
376-460 |
3.61e-03 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 40.18 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 376 VTSSNAAKLLNLyPRKGRIIPGADADVVVWDPeatktisastQVQGGDFNLYENMrcHGVPLVTISRGRVVYENGVFMcA 455
Cdd:COG1229 437 MTRAGPAKALGL-ADRGHLGVGADADIAIYDI----------NPDDKDYEDIEKM--FSKPAYVIKDGEVVVKDGEIV-A 502
|
....*
gi 1370478292 456 EGTGK 460
Cdd:COG1229 503 TPQGR 507
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
26-99 |
4.35e-03 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 40.00 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370478292 26 ADVYIENGIIQQVGR-----------ELMIPG-GAKVIDATGKLVIPGGIDTSTHFhqtfmnaTCVDDFYHgtkaALVGG 93
Cdd:cd00375 83 ADIGIKDGRIVAIGKagnpdimdgvtPNMIVGpSTEVIAGEGKIVTAGGIDTHVHF-------ICPQQIEE----ALASG 151
|
....*.
gi 1370478292 94 TTMIIG 99
Cdd:cd00375 152 ITTMIG 157
|
|
| |
