|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
7-463 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 854.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 7 SKVIKGGTVITADRTFRADILIEDGKIAAIGDSlEGDEVIDASGCYVMPGGIDPHTHLQMPFMGTYSSDDFDTGTAAALA 86
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN-LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRAAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 87 GGTTMVVDFVLPDSEGNLLDALQEWFQKA-GKARTDYSFHMAITGWNERTFNEMAEVVKRGINTFKHFMAYKGALMVNDD 165
Cdd:PRK08323 81 GGTTTIIDFALQPKGQSLREALEAWHGKAaGKAVIDYGFHMIITDWNEVVLDEMPELVEEGITSFKLFMAYKGALMLDDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 166 EMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSCEQ 245
Cdd:PRK08323 161 ELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHVSCKE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 246 SHEAIRRARQKGMRVFGEPLIQHLTLDESEYHNRDWDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQ 325
Cdd:PRK08323 241 ALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRDKEHQDALWRGLQDGDLQVVATDHCPFCFEQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 326 KRY-GIGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWDPEATKK 404
Cdd:PRK08323 321 KKQlGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDPNATKT 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 479816250 405 ISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPGDGRFIEREPNGAVN 463
Cdd:PRK08323 401 ISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQAVV 459
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
8-451 |
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: 742.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 8 KVIKGGTVITADRTFRADILIEDGKIAAIGDSLEGD---EVIDASGCYVMPGGIDPHTHLQMPFMGTYSSDDFDTGTAAA 84
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPggvEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 85 LAGGTTMVVDFVLPDSEGNLLDALQEWFQKA-GKARTDYSFHMAITGWNERTFNEMAEVVKRGINTFKHFMAYKGALMVN 163
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKAdGKSVIDYGFHMIITDWTDSVIEELPELVKKGISSFKVFMAYKGLLMVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 164 DDEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSC 243
Cdd:cd01314 161 DEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVSS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 244 EQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYhNRDWDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTT 323
Cdd:cd01314 241 KEAADEIARARKKGLPVYGETCPQYLLLDDSDY-WKDWFEGAKYVCSPPLRPKEDQEALWDGLSSGTLQTVGSDHCPFNF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 324 EQKRYGIGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWDPEATK 403
Cdd:cd01314 320 AQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNAEK 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 479816250 404 KISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPGDG 451
Cdd:cd01314 400 TISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
8-456 |
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: 635.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 8 KVIKGGTVITADRTFRADILIEDGKIAAIGDSLEGD---EVIDASGCYVMPGGIDPHTHLQMPFMGTYSSDDFDTGTAAA 84
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPdavEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 85 LAGGTTMVVDFVLPDSEGNLLDALQEWFQKA-GKARTDYSFHMAITGWNERTFNEM-AEVVKRGINTFKHFMAYKGALMV 162
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAeGKSVIDYGFHMDITHWNDSVLEEHiPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 163 NDDEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVS 242
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 243 CEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYhNRDWDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAF- 321
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHY-DKPGFEGAKYVCSPPLREPEDQDALWSALSSGALQTVGSDHCTFn 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 322 TTEQKRYGIGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWDPEA 401
Cdd:TIGR02033 320 FAQKKAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPNR 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 479816250 402 TKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPGDGRFIER 456
Cdd:TIGR02033 400 TTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
9-482 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 617.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSLE-GDE--VIDASGCYVMPGGIDPHTHLQMPFMGTYSSDDFDTGTAAAL 85
Cdd:PLN02942 8 LIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKvPDDvrVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQAAAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 AGGTTMVVDFVLPdSEGNLLDALQEWFQKAGKARTDYSFHMAITGWNERTFNEMAEVVK-RGINTFKHFMAYKGALMVND 164
Cdd:PLN02942 88 AGGTTMHIDFVIP-VNGNLLAGYEAYEKKAEKSCMDYGFHMAITKWDDTVSRDMETLVKeKGINSFKFFMAYKGSLMVTD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 165 DEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSCE 244
Cdd:PLN02942 167 ELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVVHVMSI 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 245 QSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHNRDWDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTE 324
Cdd:PLN02942 247 DAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHCPFNST 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 325 QKRYGIGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWDPEATKK 404
Cdd:PLN02942 327 QKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNPNSTFT 406
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479816250 405 ISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPGDGRFIEREPNGAVNRALSQWKEIVAPRKVERSA 482
Cdd:PLN02942 407 ISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFSYLFDGIQKADAAYLSSLRAPVK 484
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
9-456 |
0e+00 |
|
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: 551.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSL---EGDEVIDASGCYVMPGGIDPHTHLQMPFMGtySSDDFDTGTAAAL 85
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLaapEAAEVIDATGLLVLPGLIDLHVHLREPGLE--HKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 AGGTTMVVDFVLPDSEGNLLDALQEWFQKA-GKARTDYSFHMAITGWNERTFNEMAEVVKRGINTFKHFMAYK-GALMVN 163
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAeEKALVDVGPHGALTKGLGENLAELGALAEAGAVAFKVFMGSDdGNPVLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 164 DDEMFASFQRCAELGAMPLVHAENGDIVAQLQaklMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSC 243
Cdd:COG0044 159 DGLLRRALEYAAEFGALVAVHAEDPDLIRGGV---MNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVST 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 244 EQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHnrdwDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTT 323
Cdd:COG0044 236 AEAVELIREAKARGLPVTAEVCPHHLTLTDEDLE----RYGTNFKVNPPLRTEEDREALWEGLADGTIDVIATDHAPHTL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 324 EQKRygiGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADADLVIWDPEATK 403
Cdd:COG0044 312 EEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADADLVLFDPDAEW 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 479816250 404 KISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPgDGRFIER 456
Cdd:COG0044 388 TVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGEP-RGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
8-458 |
1.12e-154 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 448.76 E-value: 1.12e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 8 KVIKGGTVITADRTFRADILIEDGKIAAIGDSL-EGDEVIDASGCYVMPGGIDPHTHLQMPF-MGTYSSDDFDTGTAAAL 85
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGLgPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVSAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 AGGTTMVVDFVLPDSEGNLLDALQEWFQKA-GKARTDYSFHMAITGWNERTFN-EMAEVVKRGINTFKHFMAYKGaLMVN 163
Cdd:PRK13404 86 FGGTTTVIPFAAQHRGQSLREAVEDYHRRAaGKAVIDYAFHLIVADPTEEVLTeELPALIAQGYTSFKVFMTYDD-LKLD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 164 DDEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSC 243
Cdd:PRK13404 165 DRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVHVSG 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 244 EQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHnRDWDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAF-- 321
Cdd:PRK13404 245 REAAEQIRRARGRGLKIFAETCPQYLFLTAEDLD-RPGMEGAKYICSPPPRDKANQEAIWNGLADGTFEVFSSDHAPFrf 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 322 -TTEQKRYGIGN--FTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWD 398
Cdd:PRK13404 324 dDTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWD 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 399 PEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPGDGRFIEREP 458
Cdd:PRK13404 404 PDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLARSL 463
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
9-454 |
9.45e-96 |
|
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: 296.51 E-value: 9.45e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSL---EGDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAAL 85
Cdd:cd01315 3 VIKNGRVVTPDGVREADIAVKGGKIAAIGPDIantEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 AGGTTMVVDFVLPDSEGNLLDA-LQEWFQKA-GKARTDYSFHMAITGWNertFNEMAEVVKRGINTFKHFMAYKGA---L 160
Cdd:cd01315 81 AGGITTIIDMPLNSIPPTTTVEnLEAKLEAAqGKLHVDVGFWGGLVPGN---LDQLRPLDEAGVVGFKCFLCPSGVdefP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 161 MVNDDEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGndGPEAHAY--SRPPEVEGEATNRAIMIADQAGVPLYV 238
Cdd:cd01315 158 AVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKG--KRDYRDYlaSRPVFTEVEAIQRILLLAKETGCRLHI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 239 VHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTL--DESEyhnrdwDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVAT 316
Cdd:cd01315 236 VHLSSAEAVPLIREARAEGVDVTVETCPHYLTFtaEDVP------DGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 317 DHCAFTTEQKRYGIGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVI 396
Cdd:cd01315 310 DHSPCTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVV 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479816250 397 WDPEATKKISA---KTQHSsidYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPgDGRFI 454
Cdd:cd01315 390 WDPEEEFTVDAedlYYKNK---ISPYVGRTLKGRVHATILRGTVVYQDGEVVGEP-LGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
51-431 |
1.14e-90 |
|
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: 279.66 E-value: 1.14e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 51 CYVMPGGIDPHTHLQMPFMGTYSsDDFDTGTAAALAGGTTMVVDFVLPDSEGNLLDALQEWFQKAGK-ARTDYSFHMAIt 129
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEEsSYVDFSFHAGI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 130 gWNERTFNEMAEVVKRGINTFKHFMAYKGALM--VNDDEMFASFQRCAELGAMPLVHAEngdivaqlqaklmaegndgpe 207
Cdd:cd01302 79 -GPGDVTDELKKLFDAGINSLKVFMNYYFGELfdVDDGTLMRTFLEIASRGGPVMVHAE--------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 208 ahaysrppevegeatnRAIMIADQAGVPLYVVHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYhNRDWDYAarr 287
Cdd:cd01302 137 ----------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESML-RLNGAWG--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 288 VMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQKRYGiGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTpNEFVA 367
Cdd:cd01302 197 KVNPPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKESG-KDIWKAPPGFPGLETRLPILLTEGVKRGLSL-ETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479816250 368 VTSTNIAKILNIYPqKGAVVPGADADLVIWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMT 431
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
9-455 |
5.31e-86 |
|
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: 271.56 E-value: 5.31e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSLEGD--EVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALA 86
Cdd:TIGR03178 3 IIRGGRVILPNGEREADVGVKGGKIAAIGPDILGPaaKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAAAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 87 GGTTMVVDFVLPDSEGNL-LDALQEWFQKA-GKARTDYSFHMAITGWNERTFNEMAEVvkrGINTFKHFMAYKGA---LM 161
Cdd:TIGR03178 81 GGITTYIDMPLNSIPATTtRASLEAKFEAAkGKLAVDVGFWGGLVPYNLDDLRELDEA---GVVGFKAFLSPSGDdefPH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 162 VNDDEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGndGPEAHAY--SRPPEVEGEATNRAIMIADQAGVPLYVV 239
Cdd:TIGR03178 158 VDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQG--GVGADAYlaSRPVFAEVEAIRRTLALAKVTGCRVHVV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 240 HVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHnrdwDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHC 319
Cdd:TIGR03178 236 HLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVP----DGGTLAKCAPPIRDLANQEGLWEALLNGLIDCVVSDHS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 320 AFTTEQKRygIGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADADLVIWDP 399
Cdd:TIGR03178 312 PCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDADFVFVDP 388
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 479816250 400 EATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPgDGRFIE 455
Cdd:TIGR03178 389 DESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQFIGAP-KGQLLL 443
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
9-455 |
7.06e-74 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 239.94 E-value: 7.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSLEG---DEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAAL 85
Cdd:PRK02382 5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGsssEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 AGGTTMVVDfvLPDSEGNLLDAlqEWF-QKAGKAR----TDYSFHMAITGwnerTFNEMAEVVKRGINTFKH-FMAYKGA 159
Cdd:PRK02382 83 AGGVTTVVD--QPNTDPPTVDG--ESFdEKAELAArksiVDFGINGGVTG----NWDPLESLWERGVFALGEiFMADSTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 160 LMVNDDEMFA-SFQRCAELGAMPLVHAENGDIvaQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYV 238
Cdd:PRK02382 155 GMGIDEELFEeALAEAARLGVLATVHAEDEDL--FDELAKLLKGDADADAWSAYRPAAAEAAAVERALEVASETGARIHI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 239 VHVSCEQSHEAIRRARqkgmrVFGEPLIQHLTLDEseyhnRDWDyaarRV-----MSPPFRDKLNQDSLWAGLAAGSLQC 313
Cdd:PRK02382 233 AHISTPEGVDAARREG-----ITCEVTPHHLFLSR-----RDWE----RLgtfgkMNPPLRSEKRREALWERLNDGTIDV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 314 VATDHCAFTTEQKRYGIGNftkIPNGTGGLEERMPVLwTRGVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADAD 393
Cdd:PRK02382 299 VASDHAPHTREEKDADIWD---APSGVPGVETMLPLL-LAAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEGYDAD 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 479816250 394 LVIWDPEATKKISAKTQHSSIDYNVFEGFElkGL-PIMTLSRGRIAFDKGQVTAKPGDGRFIE 455
Cdd:PRK02382 374 LVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLR 434
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
23-438 |
2.42e-71 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 232.33 E-value: 2.42e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 23 RADILIEDGKIAAIG--DSLEGDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALAGGTTMVVDfvLPDS 100
Cdd:TIGR00857 5 EVDILVEGGRIKKIGklRIPPDAEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVAD--MPNT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 101 EGNLLDALQ-EWFQKAGK--ARTDYSFHMAITGWNE----RTFNEMAEVVKRGINTFKHFMAykgalMVNDDEMFASFQR 173
Cdd:TIGR00857 81 KPPIDTPETlEWKLQRLKkvSLVDVHLYGGVTQGNQgkelTEAYELKEAGAVGRMFTDDGSE-----VQDILSMRRALEY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 174 CAELGAMPLVHAENGDIVAQlqaKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSCEQSHEAIRRA 253
Cdd:TIGR00857 156 AAIAGVPIALHAEDPDLIYG---GVMHEGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLELIVKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 254 RQKGMRVFGEPLIQHLTLDESEYHNRDWDYAarrvMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQKRYGIGNf 333
Cdd:TIGR00857 233 KSQGIKITAEVTPHHLLLSEEDVARLDGNGK----VNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKEFAA- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 334 tkIPNGTGGLEERMPVLWTRgVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADADLVIWDPEATKKISAKTQHSS 413
Cdd:TIGR00857 308 --APPGIPGLETALPLLLQL-LVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKEWTINAETFYSK 383
|
410 420
....*....|....*....|....*
gi 479816250 414 IDYNVFEGFELKGLPIMTLSRGRIA 438
Cdd:TIGR00857 384 AKNTPFEGMSLKGKPIATILRGKVV 408
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
9-458 |
8.78e-71 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 231.90 E-value: 8.78e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSLEGD--EVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALA 86
Cdd:PRK06189 6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSParEIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 87 GGTTMVVDFVLpDSEGNLLDALQEWFQKA---GKARTDYSFHMAITGWNERTFNEMAEvvkRGINTFKHFMAYKGAL--- 160
Cdd:PRK06189 84 GGCTTYFDMPL-NSIPPTVTREALDAKAElarQKSAVDFALWGGLVPGNLEHLRELAE---AGVIGFKAFMSNSGTDefr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 161 MVNDDEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVH 240
Cdd:PRK06189 160 SSDDLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPLHFVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 241 VSCEQSHEAIRRARQKGMRVFGE--PLIQHLTLDESEyhnrDWDYAARrvMSPPFRDKLNQDSLWAGLAAGSLQCVATDH 318
Cdd:PRK06189 240 ISSGKAVALIAEAKKRGVDVSVEtcPHYLLFTEEDFE----RIGAVAK--CAPPLRSRSQKEELWRGLLAGEIDMISSDH 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 319 CAFTTEQKRYgiGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADADLVIWD 398
Cdd:PRK06189 314 SPCPPELKEG--DDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVGADADFVLVD 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 399 PEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTaKPGDGRFIEREP 458
Cdd:PRK06189 391 LDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF-PPPRGQLLRPSV 449
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-431 |
1.14e-67 |
|
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: 221.34 E-value: 1.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 42 GDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALAGGTTMVVdfVLPD-----SEGNLLDALQEWFQKAG 116
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFTTVV--CMPNtnpviDNPAVVELLKNRAKDVG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 117 KARTdysFHM-AIT-GWNERTFNEMAEVVKrgintfkhfmayKGALMVNDD----EMFASFQRCAELGAM---PL-VHAE 186
Cdd:cd01317 77 IVRV---LPIgALTkGLKGEELTEIGELLE------------AGAVGFSDDgkpiQDAELLRRALEYAAMldlPIiVHPE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 187 NGDIVAQLQAklmaegNDGPEAHA---YSRPPEVEGEATNRAIMIADQAGVPLYVVHVSCEQSHEAIRRARQKGMRVFGE 263
Cdd:cd01317 142 DPSLAGGGVM------NEGKVASRlglPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKGLPVTAE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 264 PLIQHLTLDESEYhnRDWDYAARrvMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQKRYGignFTKIPNGTGGL 343
Cdd:cd01317 216 VTPHHLLLDDEAL--ESYDTNAK--VNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAPPGIIGL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 344 EERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPqkGAVVPGADADLVIWDPEATKKISAKTQHSSiDYNV-FEGF 422
Cdd:cd01317 289 ETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSK-SKNTpFDGQ 365
|
....*....
gi 479816250 423 ELKGLPIMT 431
Cdd:cd01317 366 KLKGRVLAT 374
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
7-439 |
1.26e-63 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 212.36 E-value: 1.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 7 SKVIKGGTVIT-ADRTFRADILIEDGKIAAIG--DSLEGDEVIDASGCYVMPGGIDPHTHLQMPfMGTYSSDdFDTGTAA 83
Cdd:PRK09357 2 MILIKNGRVIDpKGLDEVADVLIDDGKIAAIGenIEAEGAEVIDATGLVVAPGLVDLHVHLREP-GQEDKET-IETGSRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 84 ALAGGTTMVVdfVLP------DSEGnLLDALQEWFQKAGKARtdysFHM--AITgwNERTFNEMAEVVKrgintfkhfMA 155
Cdd:PRK09357 80 AAAGGFTTVV--AMPntkpviDTPE-VVEYVLDRAKEAGLVD----VLPvgAIT--KGLAGEELTEFGA---------LK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 156 YKGALMVNDDE--------MFASFQRCAELGaMPLV-HAENGDIVAQLQAklmaegNDGPEAHAYS---RPPEVEGEATN 223
Cdd:PRK09357 142 EAGVVAFSDDGipvqdarlMRRALEYAKALD-LLIAqHCEDPSLTEGGVM------NEGEVSARLGlpgIPAVAEEVMIA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 224 RAIMIADQAGVPLYVVHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHNRDWDYAarrvMSPPFRDKLNQDSLW 303
Cdd:PRK09357 215 RDVLLAEATGARVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYK----VNPPLRTEEDREALI 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 304 AGLAAGSLQCVATDHCAFTTEQKRygiGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPqk 383
Cdd:PRK09357 291 EGLKDGTIDAIATDHAPHAREEKE---CEFEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINPARILGLPA-- 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 479816250 384 GAVVPGADADLVIWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAF 439
Cdd:PRK09357 366 GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
9-454 |
3.67e-62 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 209.33 E-value: 3.67e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSL-EGDEVIDASGCYVMPGGIDPHTHLQMPFMGTYssDDFDTGTAAALAG 87
Cdd:PRK08044 6 IIKNGTVILENEARVVDIAVKGGKIAAIGQDLgDAKEVMDASGLVVSPGMVDAHTHISEPGRSHW--EGYETGTRAAAKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 88 GTTMVVDFVLpdsegNLLDA------LQEWFQKA-GKARTDYSFHMAITGWNERTFNEMAEVvkrGINTFKHFMAYKGA- 159
Cdd:PRK08044 84 GITTMIEMPL-----NQLPAtvdrasIELKFDAAkGKLTIDAAQLGGLVSYNLDRLHELDEV---GVVGFKCFVATCGDr 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 160 ------LMVNDDEMFASFQRCAELGAMPLVHAENGDIVAQLQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAG 233
Cdd:PRK08044 156 gidndfRDVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 234 VPLYVVHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHnrdwDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQC 313
Cdd:PRK08044 236 CRLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFE----EIGTLAKCSPPIRDLENQKGMWEKLFNGEIDC 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 314 VATDHCAFTTEQKRygiGNFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADAD 393
Cdd:PRK08044 312 LVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIAPGKDAD 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479816250 394 LVIWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKPGDGRFI 454
Cdd:PRK08044 388 FVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFI 448
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
50-435 |
2.19e-58 |
|
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: 196.79 E-value: 2.19e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 50 GCYVMPGGIDPHTHLQMPFMgTYSsDDFDTGTAAALAGGTTMVVDfvLPDSEGNLLDAlQEWFQK----AGKARTDYSFH 125
Cdd:cd01318 1 GLLILPGVIDIHVHFREPGL-TYK-EDFVSGSRAAAAGGVTTVMD--MPNTKPPTTTA-EALYEKlrlaAAKSVVDYGLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 126 MAITGwnertFNEMAEVVKRGINTFKHFMAYK-GALMVNDDEMFASFQRCAELGAmplVHAENGDIVAQLQAKLMAEGnd 204
Cdd:cd01318 76 FGVTG-----SEDLEELDKAPPAGYKIFMGDStGDLLDDEETLERIFAEGSVLVT---FHAEDEDRLRENRKELKGES-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 205 gpeAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSCEqshEAIRRARQKGMRVFGEPLIQHLTLDESEYHNRDwdya 284
Cdd:cd01318 146 ---AHPRIRDAEAAAVATARALKLARRHGARLHICHVSTP---EELKLIKKAKPGVTVEVTPHHLFLDVEDYDRLG---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 285 ARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQKRYGIGNftkIPNGTGGLEERMPVLWTRgVRTGRLTPNE 364
Cdd:cd01318 216 TLGKVNPPLRSREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMLTL-VNKGILSLSR 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479816250 365 FVAVTSTNIAKILNIyPQKGAVVPGADADLVIWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRG 435
Cdd:cd01318 292 VVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
9-459 |
8.10e-57 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 195.14 E-value: 8.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGD--SLEGDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALA 86
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIGDlsGASAGEVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 87 GGTTMVvdFVLPDSEGNLLDALQ-EWFQKAGKAR--TDYSFHMAITGWNertFNEMAEVVK-RGINTFKHFM-AYKGALM 161
Cdd:PRK09060 86 GGVTAV--FEMPNTNPLTTTAEAlADKLARARHRmhCDFAFYVGGTRDN---ADELAELERlPGCAGIKVFMgSSTGDLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 162 VNDDE-----MFASFQRCAelgamplVHAENGdivAQLQA-KLMAEGNDgPEAHAYSRPPEVEGEATNRAIMIADQAGVP 235
Cdd:PRK09060 161 VEDDEglrriLRNGRRRAA-------FHSEDE---YRLRErKGLRVEGD-PSSHPVWRDEEAALLATRRLVRLARETGRR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 236 LYVVHVSCEQSHEAIRRARQkgmRVFGEPLIQHLTLDESEYHNRDWDYAarrVMSPPFRDKLNQDSLWAGLAAGSLQCVA 315
Cdd:PRK09060 230 IHVLHVSTAEEIDFLADHKD---VATVEVTPHHLTLAAPECYERLGTLA---QMNPPIRDARHRDGLWRGVRQGVVDVLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 316 TDHCAFTTEQKRYgigNFTKIPNGTGGLEERMPVLWTRgVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADADLV 395
Cdd:PRK09060 304 SDHAPHTLEEKAK---PYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAVGYDADFT 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 479816250 396 IWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAkPGDG---RFIEREPN 459
Cdd:PRK09060 379 IVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGELVG-PPTGepvRFLETLPR 444
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
10-444 |
8.98e-55 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 189.50 E-value: 8.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 10 IKGGTVITADRTF-RADILIEDGKIAAIGDSL---EGDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAAL 85
Cdd:PRK07575 7 IRNARILLPSGELlLGDVLVEDGKIVAIAPEIsatAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTASRACA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 AGGTTMVVDfvLPD------SEGNLLDALQewfQKAGKARTDYSFHMAITGWNERTFNEMAEVVkrGIntfKHFM-AYKG 158
Cdd:PRK07575 85 KGGVTSFLE--MPNtkplttTQAALDDKLA---RAAEKCVVNYGFFIGATPDNLPELLTANPTC--GI---KIFMgSSHG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 159 ALMVNDDE----MFASFQRcaeLGAmplVHAENGDIVAQLQAKLmaEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGV 234
Cdd:PRK07575 155 PLLVDEEAalerIFAEGTR---LIA---VHAEDQARIRARRAEF--AGISDPADHSQIQDEEAALLATRLALKLSKKYQR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 235 PLYVVHVSCEQSHEAIRRArqKGMRVFGEPLIQHLTLDESEYHNrdwdYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCV 314
Cdd:PRK07575 227 RLHILHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAYER----IGTLAQMNPPLRSPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 315 ATDHCAFTTEQKRYGignFTKIPNGTGGLEERMPVLWTRGVRtGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADADL 394
Cdd:PRK07575 301 ATDHAPHTLEEKAQP---YPNSPSGMPGVETSLPLMLTAAMR-GKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADL 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 479816250 395 VIWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQV 444
Cdd:PRK07575 376 VLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRGQV 425
|
|
| PLN02795 |
PLN02795 |
allantoinase |
9-448 |
3.06e-51 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 181.51 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGD------SLEGDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTA 82
Cdd:PLN02795 47 VLYSKRVVTPAGVIPGAVEVEGGRIVSVTKeeeapkSQKKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFPTGTK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 83 AALAGGTTMVVDFVL-PDSEGNLLDALQEWFQKA-GKARTDYSFHMAITGWNERTFNEMAEVVKRGINTFKHFMAYKGA- 159
Cdd:PLN02795 125 AAAAGGITTLVDMPLnSFPSTTSVETLELKIEAAkGKLYVDVGFWGGLVPENAHNASVLEELLDAGALGLKSFMCPSGIn 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 160 --LMVNDDEMFASFQRCAELGAMPLVHAENGDIVAQlQAKLMAEGNDgPEAHAYSRPPEVEGEATNRAIMIADQA----- 232
Cdd:PLN02795 205 dfPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVES-DSRLDADPRS-YSTYLKSRPPSWEQEAIRQLLEVAKDTrpggv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 233 --GVPLYVVHVS-CEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHNRDWDYAArrvmSPPFRDKLNQDSLWAGLAAG 309
Cdd:PLN02795 283 aeGAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKC----APPIRDAANRELLWKALLDG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 310 SLQCVATDHCAFTTEQKRYGIGNFTKIPNGTGGLEERMPVLWTRGVRTGrLTPNEFVAVTSTNIAKILNIyPQKGAVVPG 389
Cdd:PLN02795 359 DIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLARWWSERPAKLAGL-DSKGAIAPG 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 479816250 390 ADADLVIWDPEATKKISAKT----QHSSIDynVFEGFELKGLPIMTLSRGRIAFDKGQVTAKP 448
Cdd:PLN02795 437 KDADIVVWDPEAEFVLDESYpiyhKHKSLS--PYLGTKLSGKVIATFVRGNLVFLEGKHAKQA 497
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
10-448 |
3.25e-45 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 163.89 E-value: 3.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 10 IKGGTVITADRTFRADILIEDGKIAAIGDSLE---GDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALA 86
Cdd:PRK09236 6 IKNARIVNEGKIFEGDVLIENGRIAKIASSISaksADTVIDAAGRYLLPGMIDDQVHFREP--GLTHKGDIASESRAAVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 87 GGTTMVVDfvLPDSEGNL--LDALQEWFQKA-GKARTDYSFHMAITgwnertfNEMAEVVKR-------GIntfKHFM-A 155
Cdd:PRK09236 84 GGITSFME--MPNTNPPTttLEALEAKYQIAaQRSLANYSFYFGAT-------NDNLDEIKRldpkrvcGV---KVFMgA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 156 YKGALMVNDDEMFASFQRCAELgaMPLVHAENGDIVAQLQAKLMAE-GNDGP-EAHAYSRPPEVEGEATNRAIMIADQAG 233
Cdd:PRK09236 152 STGNMLVDNPETLERIFRDAPT--LIATHCEDTPTIKANLAKYKEKyGDDIPaEMHPLIRSAEACYKSSSLAVSLAKKHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 234 VPLYVVHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHnrdwDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQC 313
Cdd:PRK09236 230 TRLHVLHISTAKELSLFENGPLAEKRITAEVCVHHLWFDDSDYA----RLGNLIKCNPAIKTASDREALRQALADDRIDV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 314 VATDHCAFTTEQKRygiGNFTKIPNGTGGLEERMPVLWTRgVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVPGADAD 393
Cdd:PRK09236 306 IATDHAPHTWEEKQ---GPYFQAPSGLPLVQHALPALLEL-VHEGKLSLEKVVEKTSHAPAILFDI-KERGFIREGYWAD 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 479816250 394 LVIWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKP 448
Cdd:PRK09236 381 LVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATTFVNGQLVYHNGQLVESC 435
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
13-448 |
4.06e-43 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 157.24 E-value: 4.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 13 GTVITADRTFRADILIEDGKIAAIGD-SLEGDEVIDASGCYVMPGGIDPHTHLQmPFMGTYSsDDFDTGTAAALAGGTTM 91
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLrDLKGKEVIKVKGGIILPGLIDVHVHLR-DFEESYK-ETIESGTKAALHGGITL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 92 VVDfvLPDSEGNLLDA-----LQEWFQKagKARTDYSFHMAITGWNERTFNEMAEVVKRgintfkHFMAYKGALMVNDde 166
Cdd:PRK04250 82 VFD--MPNTKPPIMDEktyekRMRIAEK--KSYADYALNFLIAGNCEKAEEIKADFYKI------FMGASTGGIFSEN-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 167 mFASFQRCAElgAMPLVHAENGDIVAQLqaklmaegndgPEahaysRPPEVEGEATNRAIMIADQAGVPLYVVHVSCEQS 246
Cdd:PRK04250 150 -FEVDYACAP--GIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTKDG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 247 HEAIRRARQKgmRVFGEPLIQHLTLDEseyhnRDWDYAARRVMSPPFRDKLNQDSLWAGLAagSLQCVATDHCAFTTEQK 326
Cdd:PRK04250 211 LKLILKSNLP--WVSFEVTPHHLFLTR-----KDYERNPLLKVYPPLRSEEDRKALWENFS--KIPIIASDHAPHTLEDK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 327 RYGIGnftkipnGTGGLEERMPVLWTrGVRTGRLTPNEFVAVTSTNIAKILNIyPQKGAVVpGADADLVIWDPEATKKIS 406
Cdd:PRK04250 282 EAGAA-------GIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFGI-KNYGIEE-GNYANFAVFDMKKEWTIK 351
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 479816250 407 AKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKP 448
Cdd:PRK04250 352 AEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEIIGKP 393
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
54-451 |
7.65e-33 |
|
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: 127.57 E-value: 7.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 54 MPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALAGGTTMVVdfVLPDSEGNLLDALQ-EWFQK--AGKARTDYSFHMAITG 130
Cdd:cd01316 5 LPGLIDVHVHLREP--GATHKEDFASGTKAALAGGFTMVR--AMPNTNPSIVDVASlKLVQSlaQAKARCDYAFSIGATS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 131 WNERTFNEMA-EVVKRGINTFKHFMAYKGALMVNDDEMFASFQrcaelGAMPLV-HAENGDIVAQLqakLMAEgndgpea 208
Cdd:cd01316 81 TNAATVGELAsEAVGLKFYLNETFSTLILDKITAWASHFNAWP-----STKPIVtHAKSQTLAAVL---LLAS------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 209 haysrppevegeATNRAIMIAdqagvplyvvHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHNRDWDYAARRv 288
Cdd:cd01316 146 ------------LHNRSIHIC----------HVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQYEVRPFL- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 289 mspPFRDklNQDSLWAGLAagSLQCVATDHCAFTTEQKRygiGNftKIPNGTGGLEERMPVLWTrGVRTGRLTPNEFVAV 368
Cdd:cd01316 203 ---PTRE--DQEALWENLD--YIDCFATDHAPHTLAEKT---GN--KPPPGFPGVETSLPLLLT-AVHEGRLTIEDIVDR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 369 TSTNIAKILNIYPQKGAVVpgaDADLviwDPEATkkISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFDKGQVTAKP 448
Cdd:cd01316 270 LHTNPKRIFNLPPQSDTYV---EVDL---DEEWT--IPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVAPP 341
|
...
gi 479816250 449 GDG 451
Cdd:cd01316 342 GFG 344
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
15-412 |
1.78e-31 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 125.48 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 15 VITADRtfRADILIEDGKIAAIGDSLEG----DEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALAGGTT 90
Cdd:PRK07369 15 VSNTDR--IADVLIEDGKIQAIEPHIDPippdTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 91 MVVdfVLPDSE-----GNLLDALQEWFQKAGKARTDysFHMAIT-GWNERTFNEMAEVVKRGINTFkhfmaykgalmvND 164
Cdd:PRK07369 91 RVA--ILPDTFppldnPATLARLQQQAQQIPPVQLH--FWGALTlGGQGKQLTELAELAAAGVVGF------------TD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 165 DEMFASF---QRCAE----LGAMPLVHAENgdivAQLQAK-LMAEGndgPEAHAYS---RPPEVEGEATNRAIMIADQAG 233
Cdd:PRK07369 155 GQPLENLallRRLLEylkpLGKPVALWPCD----RSLAGNgVMREG---LLALRLGlpgDPASAETTALAALLELVAAIG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 234 VPLYVVHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDE---SEYH-NRDWDyaarrvmsPPFRDKLNQDSLWAGLAAG 309
Cdd:PRK07369 228 TPVHLMRISTARSVELIAQAKARGLPITASTTWMHLLLDTealASYDpNLRLD--------PPLGNPSDRQALIEGVRTG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 310 SLQCVATDHCAFTTEQKRYGignFTKIPNGTGGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPqkGAVVPG 389
Cdd:PRK07369 300 VIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEP--PSLAPG 374
|
410 420
....*....|....*....|...
gi 479816250 390 ADADLVIWDPEATKKISAKTQHS 412
Cdd:PRK07369 375 QPAELILFDPQKTWTVSAQTLHS 397
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
25-459 |
3.89e-30 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 121.50 E-value: 3.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 25 DILIEDGKIAAIGDSLEGDEVIDASGCyVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALAGGTTMVVDfvLPDSEGNL 104
Cdd:PRK01211 17 EIEVEDGKIKSIKKDAGNIGKKELKGA-ILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGTTFIMD--MPNNNIPI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 105 LD--ALQEWFQK-AGKARTDYSFHMAITGWNertfnemAEVVKRGINTFKHFMA---YKGALMVNDDEMfasfQRCAELG 178
Cdd:PRK01211 92 KDynAFSDKLGRvAPKAYVDFSLYSMETGNN-------ALILDERSIGLKVYMGgttNTNGTDIEGGEI----KKINEAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 179 AMPLVHAENGDIV--AQLQAKLMAEgndgpeaHAYSRPPEVEGEATNraimiadqagvplYVVHVSCEQSHEAIRRARQK 256
Cdd:PRK01211 161 IPVFFHAELSECLrkHQFESKNLRD-------HDLARPIECEIKAVK-------------YVKNLDLKTKIIAHVSSIDV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 257 GMRVFGEPLIQHLTLdeseyhNRDWDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQKRygigNFTKI 336
Cdd:PRK01211 221 IGRFLREVTPHHLLL------NDDMPLGSYGKVNPPLRDRWTQERLLEEYISGRFDILSSDHAPHTEEDKQ----EFEYA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 337 PNGTGGLEERMPVLWTRgVRTGRLTPNEFVAVTSTNIAKILNIypQKGAVVPGADADLVIWDPEATKKISAKTQHSSIDY 416
Cdd:PRK01211 291 KSGIIGVETRVPLFLAL-VKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPV 367
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 479816250 417 NVFEGFELKgLPIMTLSRGRIAFDKGQVTAKPgDGRFIeREPN 459
Cdd:PRK01211 368 SPFNGFDAI-FPSHVIMRGEVVIDNYELISER-TGKFV-PKGG 407
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
26-437 |
2.99e-29 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 118.65 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 26 ILIEDGKIAAIGDSLEGDEVIDASGCYVMPGGIDPHTHlqmPFMGTYSSDDFDTGTAAALAGGTTMVVdfVLPDSEGNLL 105
Cdd:PRK08417 1 IRIKDGKITEIGSDLKGEEILDAKGKTLLPALVDLNVS---LKNDSLSSKNLKSLENECLKGGVGSIV--LYPDSTPAID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 106 DALQEWFQKAGKARTDYSFHMAITGWNER-TFNEMAEVVKRGIntfkhfmayKGALMVNDDEMFaSFQRCAELGAM---P 181
Cdd:PRK08417 76 NEIALELINSAQRELPMQIFPSIRALDEDgKLSNIATLLKKGA---------KALELSSDLDAN-LLKVIAQYAKMldvP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 182 L-VHAENGDIVaqlQAKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSCEQSHEAIRRARQKGMRV 260
Cdd:PRK08417 146 IfCRCEDSSFD---DSGVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNKVLFDTLALPRSLELLDKFKSEGEKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 261 FGEPLIQHLTLDESeyHNRDWDYAARrvMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQKRYGignFTKIPNGT 340
Cdd:PRK08417 223 LKEVSIHHLILDDS--ACENFNTAAK--LNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNSKKDLA---FDEAAFGI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 341 GGLEERMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIypQKGAVVPGADADLVIWDPEATKKISAKtqhssidYNVFE 420
Cdd:PRK08417 296 DSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFDPNESTIIDDN-------FSLYS 366
|
410
....*....|....*..
gi 479816250 421 GFELKGLPIMTLSRGRI 437
Cdd:PRK08417 367 GDELYGKIEAVIIKGKL 383
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
10-440 |
1.47e-28 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 117.09 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 10 IKGGTVI----TADRtfRADILIEDGKIAAIGDSLEG---DEVIDASGCYVMPGGIDPHTHLQMP---FMGTYSSDdfdt 79
Cdd:PRK07627 5 IKGGRLIdpaaGTDR--QADLYVAAGKIAAIGQAPAGfnaDKTIDASGLIVCPGLVDLSARLREPgyeYKATLESE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 80 gTAAALAGGTTMVVdfVLPDS-----EGNLLDALQEWFQKAGKARTdYSFHMAITGWNERTFNEMAEVVKRGINTFKHfm 154
Cdd:PRK07627 79 -MAAAVAGGVTSLV--CPPDTdpvldEPGLVEMLKFRARNLNQAHV-YPLGALTVGLKGEVLTEMVELTEAGCVGFSQ-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 155 ayKGALMVNDDEMFASFQRCAELG-AMPLvhaengdivaQLQAKLMAEG---NDGPEAhaySR------PPEVEGEATNR 224
Cdd:PRK07627 153 --ANVPVVDTQVLLRALQYASTFGfTVWL----------RPLDAFLGRGgvaASGAVA---SRlglsgvPVAAETIALHT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 225 AIMIADQAGVPLYVVHVSCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESE--YHNrdwdyaARRVMSPPFRDKLNQDSL 302
Cdd:PRK07627 218 IFELMRVTGARVHLARLSSAAGVALVRAAKAEGLPVTCDVGVNHVHLIDVDigYFD------SQFRLDPPLRSQRDREAI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 303 WAGLAAGSLQCVATDHCAFTTEQKrygIGNFTKIPNGTGGLEERMP--VLWTRgvRTGRLTPNEFVAVTSTNiAKILNIy 380
Cdd:PRK07627 292 RAALADGTIDAICSDHTPVDDDEK---LLPFAEATPGATGLELLLPltLKWAD--EAKVPLARALARITSAP-ARVLGL- 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 381 pQKGAVVPGADADLVIWDPEATKKISAKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAFD 440
Cdd:PRK07627 365 -PAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLVAGQVAFE 423
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
41-456 |
9.21e-24 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 102.92 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 41 EGDEVID-ASGCYVMPGGIDPHTHLQmpfmGTYSS--DDFDTGTAAALAGGTTMVVDfvLPDSEG--NLLDALQEWFQK- 114
Cdd:PRK00369 32 RCKPDLDlPQGTLILPGAIDLHVHLR----GLKLSykEDVASGTSEAAYGGVTLVAD--MPNTIPplNTPEAITEKLAEl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 115 AGKARTDYSFHMAITgwnertfNEMAEVVKRGINTFKHFmaykgalmVNDDEMFASFQRCAELGAMPLVHAEngdivaql 194
Cdd:PRK00369 106 EYYSRVDYFVYSGVT-------KDPEKVDKLPIAGYKIF--------PEDLEREETFRVLLKSRKLKILHPE-------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 195 qaklMAEGNDGPEAHAysRPPEVEGEATNraiMIADQAGVplYVVHVSCeqsHEAIRRARQKGMRVFGEPliQHLTLD-E 273
Cdd:PRK00369 163 ----VPLALKSNRKLR--RNCWYEIAALY---YVKDYQNV--HITHASN---PRTVRLAKELGFTVDITP--HHLLVNgE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 274 SEYHNRdwdyaarrvMSPPFRDKLNQDSLWAGLAagSLQCVATDHCAFTTEQKRYgigNFTKIPNGTGGLEERMPVLWTR 353
Cdd:PRK00369 227 KDCLTK---------VNPPIRDINERLWLLQALS--EVDAIASDHAPHSSFEKLQ---PYEVCPPGIAALSFTPPFIYTL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 354 gVRTGRLTPNEFVAVTSTNIAKILNIypQKGAVVPGADADLVIWDPEATKkisAKTQHSSIDYNVFEGFELKGLPIMTLS 433
Cdd:PRK00369 293 -VSKGILSIDRAVELISTNPARILGI--PYGEIKEGYRANFTVIQFEDWR---YSTKYSKVIETPLDGFELKASVYATIV 366
|
410 420
....*....|....*....|...
gi 479816250 434 RGRIAFDKGQVTAKPGDGRFIER 456
Cdd:PRK00369 367 QGKLAYLEGEVFPVKGINPFGER 389
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
2-407 |
2.18e-21 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 95.80 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 2 AKTGASKVIKGGTVITADRT---FRADILIEDGKIAAIGDSL-----EGDEVIDASGCYVMPGGIDPHTHLqmpFMGTYS 73
Cdd:COG1228 4 PAQAGTLLITNATLVDGTGGgviENGTVLVEDGKIAAVGPAAdlavpAGAEVIDATGKTVLPGLIDAHTHL---GLGGGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 74 SDDFDTGT----------------AAALAGGTTMVVDfvLPDSEGNLLDALqewfqKAGKARtdysfhmAITGWneRTFN 137
Cdd:COG1228 81 AVEFEAGGgitptvdlvnpadkrlRRALAAGVTTVRD--LPGGPLGLRDAI-----IAGESK-------LLPGP--RVLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 138 EmaevvKRGINTFkhfmayKGALMVNDDEMFASFQRCAELGAMplvhaengdivaqlQAKLMAEGNDGP----------- 206
Cdd:COG1228 145 A-----GPALSLT------GGAHARGPEEARAALRELLAEGAD--------------YIKVFAEGGAPDfsleelraile 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 207 EAHAYSRPPEVEGEaTNRAIMIADQAGVPLyVVHVSCEqSHEAIRRARQKGMRVFGePLIQhLTLDESEYHNRDWDYAAR 286
Cdd:COG1228 200 AAHALGLPVAAHAH-QADDIRLAVEAGVDS-IEHGTYL-DDEVADLLAEAGTVVLV-PTLS-LFLALLEGAAAPVAAKAR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 287 RVMSPPFRD--KLNQdslwAGLAAGslqcVATDHcaftteqkrygigNFTKIPNGTGGLEERMPVLWtrgvrtgRLTPNE 364
Cdd:COG1228 275 KVREAALANarRLHD----AGVPVA----LGTDA-------------GVGVPPGRSLHRELALAVEA-------GLTPEE 326
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 479816250 365 -FVAVTSTNiAKILNIYPQKGAVVPGADADLVIWDPEATKKISA 407
Cdd:COG1228 327 aLRAATINA-AKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
25-439 |
2.05e-19 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 90.48 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 25 DILIEDGKIAAIGDSL------EGDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDTGTAAALAGGTTMVVdfVLP 98
Cdd:PRK09059 24 TVLIEDGVIVAAGKGAgnqgapEGAEIVDCAGKAVAPGLVDARVFVGEP--GAEHRETIASASRAAAAGGVTSII--MMP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 99 DSEGNLLD-ALQEWFQKAGKARTDYSFH--MAIT-GWNERtfnEMAEVvkrgintfkHFMAYKGALMVNDDE---MFASF 171
Cdd:PRK09059 100 DTDPVIDDvALVEFVKRTARDTAIVNIHpaAAITkGLAGE---EMTEF---------GLLRAAGAVAFTDGRrsvANTQV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 172 QRCA-----ELGAMPLVHAENGDIVAQlqaKLMAEGNDGPEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSCEQS 246
Cdd:PRK09059 168 MRRAltyarDFDAVIVHETRDPDLGGN---GVMNEGLFASWLGLSGIPREAEVIPLERDLRLAALTRGRYHAAQISCAES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 247 HEAIRRARQKGMRVFGEPLIQHLTLDEseyhNRDWDYAARRVMSPPFRDKLNQDSLWAGLAAGSLQCVATDHCAFTTEQK 326
Cdd:PRK09059 245 AEALRRAKDRGLKVTAGVSINHLSLNE----NDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 327 RYgigNFTKIPNGTGGLEERMPVLwTRGVRTGRLTPNEFVAVTSTNIAKILNIypQKGAVVPGADADLVIWDPEATKKIS 406
Cdd:PRK09059 321 RL---PFSEAAAGAIGLETLLAAA-LRLYHNGEVPLLRLIEALSTRPAEIFGL--PAGTLKPGAPADIIVIDLDEPWVVD 394
|
410 420 430
....*....|....*....|....*....|...
gi 479816250 407 AKTQHSSIDYNVFEGFELKGLPIMTLSRGRIAF 439
Cdd:PRK09059 395 PEDLKSRSKNTPFEEARFQGRVVRTIVAGKTVY 427
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
52-405 |
5.86e-18 |
|
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: 84.86 E-value: 5.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 52 YVMPGGIDPHTHLQMPFM------GTYSSDDFDTGTAAALAGGTTMVVDFVLPDSEG--NLLDALQEwfqKAGKARTDYS 123
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLrgipvpPEFAYEALRLGITTMLKSGTTTVLDMGATTSTGieALLEAAEE---LPLGLRFLGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 124 FHMAITGWNERTFNEMAEVVKRGINTFKHF--------MAYKGALMVNDDEMFASFQRCAELGAMPLVHAENGDIvaqlq 195
Cdd:pfam01979 78 GCSLDTDGELEGRKALREKLKAGAEFIKGMadgvvfvgLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETKG----- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 196 aklmaegndgpeahaysrppevEGEATNRAIMIADQAGVPLYVvhvsCEQSHEA--IRRARQKGMrvfgepliqHLTLDE 273
Cdd:pfam01979 153 ----------------------EVEDAIAAFGGGIEHGTHLEV----AESGGLLdiIKLILAHGV---------HLSPTE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 274 SEYHNRDWDyAARRVMSPPFRDKL--NQDSLWAGLAAGSLQCVATDHCAFtteqkrygignftkipNGTGGLEERMPV-L 350
Cdd:pfam01979 198 ANLLAEHLK-GAGVAHCPFSNSKLrsGRIALRKALEDGVKVGLGTDGAGS----------------GNSLNMLEELRLaL 260
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 479816250 351 WTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWDPEATKKI 405
Cdd:pfam01979 261 ELQFDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAF 315
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
9-110 |
2.40e-17 |
|
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: 84.11 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFR----ADILIEDGKIAAIGDSLE------GDEVIDASGCYVMPGGIDPHTHLQM------------ 66
Cdd:COG0402 3 LIRGAWVLTMDPAGGvledGAVLVEDGRIAAVGPGAElparypAAEVIDAGGKLVLPGLVNTHTHLPQtllrgladdlpl 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 479816250 67 ---------PFMGTYSSDDFDTGTAAA----LAGGTTMVVDF--VLPDSEGNLLDALQE 110
Cdd:COG0402 83 ldwleeyiwPLEARLDPEDVYAGALLAlaemLRSGTTTVADFyyVHPESADALAEAAAE 141
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
9-94 |
5.52e-17 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 82.52 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVI--TADRTFRADILIEDGKIAAIGDSL---EGDEVIDASGCYVMPGGIDPHTHLqmpFMG-TYSSDDFDtgtA 82
Cdd:COG3964 3 LIKGGRVIdpANGIDGVMDIAIKDGKIAAVAKDIdaaEAKKVIDASGLYVTPGLIDLHTHV---FPGgTDYGVDPD---G 76
|
90
....*....|..
gi 479816250 83 AALAGGTTMVVD 94
Cdd:COG3964 77 VGVRSGVTTVVD 88
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
9-401 |
9.45e-17 |
|
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: 81.96 E-value: 9.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVI---TADRtFRADILIEDGKIAAIGDSL--EGDEVIDASGCYVMPGGIDPHTHLQMPFMGTyssddfDTGTAA 83
Cdd:cd01297 3 VIRNGTVVdgtGAPP-FTADVGIRDGRIAAIGPILstSAREVIDAAGLVVAPGFIDVHTHYDGQVFWD------PDLRPS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 84 ALAGGTTMVV-----------------DFVLPDSEGNLLDALQ-------EWFQKAGKARTD-----YSFH----MAITG 130
Cdd:cd01297 76 SRQGVTTVVLgncgvspapanpddlarLIMLMEGLVALGEGLPwgwatfaEYLDALEARPPAvnvaaLVGHaalrRAVMG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 131 WNERT-----FNEMAEVVKRGINtfkhfmayKGALMVNDDemfasfqrcaeLGAMPLVHAENGDIVAqlQAKLMAEgNDG 205
Cdd:cd01297 156 LDAREateeeLAKMRELLREALE--------AGALGISTG-----------LAYAPRLYAGTAELVA--LARVAAR-YGG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 206 PEAHAYSRPPEVEGEATNRAIMIADQAGVPLYVVHVSC---------EQSHEAIRRARQKGMRVfgepliqhlTLDESEY 276
Cdd:cd01297 214 VYQTHVRYEGDSILEALDELLRLGRETGRPVHISHLKSagapnwgkiDRLLALIEAARAEGLQV---------TADVYPY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 277 HNRDWDyAARRVMSPPFrdklnQDSLWAGLAAGslqcvaTDHCAftteqkryGIGNFTKipngtggleermpVL--WTRG 354
Cdd:cd01297 285 GAGSED-DVRRIMAHPV-----VMGGSDGGALG------KPHPR--------SYGDFTR-------------VLghYVRE 331
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 479816250 355 vrTGRLTPNEFVAVTSTNIAKILNIYpQKGAVVPGADADLVIWDPEA 401
Cdd:cd01297 332 --RKLLSLEEAVRKMTGLPARVFGLA-DRGRIAPGYRADIVVFDPDT 375
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
9-63 |
2.79e-16 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 81.37 E-value: 2.79e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479816250 9 VIKGGTVItaDRT----FRADILIEDGKIAAIGD--SLEGDEVIDASGCYVMPGGIDPHTH 63
Cdd:COG3653 5 LIRGGTVV--DGTgappFRADVAIKGGRIVAVGDlaAAEAARVIDATGLVVAPGFIDIHTH 63
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
1-110 |
9.74e-14 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 73.11 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 1 MAKTgaskVIKGGTVITADRTF----RADILIEDGKIAAIGDSLE--GDEVIDASGCYVMPGGIDPHTHL-QMPFMGTYS 73
Cdd:PRK08204 1 MKRT----LIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPSIEapDAEVVDARGMIVMPGLVDTHRHTwQSVLRGIGA 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479816250 74 SDDFDT------------------------GTAAALAGGTTMVVDFVL----PDSEGNLLDALQE 110
Cdd:PRK08204 77 DWTLQTyfreihgnlgpmfrpedvyianllGALEALDAGVTTLLDWSHinnsPEHADAAIRGLAE 141
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
9-400 |
1.18e-13 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 72.44 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFR-ADILIEDGKIAAIGDSLE-GDEVIDASGCYVMPGGIDPHTH--LQMPFMGTySSDDFDTGTAAA 84
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPGAEpDAEVIDLGGGYLAPGFIDLHVHggGGVDFMDG-TPEALRTIARAH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 85 LAGGTTmvvdFVLP----DSEGNLLDALQewfqkagkartdysfhmAITGWNERtfNEMAEVVkrGIntfkHF------M 154
Cdd:COG1820 80 ARHGTT----SFLPttitAPPEDLLRALA-----------------AIAEAIEQ--GGGAGIL--GI----HLegpflsP 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 155 AYKGA----LMVN-DDEMFASFQRCAelgamplvhaenGDIVaqlqaKLM--AegndgpeahaysrpPEVEG--EATNRA 225
Cdd:COG1820 131 EKKGAhppeYIRPpDPEELDRLLEAA------------GGLI-----KLVtlA--------------PELPGalEFIRYL 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 226 ImiadQAGvplyvVHVSC---EQSHEAIRRARQKGMRVFgepliQHLtldeseY------HNRD----WdyAArrvmspp 292
Cdd:COG1820 180 V----EAG-----VVVSLghtDATYEQARAAFEAGATHV-----THL------FnamsplHHREpgvvG--AA------- 230
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 293 frdkLNQDSLWAGLAA-G----------SLQCVATDHCAFTT--------EQKRYGIGNFT-KIPNGTGGLEE------- 345
Cdd:COG1820 231 ----LDDDDVYAELIAdGihvhpaavrlALRAKGPDRLILVTdamaaaglPDGEYELGGLEvTVKDGVARLADgtlagst 306
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 479816250 346 -RMPVLWTRGVRTGRLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWDPE 400
Cdd:COG1820 307 lTMDDAVRNLVEWTGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
9-94 |
3.56e-13 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 71.03 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVI----TADRTFraDILIEDGKIAAIGDSLEGD---EVIDASGCYVMPGGIDPHTHLqmpFMGtySSDDFDTGT 81
Cdd:PRK09237 2 LLRGGRVIdpanGIDGVI--DIAIEDGKIAAVAGDIDGSqakKVIDLSGLYVSPGWIDLHVHV---YPG--STPYGDEPD 74
|
90
....*....|...
gi 479816250 82 AAALAGGTTMVVD 94
Cdd:PRK09237 75 EVGVRSGVTTVVD 87
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
9-63 |
8.94e-13 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 70.22 E-value: 8.94e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479816250 9 VIKGGTV------ITADRtfrADILIEDGKIAAIGDSLEGDEVIDASGCYVMPGGIDPHTH 63
Cdd:COG1229 4 IIKNGRVydpangIDGEV---MDIAIKDGKIVEEPSDPKDAKVIDASGKVVMAGGVDIHTH 61
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
9-75 |
3.00e-12 |
|
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: 68.38 E-value: 3.00e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479816250 9 VIKGGTVITAD---RTFRADILIEDGKIAAIGDSLE-----GDEVIDASGCYVMPGGIDPHTHLQMPFMGTYSSD 75
Cdd:cd01298 2 LIRNGTIVTTDprrVLEDGDVLVEDGRIVAVGPALPlpaypADEVIDAKGKVVMPGLVNTHTHLAMTLLRGLADD 76
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
30-398 |
9.72e-12 |
|
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: 66.18 E-value: 9.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 30 DGKIAAIGDSL---EGDEVIDASGCYVMPGGIDPHTHLQM--PFMGTYSSDD-------------------FDTGTAAAL 85
Cdd:cd01309 1 DGKIVAVGAEIttpADAEVIDAKGKHVTPGLIDAHSHLGLdeEGGVRETSDAneetdpvtphvraidginpDDEAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 AGGTTMVVdfVLPDSEGNL-----LDALQEWFQKAGKARTDYSFHMAitgwnertfneMAEVVKRGINTFKHFMAYKgal 160
Cdd:cd01309 81 AGGVTTVQ--VLPGSANLIggqgvVIKTDGGTIEDMFIKAPAGLKMA-----------LGENPKRVYGGKGKEPATR--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 161 MVNDDEMFASFQRCAELG-AMPLVHAENGDIVA---QLQAKLMAEGNDGP-EAHAYsRPPEVEgeatnRAIMIADQAGVP 235
Cdd:cd01309 145 MGVAALLRDAFIKAQEYGrKYDLGKNAKKDPPErdlKLEALLPVLKGEIPvRIHAH-RADDIL-----TAIRIAKEFGIK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 236 LYVVHvsCEQSHEAIRRARQKGMRVFGEPLIQHLTLDESEYHnrDWDYAARrvmsppfrdklnqdsLWAglAAGSLQCVA 315
Cdd:cd01309 219 ITIEH--GAEGYKLADELAKHGIPVIYGPTLTLPKKVEEVND--AIDTNAY---------------LLK--KGGVAFAIS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 316 TDHCAFTTEQKRYGIGNFtkipngtggleermpvlwtrgVRTGrLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLV 395
Cdd:cd01309 278 SDHPVLNIRNLNLEAAKA---------------------VKYG-LSYEEALKAITINPAKILGIEDRVGSLEPGKDADLV 335
|
...
gi 479816250 396 IWD 398
Cdd:cd01309 336 VWN 338
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
9-264 |
1.40e-11 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 65.97 E-value: 1.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIGDSLEGD-EVIDASGCYVMPGGIDPHT-----HLqMPFMGTyssdDFDTGTA 82
Cdd:PRK15446 5 ILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALpGAIDAEGDYLLPGLVDLHTdnlekHL-APRPGV----DWPADAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 83 -------AALAGGTTMV----------VDFVLPDSEGNLLDALQEWfQKAGKARTDYSFHM--AITgwNERTFNEMAEVV 143
Cdd:PRK15446 80 laahdaqLAAAGITTVFdalsvgdeedGGLRSRDLARKLIDAIEEA-RARGLLRADHRLHLrcELT--NPDALELFEALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 144 KRG-------------------INTFKHFMAYKGALmvNDDEMFASFQRCAELGAMpLVHAENGDIVAQLQAK--LMAEG 202
Cdd:PRK15446 157 AHPrvdlvslmdhtpgqrqfrdLEKYREYYAGKYGL--SDEEFDAFVEERIALSAR-YAPPNRRAIAALARARgiPLASH 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479816250 203 NDGPEAHaysrppevegeatnRAIMIADQAGV---PLyvvhvsceqSHEAIRRARQKGMRV-FGEP 264
Cdd:PRK15446 234 DDDTPEH--------------VAEAHALGVAIaefPT---------TLEAARAARALGMSVlMGAP 276
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
8-108 |
2.24e-11 |
|
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: 65.29 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 8 KVIKGGTVITADRTFRADILIEDGKIAAIGDSLE---GDEVIDASGCYVMPGGIDPHTHlqmpfmGTYSSdDFDTGTAAA 84
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDEleeADEIIDLKGQYLVPGFIDIHIH------GGGGA-DFMDGTAEA 73
|
90 100 110
....*....|....*....|....*....|..
gi 479816250 85 LAG--------GTTMVVDFVLPDSEGNLLDAL 108
Cdd:cd00854 74 LKTiaealakhGTTSFLPTTVTAPPEEIAKAL 105
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
2-138 |
2.64e-11 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 65.59 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 2 AKTGASKVIKGGTVITADRTF-RAD-ILIEDGKIAAIGDSLE-------GDEVIDASGCYVMPGGIDPHTHLqmpfmgty 72
Cdd:COG1574 4 AAAAADLLLTNGRIYTMDPAQpVAEaVAVRDGRIVAVGSDAEvralagpATEVIDLGGKTVLPGFIDAHVHL-------- 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 479816250 73 ssddfdTGTAAALAGgttmvVDFVLPDSEGNLLDALQEWFQKAGKARTdysfhmaIT--GWNERTFNE 138
Cdd:COG1574 76 ------LGGGLALLG-----VDLSGARSLDELLARLRAAAAELPPGEW-------ILgrGWDESLWPE 125
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
6-93 |
3.55e-11 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 65.51 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 6 ASKVIKGGT---VITAdRTFRADILIEDGKIAAIGD-SLEGDEVIDASGCYVMPGGIDPHTHLQmpfmgtySS----DDF 77
Cdd:COG1001 5 ADLVIKNGRlvnVFTG-EILEGDIAIAGGRIAGVGDyIGEATEVIDAAGRYLVPGFIDGHVHIE-------SSmvtpAEF 76
|
90
....*....|....*.
gi 479816250 78 DtgtAAALAGGTTMVV 93
Cdd:COG1001 77 A---RAVLPHGTTTVI 89
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
6-75 |
6.84e-11 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 64.00 E-value: 6.84e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479816250 6 ASKVIKGGTVIT--ADRTFRADILIEDGKIAAIGDSLEG--DEVIDASGCYVMPGGIDPHTHLQMPFMGTYSSD 75
Cdd:PRK06038 2 ADIIIKNAYVLTmdAGDLKKGSVVIEDGTITEVSESTPGdaDTVIDAKGSVVMPGLVNTHTHAAMTLFRGYADD 75
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
10-63 |
3.18e-10 |
|
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: 62.43 E-value: 3.18e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 479816250 10 IKGGTVItaDRTF-----RADILIEDGKIAAIGDSLEGDEVIDASGCYVMPGGIDPHTH 63
Cdd:cd01304 1 IKNGTVY--DPLNgingeKMDIFIRDGKIVESSSGAKPAKVIDASGKVVMAGGVDMHSH 57
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
44-403 |
6.85e-10 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 61.01 E-value: 6.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 44 EVIDASGCYVMPGGIDPHTHL--QMPFMGTYSSDDFDTGTAAALAGGTTMVVDFVLpdseGNLLDALQEWFQKAGKARTD 121
Cdd:pfam07969 1 EVIDAKGRLVLPGFVDPHTHLdgGGLNLRELRLPDVLPNAVVKGQAGRTPKGRWLV----GEGWDEAQFAETRFPYALAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 122 YS--------------FHMAI--------TGWNERT-FNEMAEVVKRGINTFKHFM----AYKGALMVNDDEMFASF-QR 173
Cdd:pfam07969 77 LDevapdgpvllralhTHAAVansaaldlAGITKATeDPPGGEIARDANGEGLTGLlregAYALPPLLAREAEAAAVaAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 174 CAELGAMPLVHAEN-GDIVAQLQA-----KLMAEGNDGPEAHAYSRPPEVEG--EATNRAI-MIADqaGVP-LYVVHVSC 243
Cdd:pfam07969 157 LAALPGFGITSVDGgGGNVHSLDDyeplrELTAAEKLKELLDAPERLGLPHSiyELRIGAMkLFAD--GVLgSRTAALTE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 244 EQSH---------------EAIRRARQKGMRV----FGEPLIQhLTLDESEYHNRDWDYAARRVMS-----PPFRDKLNQ 299
Cdd:pfam07969 235 PYFDapgtgwpdfedealaELVAAARERGLDVaihaIGDATID-TALDAFEAVAEKLGNQGRVRIEhaqgvVPYTYSQIE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 300 DSLWAGLAAGSlqCVATDHCAFTTEQKRYG-------------IGNFTKIPNGT---GGLEERMPVLWT--------RGV 355
Cdd:pfam07969 314 RVAALGGAAGV--QPVFDPLWGDWLQDRLGaerargltpvkelLNAGVKVALGSdapVGPFDPWPRIGAavmrqtagGGE 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 479816250 356 RTG---RLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVIWDPEATK 403
Cdd:pfam07969 392 VLGpdeELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLT 442
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
9-400 |
9.15e-10 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 60.86 E-value: 9.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRA--DILIEDGKIAAIG-DSLEGDEVIDASGCYVMPGGIDPHTHLQMPfmGTYSSDDFDtgtaaal 85
Cdd:PRK09061 22 VIRNGRVVDPETGLDAvrDVGIKGGKIAAVGtAAIEGDRTIDATGLVVAPGFIDLHAHGQSV--AAYRMQAFD------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 86 aGGTTMVvdfvlpDSEGNLLDALQEWFQKAGKART-DYSfhmAITGWnerTFNEMAEVVKRG----INTFKHFMAYKGAL 160
Cdd:PRK09061 93 -GVTTAL------ELEAGVLPVARWYAEQAGEGRPlNYG---ASVGW---TPARIAVLTGPQaegtIADFGKALGDPRWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 161 M-VNDDEMFASFQRCAELG--------AMPLVHAENGDIVAQLQAKLMAEGNDGPE----AHAYSRPPEVEGEATNRAIM 227
Cdd:PRK09061 160 ErAATPAELAEILELLEQGldegalgiGIGAGYAPGTGHKEYLELARLAARAGVPTythvRYLSNVDPRSSVDAYQELIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 228 IADQAGVPLYVVHVS------CEQSHEAIRRARQKGMRV-----------------FGEPLIQHLTldESEYHNRDWDYA 284
Cdd:PRK09061 240 AAAETGAHMHICHVNstslrdIDRCLALVEKAQAQGLDVtteaypygagstvvgaaFFDPGWLERM--GLGYGSLQWVET 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 285 ARRVMS-------------------------PPFRDKLNQDSLWAGLAagslqcVATDHCAFTTEQKRYGIGNFTKIPNG 339
Cdd:PRK09061 318 GERLLTreelaklrandpgglvlihfldednPRDRALLDRSVLFPGAA------IASDAMPWTWSDGTVYEGDAWPLPED 391
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 479816250 340 ------TGGLEERMPVLWTRgvRTGRLTPNEFVAVTSTNIAKIL-NIYPQ---KGAVVPGADADLVIWDPE 400
Cdd:PRK09061 392 avshprSAGTFARFLREYVR--ERKALSLLEAIRKCTLMPAQILeDSVPAmrrKGRLQAGADADIVVFDPE 460
|
|
| PRK12393 |
PRK12393 |
amidohydrolase; Provisional |
18-64 |
4.61e-09 |
|
amidohydrolase; Provisional
Pssm-ID: 237088 [Multi-domain] Cd Length: 457 Bit Score: 58.54 E-value: 4.61e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 479816250 18 ADRTFRADILIEDGKIAAIG--DSLEGDEVIDASGCYVMPGGIDPHTHL 64
Cdd:PRK12393 20 AARLGGPDIRIRDGRIAAIGalTPLPGERVIDATDCVVYPGWVNTHHHL 68
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
25-94 |
5.27e-09 |
|
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: 57.72 E-value: 5.27e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 479816250 25 DILIEDGKIAAIGDSL---EGDEVIDASGCYVMPGGIDPHTHLqMPFMGTYsSDDFDtgtAAALAGGTTMVVD 94
Cdd:cd01307 1 DVAIENGKIAAVGAALaapAATQIVDAGGCYVSPGWIDLHVHV-YQGGTRY-GDRPD---MIGVKSGVTTVVD 68
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
7-66 |
8.33e-09 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 57.50 E-value: 8.33e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479816250 7 SKVIKGGTVITAD--RTFRADILIEDGKIAAIGDSLE--GDEVIDASGCYVMPGGIDPHTHLQM 66
Cdd:PRK08393 2 SILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINkpADTVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
9-64 |
1.31e-08 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 56.93 E-value: 1.31e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 479816250 9 VIKGGTVITADRT---FRADILIEDGKIAAIGDSLEG---DEVIDASGCYVMPGGIDPHTHL 64
Cdd:PRK07228 4 LIKNAGIVTMNAKreiVDGDVLIEDDRIAAVGDRLDLedyDDHIDATGKVVIPGLIQGHIHL 65
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
26-64 |
5.15e-08 |
|
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: 54.96 E-value: 5.15e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 479816250 26 ILIEDGKIAAIG-------DSLEGDEVIDASGCYVMPGGIDPHTHL 64
Cdd:cd01296 1 IAIRDGRIAAVGpaaslpaPGPAAAEEIDAGGRAVTPGLVDCHTHL 46
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
16-64 |
5.25e-08 |
|
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: 54.95 E-value: 5.25e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 479816250 16 ITADRTFRADILIEDGKIAAIGDSLE---GDEVIDASGCYVMPGGIDPHTHL 64
Cdd:cd01293 7 LADGGTALVDIAIEDGRIAAIGPALAvppDAEEVDAKGRLVLPAFVDPHIHL 58
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
9-94 |
5.77e-08 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 54.77 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVI--TADRTFRADILIEDGKIAAIG--DSLEGDEVIDASGCYVMPGGIDPHTHLqmPFMGTYSSDDFDtgtAAA 84
Cdd:PRK12394 6 LITNGHIIdpARNINEINNLRIINDIIVDADkyPVASETRIIHADGCIVTPGLIDYHAHV--FYDGTEGGVRPD---MYM 80
|
90
....*....|
gi 479816250 85 LAGGTTMVVD 94
Cdd:PRK12394 81 PPNGVTTVVD 90
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
58-260 |
6.73e-08 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 53.88 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 58 IDPHTHLQMPFMGT----------------YSSDDFDTGTAAALAGGTTMVVDFVLPDSEGNLLDALQEWFQKAGKARTD 121
Cdd:cd01292 2 IDTHVHLDGSALRGtrlnlelkeaeelspeDLYEDTLRALEALLAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 122 YSF----HMAITGWNERTF-----NEMAEVVKRGINTFKHFMAYkGALMVNDDEMFASFQRCAELGAMPLVHAENGDI-- 190
Cdd:cd01292 82 RVVlglgIPGVPAAVDEDAealllELLRRGLELGAVGLKLAGPY-TATGLSDESLRRVLEEARKLGLPVVIHAGELPDpt 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 479816250 191 --VAQLQAKLMAEGNDGPEaHAYSRPPEVEG--EATNRAIMIAdqagvPLYVVHVSCEQSH-EAIRRARQKGMRV 260
Cdd:cd01292 161 raLEDLVALLRLGGRVVIG-HVSHLDPELLEllKEAGVSLEVC-----PLSNYLLGRDGEGaEALRRLLELGIRV 229
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
8-64 |
1.33e-07 |
|
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: 53.55 E-value: 1.33e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 479816250 8 KVIKGGTVITADRTFRADILIEDGKIAAIGDSLEGD-----EVIDASGCYVMPGGIDPHTHL 64
Cdd:cd01308 2 TLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPgyenvTVVDLHGKILVPGFIDQHVHI 63
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
23-70 |
1.48e-07 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 53.40 E-value: 1.48e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 479816250 23 RADILIEDGKIAAIGDSL---EGDEVIDASGCYVMPGGIDPHTHLQMPFMG 70
Cdd:PRK05985 16 AVDILIRDGRIAAIGPALaapPGAEVEDGGGALALPGLVDGHIHLDKTFWG 66
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
7-66 |
2.94e-07 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 52.58 E-value: 2.94e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479816250 7 SKVIKGGTVITAD---RTFRADILIEDGKIAAIGD-SLEGDEVIDASGCYVMPGGIDPHTHLQM 66
Cdd:PRK06380 2 SILIKNAWIVTQNekrEILQGNVYIEGNKIVYVGDvNEEADYIIDATGKVVMPGLINTHAHVGM 65
|
|
| PRK07203 |
PRK07203 |
putative aminohydrolase SsnA; |
9-64 |
1.03e-06 |
|
putative aminohydrolase SsnA;
Pssm-ID: 235963 [Multi-domain] Cd Length: 442 Bit Score: 51.09 E-value: 1.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 479816250 9 VIKGGTVITADRTFR----ADILIEDGKIAAIG--DSLEGD----EVIDASGCYVMPGGIDPHTHL 64
Cdd:PRK07203 3 LIGNGTAITRDPAKPviedGAIAIEGNVIVEIGttDELKAKypdaEFIDAKGKLIMPGLINSHNHI 68
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
9-64 |
1.58e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 50.24 E-value: 1.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479816250 9 VIKGGTVITAD--RTFRAD--ILIEDGKIAAIGDSLE----GDEVIDASGCYVMPGGIDPHTHL 64
Cdd:PRK08203 5 IKNPLAIVTMDaaRREIADggLVVEGGRIVEVGPGGAlpqpADEVFDARGHVVTPGLVNTHHHF 68
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
25-64 |
3.29e-06 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 49.61 E-value: 3.29e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 479816250 25 DILIEDGKIAAIGDS-------LEGDEVIDASGCYVMPGGIDPHTHL 64
Cdd:cd01300 1 AVAVRDGRIVAVGSDaeakalkGPATEVIDLKGKTVLPGFIDSHSHL 47
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
24-64 |
6.36e-06 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 48.48 E-value: 6.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 479816250 24 ADILIEDGKIAAIGDSLEGD--EVIDASGCYVMPGGIDPHTHL 64
Cdd:PRK07572 18 IDIGIAGGRIAAVEPGLQAEaaEEIDAAGRLVSPPFVDPHFHM 60
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
26-64 |
1.14e-05 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 47.41 E-value: 1.14e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 479816250 26 ILIEDGKIAAIGD-----SLEGDEVIDASGCYVMPGGIDPHTHL 64
Cdd:TIGR01224 6 ILIHGGKIVWIGQlaalpGEEATEIIDCGGGLVTPGLVDPHTHL 49
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
2-92 |
1.53e-05 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 47.48 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 2 AKTGASKVIKGG--------------TVIT----ADRT--FRADILIEDGKIAAIG-----DSLEG--------DEVIDA 48
Cdd:PRK13207 43 VKFGGGKVIRDGmgqsqraradgavdTVITnaliLDHWgiVKADIGIKDGRIVAIGkagnpDIQDGvdiiigpgTEVIAG 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 479816250 49 SGCYVMPGGIDPHTHL----QMPfmgtyssddfdtgtaAALAGG-TTMV 92
Cdd:PRK13207 123 EGLIVTAGGIDTHIHFicpqQIE---------------EALASGvTTMI 156
|
|
| PRK07213 |
PRK07213 |
chlorohydrolase; Provisional |
8-64 |
2.29e-05 |
|
chlorohydrolase; Provisional
Pssm-ID: 235969 [Multi-domain] Cd Length: 375 Bit Score: 46.57 E-value: 2.29e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 479816250 8 KVIKGGTVITAD--RTFRADILIEDGKIAAIGDSLEGDEVIDASGCyVMPGGIDPHTHL 64
Cdd:PRK07213 2 LVYLNGNFLYGEdfEPKKGNLVIEDGIIKGFTNEVHEGNVIDAKGL-VIPPLINAHTHI 59
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
9-93 |
4.56e-05 |
|
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: 45.78 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIG-----DSLEGD----------EVIDASGCYVMPGGIDPHTHL----QMPfm 69
Cdd:cd00375 68 VITNALIIDYTGIYKADIGIKDGRIVAIGkagnpDIMDGVtpnmivgpstEVIAGEGKIVTAGGIDTHVHFicpqQIE-- 145
|
90 100
....*....|....*....|....
gi 479816250 70 gtyssddfdtgtaAALAGGTTMVV 93
Cdd:cd00375 146 -------------EALASGITTMI 156
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
22-64 |
5.81e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 45.36 E-value: 5.81e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 479816250 22 FRADILIEDGKIAAI---GDSLEGDEVIDASGCYVMPGGIDPHTHL 64
Cdd:PRK07583 39 VLVDIEIADGKIAAIlpaGGAPDELPAVDLKGRMVWPCFVDMHTHL 84
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
11-70 |
7.74e-05 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 45.00 E-value: 7.74e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 479816250 11 KGGTVITADRTFRADILIEDGKIAAIGD----SLEGDEVIDASGCYVMPGGIDPHTHLQMPFMG 70
Cdd:PRK06846 19 YENGVIVQTETALCTLEIQDGKIVAIRPnkqvPDATLPTYDANGLLMLPAFREMHIHLDKTYYG 82
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
25-64 |
8.44e-05 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 44.69 E-value: 8.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 479816250 25 DILIEDGKIAAI----GDSLEGDEVIDASGCYVMPGGIDPHTHL 64
Cdd:PRK09230 21 QITIEDGKISAIepqsEASLEAGEVLDAEGGLAIPPFIEPHIHL 64
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
43-398 |
2.43e-04 |
|
Metallo-dependent hydrolases, subgroup A 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: 238624 [Multi-domain] Cd Length: 342 Bit Score: 43.05 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 43 DEVIDASGCYVMPGGIDPHTHLQMPFMG----TYSSDDFDTGTAA-----ALAGGTTMVVDFVLPDSeGNLLDALQEW-- 111
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDlpldLALPVEYRTIRATrqaraALRAGFTTVRDAGGADY-GLLRDAIDAGli 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 112 ----FQKAGKArtdysfhMAIT-GWNERTFNEMaevvkrgintfkHFMAYKGALMVND-DEMFASFQRCAELGAmplvha 185
Cdd:cd01299 80 pgprVFASGRA-------LSQTgGHGDPRGLSG------------LFPAGGLAAVVDGvEEVRAAVREQLRRGA------ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 186 engDIVaqlqaKLMAEG-----NDGPEAHAYSrPPEVegeatnRAIMI-ADQAGVPLyVVHVsceQSHEAIRRARQKGMR 259
Cdd:cd01299 135 ---DQI-----KIMATGgvlspGDPPPDTQFS-EEEL------RAIVDeAHKAGLYV-AAHA---YGAEAIRRAIRAGVD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 260 vfgepLIQHLTLDESE------------------YHNRDWDYAARRVMS-PPFRDKLNQDSLWAGLA----AGSLQCVAT 316
Cdd:cd01299 196 -----TIEHGFLIDDEtielmkekgiflvptlatYEALAAEGAAPGLPAdSAEKVALVLEAGRDALRrahkAGVKIAFGT 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 317 DhcaftteqkrYGignFTKIPNGTGGLEerMPVLwtrgVRTGrLTPNEFVAVTSTNIAKILNIYPQKGAVVPGADADLVI 396
Cdd:cd01299 271 D----------AG---FPVPPHGWNARE--LELL----VKAG-GTPAEALRAATANAAELLGLSDELGVIEAGKLADLLV 330
|
..
gi 479816250 397 WD 398
Cdd:cd01299 331 VD 332
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
9-89 |
5.21e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 42.57 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIG--------DSLE-------GDEVIDASGCYVMPGGIDPHTHLQMPfmgTYS 73
Cdd:PRK13985 68 IITNALIIDYTGIYKADIGIKDGKIAGIGkggnkdmqDGVKnnlsvgpATEALAGEGLIVTAGGIDTHIHFISP---QQI 144
|
90
....*....|....*.
gi 479816250 74 SDDFDTGTAAALAGGT 89
Cdd:PRK13985 145 PTAFASGVTTMIGGGT 160
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
23-111 |
5.45e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 42.39 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 23 RADILIEDGKIAAIG-----DSLEG----------DEVIDASGCYVMPGGIDPHTHLQMPFMgtyssddfdtgTAAALAG 87
Cdd:PRK13308 86 KGDIGIRDGRIVGIGkagnpDIMDGvdprlvvgpgTDVRPAEGLIATPGAIDVHVHFDSAQL-----------VDHALAS 154
|
90 100 110
....*....|....*....|....*....|....
gi 479816250 88 G-TTMV---------VDFVLPDSEGNLLDALQEW 111
Cdd:PRK13308 155 GiTTMLggglgptvgIDSGGPFNTGRMLQAAEAW 188
|
|
| ureC |
PRK13206 |
urease subunit alpha; Reviewed |
9-93 |
6.48e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237304 [Multi-domain] Cd Length: 573 Bit Score: 42.39 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIG-----DSLEG----------DEVIDASGCYVMPGGIDPHTHLQMPfmgtys 73
Cdd:PRK13206 74 VITGAVILDHWGIVKADVGIRDGRIVAIGkagnpDIMDGvhpdlvigpsTEIIAGNGRILTAGAIDCHVHFICP------ 147
|
90 100
....*....|....*....|
gi 479816250 74 sddfdTGTAAALAGGTTMVV 93
Cdd:PRK13206 148 -----QIVDEALAAGITTLI 162
|
|
| PLN02303 |
PLN02303 |
urease |
9-89 |
1.02e-03 |
|
urease
Pssm-ID: 215172 [Multi-domain] Cd Length: 837 Bit Score: 41.66 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITADRTFRADILIEDGKIAAIG-----DSLEG----------DEVIDASGCYVMPGGIDPHTHLQMPFMGTYS 73
Cdd:PLN02303 337 VITNAVIIDYTGIYKADIGIKDGLIVGIGkagnpDVMDGvtsnmivgvnTEVIAGEGMIVTAGGIDCHVHFICPQLATEA 416
|
90
....*....|....*.
gi 479816250 74 sddFDTGTAAALAGGT 89
Cdd:PLN02303 417 ---IASGITTLVGGGT 429
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
26-72 |
1.60e-03 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 40.94 E-value: 1.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 479816250 26 ILIEDGKIAAIGDSLE-------GDEVIDASGCYVMPGGIDPHTHL-QMPFMGTY 72
Cdd:PRK09228 34 LLVEDGRIVAAGPYAElraqlpaDAEVTDYRGKLILPGFIDTHIHYpQTDMIASY 88
|
|
| PRK10027 |
PRK10027 |
cryptic adenine deaminase; Provisional |
9-93 |
2.04e-03 |
|
cryptic adenine deaminase; Provisional
Pssm-ID: 182201 [Multi-domain] Cd Length: 588 Bit Score: 40.58 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 479816250 9 VIKGGTVITAdrtfradILIEDGKIAAIG---DSLEGDEVIDASGCYVMPGGIDPHTHLQMPFMGTYSsddFDTGTaaaL 85
Cdd:PRK10027 42 LINGGEISGP-------IVIKGRYIAGVGaeyADAPALQRIDARGATAVPGFIDAHLHIESSMMTPVT---FETAT---L 108
|
....*...
gi 479816250 86 AGGTTMVV 93
Cdd:PRK10027 109 PRGLTTVI 116
|
|
| |
