|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
17-466 |
0e+00 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 732.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKdHGVNSFLVYMAFKDRFQL 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 177 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 257 PKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSPDpTTPDFLNSLLSCGDLQVTGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 337 NTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDS 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1915913 417 VKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSG 466
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
17-471 |
0e+00 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 672.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQL 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 177 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 257 PKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 337 NTAQK-AVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915913 416 SVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 471
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
16-475 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 582.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 16 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlivpGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 96 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVkDHGVNSFLVYMAFKDRFQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 176 LTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 256 MPKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCT 335
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 336 FNTAQKA-VGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDP 414
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915913 415 DSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 475
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-475 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 552.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 12 ITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 92 GTKAALAGGTTMIIDHVVPEPGtSLLAAFDQWREWADsKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSFLVYMAFK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 172 DRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 252 VTKVMPKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGS 331
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 332 AHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVI 411
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915913 412 WDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 475
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-471 |
6.54e-123 |
|
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: 369.04 E-value: 6.54e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 18 LIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 98 AGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVkDHGVNSFLVYMAFKD-RFQL 176
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 177 TDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRildLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVM 256
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRGGVMN---EGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 257 PKSAAEVIAQARKKGTVVYGE--P----ITAS-LGTDGSHYwsknwakaaafVTSPPLsPDPTTPDFL-NSLLScGDLQV 328
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPL-RTEEDREALwEGLAD-GTIDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 329 TGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDAD 408
Cdd:COG0044 302 IATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADAD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915913 409 LVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 471
Cdd:COG0044 378 LVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-471 |
2.22e-120 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 364.02 E-value: 2.22e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPD-QGMTSADDFFQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 96 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGI-QEEMEALVKDhGVNSFLVYMAFkDRF 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 175 QLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 255 VMPKSAAEVIAQARKKGTVVYGEP------ITAS-LGTDGSHywsknwakAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQ 327
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 328 VTGSAHCTFN---TAQKAVGKDN--FTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIS 402
Cdd:PRK13404 313 VFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915913 403 VGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 471
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
17-469 |
1.29e-62 |
|
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: 212.53 E-value: 1.29e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWH-KGIQEEMEALVKdhGVNSFLVYMAFKD 172
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNlDQLRPLDEAGVV--GFKCFLCPSGVDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 173 RFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYV 252
Cdd:cd01315 156 FPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKETGCRLHI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 253 TKVMPKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPLSpDPTTPDFLNSLLSCGD 325
Cdd:cd01315 236 VHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWEALENGD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 326 LQVTGSAH--CTfnTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISV 403
Cdd:cd01315 304 IDMVVSDHspCT--PELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQKGRIAV 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915913 404 GSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTlHVTEGSGRYI 469
Cdd:cd01315 382 GYDADFVVWDPEEEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
65-443 |
8.22e-60 |
|
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: 201.85 E-value: 8.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 65 VIPGGIDVHTRFQMPDQGMTSaDDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEw 144
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 145 hkGIQEEMEALVKDHGVNSFLVYMAFK--DRFQLTDSQIYEVLSVIRDIGAIAQVHAEngdiiaeaqqrildlgitgpeg 222
Cdd:cd01302 81 --GDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 223 hvlsrpeeveaeavnRSITIANQTNCPLYVTKVMPKSAAEVIAQARKKGTVVYGEPITASLGTDGShYWSKNWAKaaaFV 302
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 303 TSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDnFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 382
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915913 383 VTSTNAAKVFNLYPrKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSP 443
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-472 |
5.06e-52 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 184.09 E-value: 5.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIT-EWhkgiqEEMEALVkDHGVNSF-LVYMA----- 169
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGINGGVTgNW-----DPLESLW-ERGVFALgEIFMAdstgg 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 170 ---FKDRFQltdsqiyEVLSVIRDIGAIAQVHAENGDIIAEAqQRILDlGITGPEGHVLSRPEEVEAEAVNRSITIANQT 246
Cdd:PRK02382 156 mgiDEELFE-------EALAEAARLGVLATVHAEDEDLFDEL-AKLLK-GDADADAWSAYRPAAAEAAAVERALEVASET 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 247 NCPLYVTKVmpkSAAEVIAQARKKGTVVYGEPITASLGTDgshywskNWAKAAAFV-TSPPLSPDPTTPDFLNSLLScGD 325
Cdd:PRK02382 227 GARIHIAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRREALWERLND-GT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 326 LQVTGSAHCTFNTAQKAVG-KDnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVG 404
Cdd:PRK02382 296 IDVVASDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAEG 369
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915913 405 SDADLVIWDPDSVKTISAKTHNSALEYNIFEGMEcrGS-PLVVISQGKIVLEDGTLHVTEGSGRYIPRK 472
Cdd:PRK02382 370 YDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-460 |
1.02e-51 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 183.75 E-value: 1.02e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKgiqEEMEALVkDHGVNSFLVYMAFK-- 171
Cdd:PRK06189 82 AAGGCTTYFD--MPlnsIPPTVTREALDAKAELARQKSAVDFALWGGLVPGNL---EHLRELA-EAGVIGFKAFMSNSgt 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 172 DRFQLTDSQ-IYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPL 250
Cdd:PRK06189 156 DEFRSSDDLtLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGCPL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 251 YVTKVMPKSAAEVIAQARKKGtvvygepITASLGTdGSHY--WSKN--WAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDL 326
Cdd:PRK06189 236 HFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYllFTEEdfERIGAVAKCAPPLR-SRSQKEELWRGLLAGEI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 327 QVTGSAH--CTFNTAQkavgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVG 404
Cdd:PRK06189 307 DMISSDHspCPPELKE----GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLEVG 381
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915913 405 SDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLH 460
Cdd:PRK06189 382 ADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
17-470 |
7.84e-49 |
|
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: 175.65 E-value: 7.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWH-KGIQEEMEALVkdHGVNSFLVYMAFKD 172
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNlDDLRELDEAGV--VGFKAFLSPSGDDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 173 RFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYV 252
Cdd:TIGR03178 155 FPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 253 TKVMPKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAK----AAAFVTSPPLSpDPTTPDFLNSLLSCGDLQV 328
Cdd:TIGR03178 235 VHLSSAEAVELITEAKQEGLDVTVETCP--------HYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNGLIDC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 329 TGSAHCTFNTAQKAvgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDAD 408
Cdd:TIGR03178 306 VVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDAD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915913 409 LVIWDPDSVKTISakthNSALEY----NIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIP 470
Cdd:TIGR03178 383 FVFVDPDESYTLT----PDDLYYrhkvSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
33-456 |
7.45e-47 |
|
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: 169.16 E-value: 7.45e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 33 ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIID--HVVP 110
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADmpNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 111 EPGTSllAAFDQWREWADSKSCCDYSLHVDITEWHKGiQEEMEAlvkdhgvnSFLVYMA-----FKDRFQ--LTDSQIYE 183
Cdd:TIGR00857 83 PIDTP--ETLEWKLQRLKKVSLVDVHLYGGVTQGNQG-KELTEA--------YELKEAGavgrmFTDDGSevQDILSMRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 184 VLSVIRDIGAIAQVHAENGDIIAEAQQRildLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMPKSAAEV 263
Cdd:TIGR00857 152 ALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 264 IAQARKkgtvvYGEPITAS------LGTDGSHYWSKNWAKaaafvTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFN 337
Cdd:TIGR00857 229 IVKAKS-----QGIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 338 TAQKAVgkdNFTLIPEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSV 417
Cdd:TIGR00857 298 LEEKTK---EFAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKE 372
|
410 420 430
....*....|....*....|....*....|....*....
gi 1915913 418 KTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLED 456
Cdd:TIGR00857 373 WTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
65-450 |
2.27e-35 |
|
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: 136.31 E-value: 2.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 65 VIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEw 144
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 145 hkgiQEEMEALVKdHGVNSFLVYMAfkdrfQLTDS--QIYEVLSVI-RDIGAIAQVHAENGDIIAEAQQRILDLGItgpe 221
Cdd:cd01318 81 ----SEDLEELDK-APPAGYKIFMG-----DSTGDllDDEETLERIfAEGSVLVTFHAEDEDRLRENRKELKGESA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 222 gHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMPKSAAEVIAQARKKGTVvygePITAS--LGTDGSHYWSKNWAKaa 299
Cdd:cd01318 147 -HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTV----EVTPHhlFLDVEDYDRLGTLGK-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 300 afvTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVI---WDKAVVTGKmd 376
Cdd:cd01318 220 ---VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILSLS-- 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915913 377 enQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQG 450
Cdd:cd01318 291 --RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
2.33e-33 |
|
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: 129.93 E-value: 2.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 64 MVIPGGIDVHTRFQM------PDQGMTSADDFFQGTKAALAGGTTMIIDHVV--PEPGTSLLAAFDQW----REWAdsKS 131
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELplglRFLG--PG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 132 CC---DYSLHVDITEWHKGIQEEMEALVKDHGVnsFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDiiAEA 208
Cdd:pfam01979 79 CSldtDGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETK--GEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 209 QQRILDLGITGPEGHVLSRPEEVeaeAVNRSITIANQTNCPLyvtkvMPKSAAEVIAQARKKGTVvygepitasLGTDGS 288
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESG---GLLDIIKLILAHGVHL-----SPTEANLLAEHLKGAGVA---------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 289 HYWSKNWAKAAAfvtspplspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkaVGKDNFTLIPEGTNGTEERmsviwdk 368
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 369 AVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSvktisakthnsaleYNIFEGMECRGSPLVVIS 448
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------------LAAFFGLKPDGNVKKVIV 329
|
....*
gi 1915913 449 QGKIV 453
Cdd:pfam01979 330 KGKIV 334
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-444 |
2.06e-32 |
|
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: 128.12 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 54 GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTmiidHVVPEPGTsllaafdqwREWADSKSCC 133
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVIDNPAVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 134 DYSLHVD-------------ITEWHKGIQ-EEMEALvKDHGVNSFlvymaFKDRFQLTDSQI-YEVLSVIRDIGAIAQVH 198
Cdd:cd01317 66 ELLKNRAkdvgivrvlpigaLTKGLKGEElTEIGEL-LEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 199 AENGDIIAEAQqrILDLGITGPEGhVLSRPEEVEAEAVNRSITIANQTNCPLYVTKVMPKSAAEVIAQARKKGtvvygEP 278
Cdd:cd01317 140 PEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 279 ITASLGtdgSHYWS------KNWAkaAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIP 352
Cdd:cd01317 212 VTAEVT---PHHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 353 EGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPrkGRISVGSDADLVIWDPDSVKTISAKTHNSALEYN 432
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNT 360
|
410
....*....|..
gi 1915913 433 IFEGMECRGSPL 444
Cdd:cd01317 361 PFDGQKLKGRVL 372
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
1.25e-30 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 124.15 E-value: 1.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 16 RLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPDQgmTSADDFFQGTK 94
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREPGQ--EDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 95 AALAGGTTMiidhVVPEPGT----SLLAAFDQWREWADSKSCCDysLHV--DITEWHKGIQE-EMEALvKDHGVnsflvy 167
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNTkpviDTPEVVEYVLDRAKEAGLVD--VLPvgAITKGLAGEELtEFGAL-KEAGV------ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 168 MAFK-DRFQLTDSQI-YEVLSVIRDIG-AIAQvHAENGDIIAEAQ----QRILDLGITGpeghvlsRPEEVEAEAVNRSI 240
Cdd:PRK09357 146 VAFSdDGIPVQDARLmRRALEYAKALDlLIAQ-HCEDPSLTEGGVmnegEVSARLGLPG-------IPAVAEEVMIARDV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 241 TIANQTNCPLYVTKVMPKSAAEVIAQARKKGTvvygePITA------------SLGTDGSHYwsknwaKAAafvtsPPLS 308
Cdd:PRK09357 218 LLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN-----PPLR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 309 PDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNA 388
Cdd:PRK09357 282 TEEDREALIEGLKD-GTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLEKMTINP 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915913 389 AKVFNLYPrkGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLED 456
Cdd:PRK09357 358 ARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-431 |
7.63e-29 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 119.58 E-value: 7.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDHVVPE-PGTSLLAAFDQWREWADSKsccdysLHVDITEWHKGIQEEMEAL--VKDHGVNSFLVYMAF-KD 172
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGK------LTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 173 R-----FQ-LTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQT 246
Cdd:PRK08044 155 RgidndFRdVNDWQFYKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 247 NCPLYVTKVMPKSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPLSPDPTTPDFLNSLLS 322
Cdd:PRK08044 235 GCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEKLFN 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 323 cGDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIS 402
Cdd:PRK08044 307 -GEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKGRIA 381
|
410 420
....*....|....*....|....*....
gi 1915913 403 VGSDADLVIWDPDSvktiSAKTHNSALEY 431
Cdd:PRK08044 382 PGKDADFVFIQPNS----SYVLKNEDLEY 406
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-457 |
1.72e-27 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 115.16 E-value: 1.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 14 SDRLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQG 92
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 93 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITewhkgiQEEMEALVKDHGVNSFLVYMAFKD 172
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMGSSH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 173 RFQLTDSQiyEVLSVI--RDIGAIAqVHAENGDIIAEAQQRILdlGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCPL 250
Cdd:PRK07575 154 GPLLVDEE--AALERIfaEGTRLIA-VHAEDQARIRARRAEFA--GISDPADHSQIQDEEAALLATRLALKLSKKYQRRL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 251 YVTKVmpKSAAEVIAQARKKGTVVYGEPITASLGTDGSHYwsknwAKAAAFVT-SPPLSpDPTTPDFLNSLLSCGDLQVT 329
Cdd:PRK07575 229 HILHL--STAIEAELLRQDKPSWVTAEVTPQHLLLNTDAY-----ERIGTLAQmNPPLR-SPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 330 GSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVIWDKAVvTGKMDENQFVAVTSTNAAKVFNLyPRKGRISVGSDADL 409
Cdd:PRK07575 301 ATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADL 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1915913 410 VIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDG 457
Cdd:PRK07575 376 VLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
5.02e-26 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 111.17 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITewHKGIQE--EMEALVKDHGVNsflVYM--AFKD 172
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGT--RDNADElaELERLPGCAGIK---VFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 173 RFQLTDSQIYEVLSVIRDIGAiaqVHAENGDIIAEAQqrilDLGITG-PEGHVLSRPEEVEAEAVNRSITIANQTNCPLY 251
Cdd:PRK09060 159 LLVEDDEGLRRILRNGRRRAA---FHSEDEYRLRERK----GLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 252 VTKVMPKSAAEVIAQARKKGTV--------VYGEPITASLGTdgshYWSKNwakaaafvtsPPLSpDPTTPDFLNSLLSC 323
Cdd:PRK09060 232 VLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGVRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 324 GDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKaVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRISV 403
Cdd:PRK09060 297 GVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915913 404 GSDADLVIWDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGR 467
Cdd:PRK09060 372 GYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
22-471 |
1.43e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 109.18 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 22 GKIVNDDQSFYADIYMEDGLIKQIGENLivpGGVKTIEAHSrMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGT 101
Cdd:PRK01211 5 GNFYYKGKFDYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 102 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHvditewhkgiqeEME----ALVKDHGVNSFLVYMAFKDRFQLT 177
Cdd:PRK01211 79 TFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLY------------SMEtgnnALILDERSIGLKVYMGGTTNTNGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 178 DSQIYEVlSVIRDIGAIAQVHAENGDIIAEAQQRILDLgitgpEGHVLSRPEEVEAEAVNRSITIANQTNCPLYVTKvmP 257
Cdd:PRK01211 147 DIEGGEI-KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLKTKIIAHVSS--I 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 258 KSAAEVIAQARKKGTVVYGEpitASLGTDGShywsknwakaaafvTSPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFN 337
Cdd:PRK01211 219 DVIGRFLREVTPHHLLLNDD---MPLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSDHAPHT 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 338 TAQKAvgkdNFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRISVGSDADLVIWDPDSV 417
Cdd:PRK01211 281 EEDKQ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAFDFTNI 353
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1915913 418 KTISAKTHNSALEYNIFEGMECRgSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 471
Cdd:PRK01211 354 KKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-469 |
6.41e-25 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 107.16 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 22 GKIVNDDQSFYADIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTRFQmpDQGMTSADDFFQGTKAALAGGT 101
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR--DFEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 102 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDITEWHKGIQEEMEALVKDHGVNSflVYMAFKDRFQLTDSQI 181
Cdd:PRK04250 80 TLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGAS--TGGIFSENFEVDYACA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 182 YEVLSvirdigaiaqVHAENGDIIAEAqqrildlgitgPEghvlsRPEEVEAEAVNRSITIANQTNCPLYVTKVMPKSAA 261
Cdd:PRK04250 158 PGIVS----------VHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTKDGL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 262 EVIAQARKKGTVVYGEPitaslgtdgSH--YWSKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDlqVTGSAHCTFNTA 339
Cdd:PRK04250 212 KLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP--IIASDHAPHTLE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 340 QKAVGKdnftlipEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNlYPRKGrISVGSDADLVIWDPDSVKT 419
Cdd:PRK04250 280 DKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEWT 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1915913 420 ISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYI 469
Cdd:PRK04250 350 IKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-472 |
1.38e-23 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 104.47 E-value: 1.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 12 ITSDRLLIKGGKIVNDdqsfyadIYMEDGLIKQIGENLIVPG---GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADD 88
Cdd:PLN02795 48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 89 FFQGTKAALAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKsccdysLHVDITEWHKGIQE------EMEALVkDH 159
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 160 GV---NSFLVYMAFKDRFQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAQQRILDLgiTGPEGHVLSRPEEVEAEAV 236
Cdd:PLN02795 190 GAlglKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 237 NRSITIANQTN-------CPLYVTKVMP-KSAAEVIAQARKKGTVVYGEPITaslgtdgsHYWsknwAKAAA-------- 300
Cdd:PLN02795 268 RQLLEVAKDTRpggvaegAHVHIVHLSDaESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtr 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 301 FVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGkMDENQF 380
Cdd:PLN02795 336 YKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 381 VAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDP------DSVKTISAKTHN-SAleyniFEGMECRGSPLVVISQGKIV 453
Cdd:PLN02795 414 ARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHKHKSlSP-----YLGTKLSGKVIATFVRGNLV 487
|
490
....*....|....*....
gi 1915913 454 LEDGtLHVTEGSGRYIPRK 472
Cdd:PLN02795 488 FLEG-KHAKQACGSPILAK 505
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-138 |
9.43e-17 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 83.00 E-value: 9.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 15 DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGID--VHTRfqmpDQGMTSADDFFQG 92
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR----EPGLTHKGDIASE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1915913 93 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLH 138
Cdd:PRK09236 78 SRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFY 123
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
8-422 |
2.67e-12 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 68.45 E-value: 2.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 8 NIPPITSDRLLIKGGKIVNDDQSFY---ADIYMEDGLIKQIGEN--LIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPD-- 80
Cdd:COG1228 1 KKAPAQAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGgr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 81 -------QGMTSADDFFQGT----KAALAGGTTMIIDHvvpePGTSL----------LAAFDQWREWADSKSccdyslhV 139
Cdd:COG1228 81 avefeagGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRVLAAGPA-------L 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 140 DITE-WHKGIQEEMEALV---KDHGVNSFLVYMAFKDRfQLTDSQIYEVLSVIRDIGAIAQVHAENGDIIAEAqqriLDL 215
Cdd:COG1228 150 SLTGgAHARGPEEARAALrelLAEGADYIKVFAEGGAP-DFSLEELRAILEAAHALGLPVAAHAHQADDIRLA----VEA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 216 GITGPEgHVLSRPEeveaeavnrsitianqtncplyvtkvmpksaaEVIAQARKKGTVVYGePiTASLGTDGSHYWSKNW 295
Cdd:COG1228 225 GVDSIE-HGTYLDD--------------------------------EVADLLAEAGTVVLV-P-TLSLFLALLEGAAAPV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 296 AKAAAFVtspplspDPTTPDFLNSLLSCGdlqvtgsahCTFntaqkAVGKD-NFTLIPEGTNGTEERMsviwdkaVVTGK 374
Cdd:COG1228 270 AAKARKV-------REAALANARRLHDAG---------VPV-----ALGTDaGVGVPPGRSLHRELAL-------AVEAG 321
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1915913 375 MDENQ-FVAVTStNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISA 422
Cdd:COG1228 322 LTPEEaLRAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-467 |
3.30e-11 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 65.40 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVndDQS----FYADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDF--- 89
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHY---DGQVFWDPDLrps 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 90 -FQGTKAALAG------------GTTMIIDHVVPEPGTSLLAAFDqWREWAD-------SKSCCDYSLHV---DITEWHK 146
Cdd:cd01297 76 sRQGVTTVVLGncgvspapanpdDLARLIMLMEGLVALGEGLPWG-WATFAEyldaleaRPPAVNVAALVghaALRRAVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 147 GI---------QEEMEALVKDH------GVNSFLVYMafkDRFQLTDSQIYEVLSVIRDIGAIAQVHAEN-GDIIAEAQQ 210
Cdd:cd01297 155 GLdareateeeLAKMRELLREAleagalGISTGLAYA---PRLYAGTAELVALARVAARYGGVYQTHVRYeGDSILEALD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 211 RILDLGitgpeghvlsrpeeveaEAVNRSITIANQTNCPLYVTKVMPKSAAEvIAQARKKGTVVYGE--PITASLGTDgs 288
Cdd:cd01297 232 ELLRLG-----------------RETGRPVHISHLKSAGAPNWGKIDRLLAL-IEAARAEGLQVTADvyPYGAGSEDD-- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 289 hywsknwakAAAFVTSPPlspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkavgkdnftlipeGTNGTEERMSVIWdk 368
Cdd:cd01297 292 ---------VRRIMAHPV-------------VMGGSDGGALGKPHP-------------------RSYGDFTRVLGHY-- 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 369 AVVTGKMDENQFVAVTSTNAAKVFNLYPRkGRISVGSDADLVIWDPDSVK---TISAKTHNSaleynifEGMEcrgspLV 445
Cdd:cd01297 329 VRERKLLSLEEAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGIE-----AV 395
|
490 500
....*....|....*....|..
gi 1915913 446 VISqGKIVLEDGtLHVTEGSGR 467
Cdd:cd01297 396 LVN-GVPVVRDG-AFTGARPGR 415
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-459 |
1.39e-10 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 63.38 E-value: 1.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQS---FYADIYMEDGLIKQIGENLIVPG--GVKTIEAHSRMVIPGGIDVHTRFQM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 79 --------PDQGMTSADDFFQGTKAALA----GGTTMIIDHVVPEPGTSLLAA-------------FDQWREWADSKscc 133
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVAEAAeelgiravlgrgiMDLGTEDVEET--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 134 dyslhvditewhKGIQEEMEALVKD-HGVNSFLVYMAFKDR--FQLTDSQIYEVLSVIRDIGAIAQVH-AENGDIIAEAQ 209
Cdd:cd01298 158 ------------EEALAEAERLIREwHGAADGRIRVALAPHapYTCSDELLREVAELAREYGVPLHIHlAETEDEVEESL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 210 QR--------ILDLGITGPE---GH-VLSRPEEVEAEAvNRSITIAnqtNCPlyvTKVMpKSAAEV--IAQARKKGtvvy 275
Cdd:cd01298 226 EKygkrpveyLEELGLLGPDvvlAHcVWLTDEEIELLA-ETGTGVA---HNP---ASNM-KLASGIapVPEMLEAG---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 276 gepITASLGTDGShywsknwakaaafvtspplspdpttpdflnsllSCGD-LQVTGSAHCTFNTaQKAVGKDNFTLIPEg 354
Cdd:cd01298 294 ---VNVGLGTDGA---------------------------------ASNNnLDMFEEMRLAALL-QKLAHGDPTALPAE- 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 355 tngteermsviwdkavvtgkmdenQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNif 434
Cdd:cd01298 336 ------------------------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVHDPISHLVYS-- 388
|
490 500
....*....|....*....|....*..
gi 1915913 435 egmeCRGSP--LVVISqGKIVLEDGTL 459
Cdd:cd01298 389 ----ANGGDvdTVIVN-GRVVMEDGEL 410
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
66-466 |
3.42e-09 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 58.62 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 66 IPGGIDVHTrfQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIT--E 143
Cdd:cd01316 5 LPGLIDVHV--HLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATstN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 144 WHKGIQeemealVKDHGVNS-FLVYMAFKDrfqLTDSQIYEVLSVIrdigaiaQVHAENGDIIAEAQQRILdlgitgpeG 222
Cdd:cd01316 83 AATVGE------LASEAVGLkFYLNETFST---LILDKITAWASHF-------NAWPSTKPIVTHAKSQTL--------A 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 223 HVLsrpeeVEAEAVNRSITIANQTNcplyvtkvmpKSAAEVIAQARKKGTVVYGEPITASLgtdgshYWSKNWAKAAAFV 302
Cdd:cd01316 139 AVL-----LLASLHNRSIHICHVSS----------KEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 303 TSPPLsPDPTTPDFLNSLLSCGDLQVTGSAHCTFntAQKAVGKdnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 382
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 383 VTSTNAAKVFNLYPrkgrisvgsDADLVI-WDPDSVKTISAKTHNSALEYNIFEGMECRGSPLVVISQGKIVLEDGTLHV 461
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 1915913 462 TEGSG 466
Cdd:cd01316 340 PPGFG 344
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
35-455 |
2.45e-08 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 56.25 E-value: 2.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 35 IYMEDGLIKQIGENLivpGGVKTIEAHSRMVIPGGIDVHTRfqMPDQGMtSADDFFQGTKAALAGGttmiIDHVVPEPGT 114
Cdd:PRK08417 1 IRIKDGKITEIGSDL---KGEEILDAKGKTLLPALVDLNVS--LKNDSL-SSKNLKSLENECLKGG----VGSIVLYPDS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 115 SllaafdqwrewadsKSCCD-YSLhvditEWHKGIQEEMEalvkdhgVNSFLVYMAFKDRFQLTDsqiyevLSVIRDIGA 193
Cdd:PRK08417 71 T--------------PAIDNeIAL-----ELINSAQRELP-------MQIFPSIRALDEDGKLSN------IATLLKKGA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 194 IAqVHAE---NGDIIAEAQQR---------------------ILDLGITGPEGHVLSRPEEVEAEAVNRSITIANQTNCP 249
Cdd:PRK08417 119 KA-LELSsdlDANLLKVIAQYakmldvpifcrcedssfddsgVMNDGELSFELGLPGIPSIAETKEVAKMKELAKFYKNK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 250 -LYVTKVMPKSAaEVIAQARKKGTVVYGEPITASLGTDGSHywSKNWAKAAAFvtSPPLSpDPTTPDFLNSLLSCGDLQV 328
Cdd:PRK08417 198 vLFDTLALPRSL-ELLDKFKSEGEKLLKEVSIHHLILDDSA--CENFNTAAKL--NPPLR-SKEDRLALLEALKEGKIDF 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 329 TGSAHC-TFNTAQKAVgkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRISVGSDA 407
Cdd:PRK08417 272 LTSLHSaKSNSKKDLA----FDEAAFGIDSICEYFSLCYTYLVKEGIITWSELSRFTSYNPAQFLGL--NSGEIEVGKEA 345
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1915913 408 DLVIWDPDSVKTISAKthnsaleYNIFEGMECRGSPLVVISQGKIVLE 455
Cdd:PRK08417 346 DLVLFDPNESTIIDDN-------FSLYSGDELYGKIEAVIIKGKLYLE 386
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-220 |
1.56e-07 |
|
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: 53.68 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 16 RLLIKGGKIV--NDDQSFYAD--IYMEDGLIKQIGENLIVP---GGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSAD 87
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 88 DFFQ--------------------GTKAA----LAGGTTMIIDHvvpepGTSLLAAFDQWREWAD--------SKSCCDY 135
Cdd:COG0402 81 PLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADF-----YYVHPESADALAEAAAeagiravlGRGLMDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 136 SLHVDITEWHKGIQEEMEALVKD-HGVNSFLVYMAFKDRF--QLTDSQIYEVLSVIRDIGAIAQVH-AENGDIIAEAQ-- 209
Cdd:COG0402 156 GFPDGLREDADEGLADSERLIERwHGAADGRIRVALAPHApyTVSPELLRAAAALARELGLPLHTHlAETRDEVEWVLel 235
|
250
....*....|....*..
gi 1915913 210 ------QRILDLGITGP 220
Cdd:COG0402 236 ygkrpvEYLDELGLLGP 252
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-415 |
2.38e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 52.97 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTrfqmpdqgmtsaddffQGtkaa 96
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHI----------------HG---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 97 lAGGttmiidhvvpepgtsllAAFDQWRewadsksccdyslhvditewHKGIQEEMEALVKdHGVNSFLVYMafkdrfqL 176
Cdd:cd00854 61 -GGG-----------------ADFMDGT--------------------AEALKTIAEALAK-HGTTSFLPTT-------V 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 177 TDS--QIYEVLSVIRD-----IGA-IAQVHAEnGDIIAE----AQqrildlgitgPEGHVLS-RPEEVE-----AEAVNR 238
Cdd:cd00854 95 TAPpeEIAKALAAIAEaiaegQGAeILGIHLE-GPFISPekkgAH----------PPEYLRApDPEELKkwleaAGGLIK 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 239 SITIAnqtncplyvtkvmP--KSAAEVIAQARKKGtvvygepITASLG-TDGSHYWSKNWAKAAA-FVTS-----PPLS- 308
Cdd:cd00854 164 LVTLA-------------PelDGALELIRYLVERG-------IIVSIGhSDATYEQAVAAFEAGAtHVTHlfnamSPLHh 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 309 --PDPTTPDFLNSLLSCG---DLQvtgsaHC---TFNTAQKAVGKDNFTLI---------PEGT---NGTEERM------ 362
Cdd:cd00854 224 rePGVVGAALSDDDVYAEliaDGI-----HVhpaAVRLAYRAKGADKIVLVtdamaaaglPDGEyelGGQTVTVkdgvar 298
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1915913 363 --------SVI-WDKAVVT----GKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 415
Cdd:cd00854 299 ladgtlagSTLtMDQAVRNmvkwGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
381-415 |
8.19e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 51.25 E-value: 8.19e-07
10 20 30
....*....|....*....|....*....|....*
gi 1915913 381 VAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPD 415
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-89 |
1.19e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.00 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT--------RFQMP------- 79
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVhvypgstpYGDEPdevgvrs 80
|
90
....*....|....*.
gi 1915913 80 ------DQGMTSADDF 89
Cdd:PRK09237 81 gvttvvDAGSAGADNF 96
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-424 |
8.78e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 48.44 E-value: 8.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 33 ADIYMEDGLIKQIGENLI-VPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTM--IIDHVV 109
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRvaILPDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 110 P---EPGTslLAAFDQ---------WREWAD-SKSCCDYSLhvdiTEWhkgiQEEMEAlvkdhGVNSFlvymafkdrfql 176
Cdd:PRK07369 100 PpldNPAT--LARLQQqaqqippvqLHFWGAlTLGGQGKQL----TEL----AELAAA-----GVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 177 TDSQIYEVLSVIRDIGAIAQVH-------AENGDIIAEAQQR----ILDLGITGpeghvlsRPEEVEAEAVNRSITIANQ 245
Cdd:PRK07369 153 TDGQPLENLALLRRLLEYLKPLgkpvalwPCDRSLAGNGVMRegllALRLGLPG-------DPASAETTALAALLELVAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 246 TNCPLYVTKVMPKSAAEVIAQARKKGTvvygePITAS-------LGT-DGSHYwSKNWAKAaafvtsPPLsPDPTTPDFL 317
Cdd:PRK07369 226 IGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD------PPL-GNPSDRQAL 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 318 NSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPR 397
Cdd:PRK07369 293 IEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQEPP 369
|
410 420
....*....|....*....|....*..
gi 1915913 398 kgRISVGSDADLVIWDPDSVKTISAKT 424
Cdd:PRK07369 370 --SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-74 |
3.75e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.25 E-value: 3.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1915913 18 LIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENliVPGGVKTIEAHSRMVIPGGIDVHT 74
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
381-436 |
6.44e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 45.60 E-value: 6.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1915913 381 VAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDSVKTISAKTHNSALEYNIFEG 436
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-113 |
8.56e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.05 E-value: 8.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 16 RLLIKGGKIVN-----DDQsfyADIYMEDGLIKQIGEnliVPGGV---KTIEAHSRMVIPGGIDVHTRFQMPdqGMTSAD 87
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110
....*....|....*....|....*....|.
gi 1915913 88 DFFQGTKAALAGGTTMII-----DHVVPEPG 113
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPG 104
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
396-474 |
9.95e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 45.07 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 396 PRKGRISVGSDADLVIWDPDSVK---TISAKTHNSaleynifEGMEcrgsplVVISQGKIVLEDGTLHVTEGSGRYIpRK 472
Cdd:PRK09061 441 RRKGRLQAGADADIVVFDPETITdraTFEDPNRPS-------EGVR------HVLVNGVPVVSNGELVRDARPGRPV-RR 506
|
..
gi 1915913 473 PF 474
Cdd:PRK09061 507 PV 508
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-74 |
1.51e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 44.41 E-value: 1.51e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915913 17 LLIKGGKI------VNDDQsfyADIYMEDGlikQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 74
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHT 60
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-103 |
2.07e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 44.01 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 16 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvkTIEAHSRMVIPGGIDVHT----RFQMP--------DQGM 83
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHTdnleKHLAPrpgvdwpaDAAL 80
|
90 100
....*....|....*....|
gi 1915913 84 TSADdffqgTKAALAGGTTM 103
Cdd:PRK15446 81 AAHD-----AQLAAAGITTV 95
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
383-423 |
3.26e-04 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 43.15 E-value: 3.26e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1915913 383 VTSTNAAKVFNLYPrKGRISVGSDADLVIWDPD-SVKTISAK 423
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
356-416 |
3.46e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 43.02 E-value: 3.46e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1915913 356 NGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRISVGSDADLVIWDPDS 416
Cdd:cd01296 291 SSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPS 351
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
19-101 |
3.88e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 43.35 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 19 IKGGKIVNDDQSFYADiyMEDGlikqIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSaddFFQGTKAALA 98
Cdd:PRK13985 87 IKDGKIAGIGKGGNKD--MQDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGVTTMIG 157
|
...
gi 1915913 99 GGT 101
Cdd:PRK13985 158 GGT 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-78 |
4.40e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 42.87 E-value: 4.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915913 17 LLIKGGKIVNDD--QSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQM 78
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-112 |
6.29e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 42.30 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 15 DRLLIKGGKIVNDDQSF----YADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVH-------TRFQMPD--- 80
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHrhtwqsvLRGIGADwtl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1915913 81 -----------QGMTSADDFFQGTKA----ALAGGTTMIID--HVVPEP 112
Cdd:PRK08204 81 qtyfreihgnlGPMFRPEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-413 |
1.59e-03 |
|
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: 40.77 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 34 DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSADDFfqgtkaALAGGTTMIIDhvvpep 112
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHvYQGGTRYGDRPDMI------GVKSGVTTVVD------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 113 gtsllaafdqwrewADSKSCCDyslhvditewhkgIQEEMEALVKDHGVNsFLVYMAFKDRFQLTDSQIYEVLSVirDIG 192
Cdd:cd01307 69 --------------AGSAGADN-------------IDGFRYTVIERSATR-VYAFLNISRVGLVAQDELPDPDNI--DED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 193 AIAQVHAENGDIIAEAQQRIlDLGITGPEGhvlsrpeeveAEAVNRSITIANQTNCPLYV-TKVMPKSAAEVIAQARKkg 271
Cdd:cd01307 119 AVVAAAREYPDVIVGLKARA-SKSVVGEWG----------IKPLELAKKIAKEADLPLMVhIGSPPPILDEVVPLLRR-- 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 272 tvvyGEPITaslgtdgsHYWSknwAKAAAFVTSpplspdptTPDFLNSLLSCGDLQVT-----GSAHCTFNTAQKAVGKD 346
Cdd:cd01307 186 ----GDVLT--------HCFN---GKPNGIVDE--------EGEVLPLVRRARERGVIfdvghGTASFSFRVARAAIAAG 242
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1915913 347 nftLIPEgTNGTE----ERMSV-IWDKAVVTGK-----MDENQFVAVTSTNAAKVFNLyPRKGRISVGSDADLVIWD 413
Cdd:cd01307 243 ---LLPD-TISSDihgrNRTNGpVYALATTLSKllalgMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
33-105 |
1.69e-03 |
|
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis of urea to form ammonia and carbon dioxide. Nickel-dependent ureases are found in bacteria, fungi and plants. Their primary role is to allow the use of external and internally generated urea as a nitrogen source. The enzyme consists of 3 subunits, alpha, beta and gamma, which can be fused and present on a single protein chain and which in turn forms multimers, mainly trimers. The large alpha subunit is the catalytic domain containing an active site with a bi-nickel center complexed by a carbamylated lysine. The beta and gamma subunits play a role in subunit association to form the higher order trimers.
Pssm-ID: 238221 [Multi-domain] Cd Length: 567 Bit Score: 41.16 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 33 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 100
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQ-----------IEEALASG 151
|
....*
gi 1915913 101 TTMII 105
Cdd:cd00375 152 ITTMI 156
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-74 |
2.11e-03 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 40.69 E-value: 2.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915913 12 ITSDRLLIKGGKIVnddqsfyaDIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 74
Cdd:cd01293 2 LRNARLADGGTALV--------DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHI 56
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
383-467 |
2.82e-03 |
|
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: 40.47 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 383 VTSTNAAKVFNLyPRKGRISVGSDADLVIW--DPDSVKTISAKTHNSALEYnifegmecrgsPLVVISQGKIVLEDGTLh 460
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYddDPDQVDPSDYEKVEKAFSR-----------AAYVLKDGEIVVKDGEV- 501
|
....*..
gi 1915913 461 VTEGSGR 467
Cdd:cd01304 502 VAEPWGR 508
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-106 |
3.12e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.47 E-value: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 17 LLIKGGKIVN--DDQSFYADIYMEDGLIKQIGEnlIVPGGVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDFfqgTK 94
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHI---ESSMVTPAEF---AR 78
|
90
....*....|...
gi 1915913 95 AALAGGTT-MIID 106
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
388-473 |
3.51e-03 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 40.16 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 388 AAKVFNLYPRkGRISVGSDADLVIWDPDSVKtiSAKTHNSALEYNifEGMECrgsplVVISqGKIVLEDGTlHVTEGSGR 467
Cdd:COG3653 453 PADRLGLKDR-GLLRPGYRADLVVFDPATLA--DRATFDLPAQRA--DGIRA-----VIVN-GVVVVEDGK-PTGARPGR 520
|
....*.
gi 1915913 468 YIPRKP 473
Cdd:COG3653 521 VLRGGG 526
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
33-104 |
3.69e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.08 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 33 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 100
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL-----------VDHALASG 155
|
....*
gi 1915913 101 -TTMI 104
Cdd:PRK13308 156 iTTML 160
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-415 |
5.78e-03 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 39.22 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 39 DGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT---------RFQMPDQGMTSAD--------DFFQ----GTKAAL 97
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHShlgldeeggVRETSDANEETDPvtphvraiDGINpddeAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 98 AGGTTmiidHVVPEPGTSLLAAfdqwREWADSKSccdyslhvditewhKGIQEEMEALVKDHGVNSFLVYMAFK--DRFQ 175
Cdd:cd01309 81 AGGVT----TVQVLPGSANLIG----GQGVVIKT--------------DGGTIEDMFIKAPAGLKMALGENPKRvyGGKG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 176 LTDSQIYEVLSVIRDIGAIAQVHAEngdiiaeAQQRILDLGITGPEghvlSRPE-EVEAEAVNRSItianqtncPLYVTK 254
Cdd:cd01309 139 KEPATRMGVAALLRDAFIKAQEYGR-------KYDLGKNAKKDPPE----RDLKlEALLPVLKGEI--------PVRIHA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 255 VMPKSAAEVIAQARKkgtvvYGEPITASLGTDGsHYWSKNWAKAAAFVTSPPLSPDPTTPDFLNSLlscgdlqvtgsahc 334
Cdd:cd01309 200 HRADDILTAIRIAKE-----FGIKITIEHGAEG-YKLADELAKHGIPVIYGPTLTLPKKVEEVNDA-------------- 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915913 335 TFNTAQ-KAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTStNAAKVFNLYPRKGRISVGSDADLVIWD 413
Cdd:cd01309 260 IDTNAYlLKKGGVAFAISSDHPVLNIRNLNLEAAKAVKYGLSYEEALKAITI-NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
..
gi 1915913 414 PD 415
Cdd:cd01309 339 GD 340
|
|
| |
