|
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: 735.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 96
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKdHGVNSFLVYMAFKDRFQL 176
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 177 TDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVM 256
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 257 SKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSPDpTTPDFLNSLLSCGDLQVTGSAHCTF 336
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 337 NTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDS 416
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 4503377 417 VKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSG 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: 678.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 96
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQL 176
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 177 TDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVM 256
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 257 SKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTF 336
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 337 NTAQK-AVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 415
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 4503377 416 SVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 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: 585.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 16 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlivpGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKA 95
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 96 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVkDHGVNSFLVYMAFKDRFQ 175
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 176 LTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKV 255
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 256 MSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCT 335
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 336 FNTAQKA-VGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP 414
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503377 415 DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 475
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
12-475 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 549.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 12 ITSDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQ 91
Cdd:PLN02942 2 ASSTKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 92 GTKAALAGGTTMIIDHVVPEPGtSLLAAFDQWREWADsKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFK 171
Cdd:PLN02942 82 GQAAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 172 DRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLY 251
Cdd:PLN02942 160 GSLMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 252 ITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGS 331
Cdd:PLN02942 240 VVHVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 332 AHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVI 411
Cdd:PLN02942 319 DHCPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIII 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503377 412 WDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 475
Cdd:PLN02942 399 LNPNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
18-471 |
4.43e-124 |
|
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: 372.12 E-value: 4.43e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 18 LIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAAL 97
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 98 AGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVkDHGVNSFLVYMAFKD-RFQL 176
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 177 TDCQIYEVLSVIRDIGAIAQVHAENGDIIAEeqqRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVM 256
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 257 SKSSAEVIAQARKKGTVVYGE--P----ITAS-LGTDGSHYwsknwakaaafVTSPPLsPDPTTPDFL-NSLLScGDLQV 328
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPL-RTEEDREALwEGLAD-GTIDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 329 TGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDAD 408
Cdd:COG0044 302 IATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADAD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503377 409 LVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 471
Cdd:COG0044 378 LVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
17-471 |
1.71e-121 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 366.72 E-value: 1.71e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPD-QGMTSADDFFQGTKA 95
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 96 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGI-QEEMEALVKDhGVNSFLVYMAFkDRF 174
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 175 QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK 254
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 255 VMSKSSAEVIAQARKKGTVVYGEP------ITAS-LGTDGSHywsknwakAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQ 327
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 328 VTGSAHCTFN---TAQKAVGKDN--FTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIA 402
Cdd:PRK13404 313 VFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503377 403 VGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 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 |
8.52e-65 |
|
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: 218.31 E-value: 8.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSccdyslHVDISEWH-------KGIQEEMEALVKdhGVNSFLV 166
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKL------HVDVGFWGglvpgnlDQLRPLDEAGVV--GFKCFLC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 167 YMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQT 246
Cdd:cd01315 150 PSGVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 247 NCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPLSpDPTTPDFLNS 319
Cdd:cd01315 230 GCRLHIVHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 320 LLSCGDLQVTGSAH--CTfnTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPR 397
Cdd:cd01315 298 ALENGDIDMVVSDHspCT--PELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQ 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4503377 398 KGRIAVGSDADLVIWDPDSVKTISAkthnSSLEY----NIFEGMECRGSPLVVISQGKIVLEDGTlHVTEGSGRYI 469
Cdd:cd01315 376 KGRIAVGYDADFVVWDPEEEFTVDA----EDLYYknkiSPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
65-443 |
3.81e-61 |
|
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: 205.32 E-value: 3.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 65 VIPGGIDVHTRFQMPDQGMTSaDDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEw 144
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 145 hkGIQEEMEALVKDHGVNSFLVYMAFK--DRFQLTDCQIYEVLSVIRDIGAIAQVHAEngdiiaeeqqrildlgitgpeg 222
Cdd:cd01302 81 --GDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 223 hvlsrpeeveaeavnRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGShYWSKNWAKaaaFV 302
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 303 TSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDnFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 382
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503377 383 VTSTNAAKVFNLYPrKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSP 443
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
17-472 |
3.62e-54 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 189.86 E-value: 3.62e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHvdisewhKGIQEEMEALVK--DHGVNSF-LVYMA---- 169
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGIN-------GGVTGNWDPLESlwERGVFALgEIFMAdstg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 170 ----FKDRFQltdcqiyEVLSVIRDIGAIAQVHAENGDIIaEEQQRILDlGITGPEGHVLSRPEEVEAEAVNRAITIANQ 245
Cdd:PRK02382 155 gmgiDEELFE-------EALAEAARLGVLATVHAEDEDLF-DELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 246 TNCPLYITKVmskSSAEVIAQARKKGTVVYGEPITASLGTDgshywskNWAKAAAFV-TSPPLSPDPTTPDFLNSLLScG 324
Cdd:PRK02382 226 TGARIHIAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRREALWERLND-G 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 325 DLQVTGSAHCTFNTAQKAVG-KDnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAV 403
Cdd:PRK02382 295 TIDVVASDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAE 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 404 GSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMEcrGS-PLVVISQGKIVLEDGTLHVTEGSGRYIPRK 472
Cdd:PRK02382 369 GYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
17-460 |
1.08e-52 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 186.06 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLhvdiseWHKGIQEEMEALVK--DHGVNSFLVYMAFK 171
Cdd:PRK06189 82 AAGGCTTYFD--MPlnsIPPTVTREALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 172 --DRFQLTD-CQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNC 248
Cdd:PRK06189 154 gtDEFRSSDdLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 249 PLYITKVMSKSSAEVIAQARKKGtvvygepITASLGTdGSHY--WSKN--WAKAAAFVTSPPLSpDPTTPDFLNSLLSCG 324
Cdd:PRK06189 234 PLHFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYllFTEEdfERIGAVAKCAPPLR-SRSQKEELWRGLLAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 325 DLQVTGSAH--CTFNTAQkavgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIA 402
Cdd:PRK06189 305 EIDMISSDHspCPPELKE----GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503377 403 VGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLH 460
Cdd:PRK06189 380 VGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
17-470 |
3.20e-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: 176.42 E-value: 3.20e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKsccdysLHVDISEWH-------KGIQEEMEALVkdHGVNSFLV 166
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGK------LAVDVGFWGglvpynlDDLRELDEAGV--VGFKAFLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 167 YMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQT 246
Cdd:TIGR03178 149 PSGDDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 247 NCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAK----AAAFVTSPPLSpDPTTPDFLNSLLS 322
Cdd:TIGR03178 229 GCRVHVVHLSSAEAVELITEAKQEGLDVTVETCP--------HYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 323 CGDLQVTGSAHCTFNTAQKAvgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIA 402
Cdd:TIGR03178 300 NGLIDCVVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIA 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4503377 403 VGSDADLVIWDPDSVKTISakthNSSLEY----NIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIP 470
Cdd:TIGR03178 377 PGKDADFVFVDPDESYTLT----PDDLYYrhkvSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
33-456 |
3.11e-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: 170.32 E-value: 3.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 33 ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIID--HVVP 110
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADmpNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 111 EPGTSllAAFDQWREWADSKSCCDYSLHVDISEWHKGiQEEMEAlvkdhgvnSFLVYMA-----FKDRFQ--LTDCQIYE 183
Cdd:TIGR00857 83 PIDTP--ETLEWKLQRLKKVSLVDVHLYGGVTQGNQG-KELTEA--------YELKEAGavgrmFTDDGSevQDILSMRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 184 VLSVIRDIGAIAQVHAENGDIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEV 263
Cdd:TIGR00857 152 ALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 264 IAQARKkgtvvYGEPITAS------LGTDGSHYWSKNWAKaaafvTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFN 337
Cdd:TIGR00857 229 IVKAKS-----QGIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 338 TAQKAVgkdNFTLIPEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSV 417
Cdd:TIGR00857 298 LEEKTK---EFAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKE 372
|
410 420 430
....*....|....*....|....*....|....*....
gi 4503377 418 KTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLED 456
Cdd:TIGR00857 373 WTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
65-450 |
3.25e-37 |
|
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: 141.32 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 65 VIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEw 144
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 145 hkgiQEEMEALVKdHGVNSFLVYMA--FKDRFQltdcqIYEVLSVI-RDIGAIAQVHAENGDIIAEEQQRILDLGItgpe 221
Cdd:cd01318 81 ----SEDLEELDK-APPAGYKIFMGdsTGDLLD-----DEETLERIfAEGSVLVTFHAEDEDRLRENRKELKGESA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 222 gHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVvygePITAS--LGTDGSHYWSKNWAKaa 299
Cdd:cd01318 147 -HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTV----EVTPHhlFLDVEDYDRLGTLGK-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 300 afvTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVI---WDKAVVTGKmd 376
Cdd:cd01318 220 ---VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILSLS-- 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503377 377 enQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQG 450
Cdd:cd01318 291 --RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
54-444 |
1.31e-33 |
|
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: 131.59 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 54 GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTmiidHVVPEPGTsllaafdqwREWADSKSCC 133
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVIDNPAVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 134 DYSLH----VDISEWH------KGIQ----EEMEALvKDHGVNSFlvymaFKDRFQLTDCQI-YEVLSVIRDIGAIAQVH 198
Cdd:cd01317 66 ELLKNrakdVGIVRVLpigaltKGLKgeelTEIGEL-LEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 199 AENGDIIAEEQqrILDLGITGPEGhVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGtvvygEP 278
Cdd:cd01317 140 PEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 279 ITASLGtdgSHYWS------KNWAkaAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIP 352
Cdd:cd01317 212 VTAEVT---PHHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 353 EGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPrkGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYN 432
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNT 360
|
410
....*....|..
gi 4503377 433 IFEGMECRGSPL 444
Cdd:cd01317 361 PFDGQKLKGRVL 372
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
64-453 |
1.45e-31 |
|
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: 124.92 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 64 MVIPGGIDVHTRFQM------PDQGMTSADDFFQGTKAALAGGTTMIIDHVV--PEPGTSLLAAFDQW----REWAdsKS 131
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELplglRFLG--PG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 132 CC---DYSLHVDISEWHKGIQEEMEALVKDHGVnsFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDiiAEE 208
Cdd:pfam01979 79 CSldtDGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETK--GEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 209 QQRILDLGITGPEGHVLSRPEEVeaeAVNRAITIANQTNCPLyitkvmSKSSAEVIAQARKKGTVVygepitasLGTDGS 288
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESG---GLLDIIKLILAHGVHL------SPTEANLLAEHLKGAGVA--------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 289 HYWSKNWAKAAAfvtspplspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkaVGKDNFTLIPEGTNGTEERmsviwdk 368
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 369 AVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSvktisakthnssleYNIFEGMECRGSPLVVIS 448
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------------LAAFFGLKPDGNVKKVIV 329
|
....*
gi 4503377 449 QGKIV 453
Cdd:pfam01979 330 KGKIV 334
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
16-456 |
4.06e-31 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 125.69 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 16 RLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPDQgmTSADDFFQGTK 94
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREPGQ--EDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 95 AALAGGTTMiidhVVPEPGT----SLLAAFDQWREWADSKSCCDysLHV--DISEWHKGIQE-EMEALvKDHGV------ 161
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNTkpviDTPEVVEYVLDRAKEAGLVD--VLPvgAITKGLAGEELtEFGAL-KEAGVvafsdd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 162 -----NSFLVYMAFK--DRFQLTDCQIYEVLSVIRdiGAIAqvhaeNGDIIAEEqqrildLGITGpeghvlsRPEEVEAE 234
Cdd:PRK09357 152 gipvqDARLMRRALEyaKALDLLIAQHCEDPSLTE--GGVM-----NEGEVSAR------LGLPG-------IPAVAEEV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 235 AVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTvvygePITA------------SLGTDGSHYwsknwaKAAafv 302
Cdd:PRK09357 212 MIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 303 tsPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVA 382
Cdd:PRK09357 278 --PPLRTEEDREALIEGLKD-GTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLE 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503377 383 VTSTNAAKVFNLYPrkGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLED 456
Cdd:PRK09357 352 KMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
17-431 |
2.00e-30 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 124.20 E-value: 2.00e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDHVVPE-PGTSLLAAFDQWREWADSKsccdysLHVDISEWHKGIQEEMEAL--VKDHGVNSFLVYMAF-KD 172
Cdd:PRK08044 81 AKGGITTMIEMPLNQlPATVDRASIELKFDAAKGK------LTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 173 R-----FQ-LTDCQIYEVLSVIRDIGAIAQVHAENG---DIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRAITIA 243
Cdd:PRK08044 155 RgidndFRdVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRVLYLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 244 NQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPLSPDPTTPDFLNS 319
Cdd:PRK08044 232 KVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 320 LLScGDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKG 399
Cdd:PRK08044 304 LFN-GEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKG 378
|
410 420 430
....*....|....*....|....*....|..
gi 4503377 400 RIAVGSDADLVIWDPDSvktiSAKTHNSSLEY 431
Cdd:PRK08044 379 RIAPGKDADFVFIQPNS----SYVLKNEDLEY 406
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
14-457 |
1.64e-28 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 118.24 E-value: 1.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 14 SDRLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQG 92
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 93 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISewhkgiQEEMEALVKDHGVNSFLVYMAFKD 172
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMGSSH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 173 RFQLTDCQiyEVLSVI--RDIGAIAqVHAENGDIIAEEQQRILdlGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPL 250
Cdd:PRK07575 154 GPLLVDEE--AALERIfaEGTRLIA-VHAEDQARIRARRAEFA--GISDPADHSQIQDEEAALLATRLALKLSKKYQRRL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 251 YITKVMSKSSAEVIAQArkKGTVVYGEPITASLGTDGSHYwsknwAKAAAFVT-SPPLSpDPTTPDFLNSLLSCGDLQVT 329
Cdd:PRK07575 229 HILHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAQmNPPLR-SPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 330 GSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVIWDKAVvTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADL 409
Cdd:PRK07575 301 ATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADL 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 4503377 410 VIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDG 457
Cdd:PRK07575 376 VLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
17-467 |
9.79e-27 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 113.09 E-value: 9.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 96
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 97 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISewHKGIQE--EMEALVKDHGVNsflVYM--AFKD 172
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGT--RDNADElaELERLPGCAGIK---VFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 173 RFQLTDCQIYEVLSVIRDIGAiaqVHAENGDIIAEEQqrilDLGITG-PEGHVLSRPEEVEAEAVNRAITIANQTNCPLY 251
Cdd:PRK09060 159 LLVEDDEGLRRILRNGRRRAA---FHSEDEYRLRERK----GLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 252 ITKVMSKSSAEVIAQARKKGTV--------VYGEPITASLGTdgshYWSKNwakaaafvtsPPLSpDPTTPDFLNSLLSC 323
Cdd:PRK09060 232 VLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGVRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 324 GDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKaVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAV 403
Cdd:PRK09060 297 GVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503377 404 GSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGR 467
Cdd:PRK09060 372 GYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
22-471 |
1.64e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 111.87 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 22 GKIVNDDQSFYADIYMEDGLIKQIGENLivpGGVKTIEAHSrMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGT 101
Cdd:PRK01211 5 GNFYYKGKFDYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 102 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHvdisewhkgiqeEME----ALVKDHGVNSFLVYMAFKDRFQLT 177
Cdd:PRK01211 79 TFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLY------------SMEtgnnALILDERSIGLKVYMGGTTNTNGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 178 DCQIYEVlSVIRDIGAIAQVHAENGDIIAEEQQRILDLgitgpEGHVLSRPEEVEAEAVNRAITIANQtncplyiTKVMS 257
Cdd:PRK01211 147 DIEGGEI-KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 258 -KSSAEVIAQARKKGT----VVYGEpitASLGTDGShywsknwakaaafvTSPPLSPDPTTPDFLNSLLScGDLQVTGSA 332
Cdd:PRK01211 214 hVSSIDVIGRFLREVTphhlLLNDD---MPLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 333 HCTFNTAQKAvgkdNFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRIAVGSDADLVIW 412
Cdd:PRK01211 276 HAPHTEEDKQ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAF 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 4503377 413 DPDSVKTISAKTHNSSLEYNIFEGMECRgSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 471
Cdd:PRK01211 349 DFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-472 |
4.83e-26 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 111.79 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 12 ITSDRLLIKGGKIVNDdqsfyadIYMEDGLIKQIGENLIVPG---GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADD 88
Cdd:PLN02795 48 LYSKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 89 FFQGTKAALAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKsccdysLHVDISEWHKGIQE------EMEALVkDH 159
Cdd:PLN02795 119 FPTGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 160 GV---NSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLgiTGPEGHVLSRPEEVEAEAV 236
Cdd:PLN02795 190 GAlglKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAI 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 237 NRAITIANQTN-------CPLYITKVM-SKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWsknwAKAAA-------- 300
Cdd:PLN02795 268 RQLLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtr 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 301 FVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGkMDENQF 380
Cdd:PLN02795 336 YKCAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQL 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 381 VAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDP------DSVKTISAKTHNSSleynIFEGMECRGSPLVVISQGKIVL 454
Cdd:PLN02795 414 ARWWSERPAKLAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHKHKSLS----PYLGTKLSGKVIATFVRGNLVF 488
|
490
....*....|....*...
gi 4503377 455 EDGtLHVTEGSGRYIPRK 472
Cdd:PLN02795 489 LEG-KHAKQACGSPILAK 505
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
22-469 |
5.13e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 110.24 E-value: 5.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 22 GKIVNDDQSFYADIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTRFQmpDQGMTSADDFFQGTKAALAGGT 101
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR--DFEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 102 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSflVYMAFKDRFQLTdcqi 181
Cdd:PRK04250 80 TLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGAS--TGGIFSENFEVD---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 182 YEVLSvirdigAIAQVHAENGDIIAEEqqrildlgitgPEghvlsRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSA 261
Cdd:PRK04250 154 YACAP------GIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTKDGL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 262 EVIAQARKKGTVVYGEPitaslgtdgSH--YWSKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDlqVTGSAHCTFNTA 339
Cdd:PRK04250 212 KLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP--IIASDHAPHTLE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 340 QKAVGKdnftlipEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNlYPRKGrIAVGSDADLVIWDPDSVKT 419
Cdd:PRK04250 280 DKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEWT 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 4503377 420 ISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYI 469
Cdd:PRK04250 350 IKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
15-138 |
9.60e-17 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 82.61 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 15 DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGID--VHTRfqmpDQGMTSADDFFQG 92
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR----EPGLTHKGDIASE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 4503377 93 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLH 138
Cdd:PRK09236 78 SRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFY 123
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
17-467 |
6.92e-13 |
|
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: 70.79 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVndDQS----FYADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDF--- 89
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHY---DGQVFWDPDLrps 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 90 -FQGTKAALAG------------GTTMIIDHVVPEPGTSLLAAFDqWREWAD-------SKSCCDYSLHV---DISEWHK 146
Cdd:cd01297 76 sRQGVTTVVLGncgvspapanpdDLARLIMLMEGLVALGEGLPWG-WATFAEyldaleaRPPAVNVAALVghaALRRAVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 147 GI---------QEEMEALVKDH------GVNSFLVYMafkDRFQLTDCQIYEVLSVIRDIGAIAQVHaengdiIAEEQQR 211
Cdd:cd01297 155 GLdareateeeLAKMRELLREAleagalGISTGLAYA---PRLYAGTAELVALARVAARYGGVYQTH------VRYEGDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 212 ILdlgitgpeghvlsrpeeveaEAVNRAITIANQTNCPLYIT--KVMSKSSAEVIAQ-------ARKKGTVVYGE--PIT 280
Cdd:cd01297 226 IL--------------------EALDELLRLGRETGRPVHIShlKSAGAPNWGKIDRllalieaARAEGLQVTADvyPYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 281 ASLGTDgshywsknwakAAAFVTSPPlspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkavgkdnftlipeGTNGTEE 360
Cdd:cd01297 286 AGSEDD-----------VRRIMAHPV-------------VMGGSDGGALGKPHP-------------------RSYGDFT 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 361 RMSVIW--DKAVVTgkMDENqfVAVTSTNAAKVFNLYPRkGRIAVGSDADLVIWDPDSVK---TISAKTHNSsleynifE 435
Cdd:cd01297 323 RVLGHYvrERKLLS--LEEA--VRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------E 390
|
490 500 510
....*....|....*....|....*....|..
gi 4503377 436 GMEcrgspLVVISqGKIVLEDGtLHVTEGSGR 467
Cdd:cd01297 391 GIE-----AVLVN-GVPVVRDG-AFTGARPGR 415
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
13-422 |
7.44e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 64.21 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 13 TSDRLLIKGGKIVNDDQSFY---ADIYMEDGLIKQIGEN--LIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPD------- 80
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGgravefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 81 --QGMTSADDFFQGT----KAALAGGTTMIIDHvvpePGTSL----------LAAFDQWREWAdskscCDYSLHVDISEW 144
Cdd:COG1228 86 agGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRVLA-----AGPALSLTGGAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 145 HKGIQEEMEAL--VKDHGVNSFLVYMAFKDRfQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIaeeqQRILDLGITGPEg 222
Cdd:COG1228 157 ARGPEEARAALreLLAEGADYIKVFAEGGAP-DFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 223 HVLSRpeeveaeavnraitianqtncplyitkvmsksSAEVIAQARKKGTVVYGePiTASLGTDGSHYWSKNWAKAAAFV 302
Cdd:COG1228 231 HGTYL--------------------------------DDEVADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARKV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 303 tspplspDPTTPDFLNSLLSCGDLQVTGSAHctfntaqkavgkdNFTLIPEGTNGTEERMsviwdkaVVTGKMDENQ-FV 381
Cdd:COG1228 277 -------REAALANARRLHDAGVPVALGTDA-------------GVGVPPGRSLHRELAL-------AVEAGLTPEEaLR 329
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 4503377 382 AVTStNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISA 422
Cdd:COG1228 330 AATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
66-466 |
2.71e-09 |
|
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate synthetase-aspartate transcarbamoylase-dihydroorotase, which catalyzes the first three steps of de novo pyrimidine nucleotide biosynthesis. Dihydroorotase (DHOase) catalyzes the third step, the reversible interconversion of carbamoyl aspartate to dihydroorotate.
Pssm-ID: 238641 [Multi-domain] Cd Length: 344 Bit Score: 59.00 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 66 IPGGIDVHTrfQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIS--E 143
Cdd:cd01316 5 LPGLIDVHV--HLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATstN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 144 WHKGIQeemealVKDHGVNS-FLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAqVHAENGDIIAeeqqrILDLgitgpeg 222
Cdd:cd01316 83 AATVGE------LASEAVGLkFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 223 hvlsrpeeveAEAVNRAItianqtncplYITKVMSKSSAEVIAQARKKGTVVYGEPITASLgtdgshYWSKNWAKAAAFV 302
Cdd:cd01316 144 ----------ASLHNRSI----------HICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 303 TSPPLsPDPTTPDFLNSLLSCGDLQVTGSAHCTFntAQKAVGKdnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 382
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 383 VTSTNAAKVFNLYPrkgriavgsDADLVI-WDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHV 461
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 4503377 462 TEGSG 466
Cdd:cd01316 340 PPGFG 344
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
17-459 |
4.17e-09 |
|
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: 58.75 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQS---FYADIYMEDGLIKQIGENLIVPG--GVKTIEAHSRMVIPGGIDVHTRFQM------------- 78
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 79 --------PDQGMTSADDFFQGTKAALA----GGTTMIIDHVVPEPGTSLLAA-------------FDQWREWADSKscc 133
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVAEAAeelgiravlgrgiMDLGTEDVEET--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 134 dyslhvdisewhKGIQEEMEALVKD-HGVNSFLVymafkdRFQLTDCQIYEV-LSVIRDIGAIA-------QVH-AENGD 203
Cdd:cd01298 158 ------------EEALAEAERLIREwHGAADGRI------RVALAPHAPYTCsDELLREVAELAreygvplHIHlAETED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 204 IIAEEQQR--------ILDLGITGPE---GH-VLSRPEEVEaeavnraitIANQTN-----CPlyiTKVMsKSSAEV--I 264
Cdd:cd01298 220 EVEESLEKygkrpveyLEELGLLGPDvvlAHcVWLTDEEIE---------LLAETGtgvahNP---ASNM-KLASGIapV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 265 AQARKKGtvvygepITASLGTDGShywsknwakaaafvtspplspdpttpdflnsllSCGD-LQVTGSAHCTFNTaQKAV 343
Cdd:cd01298 287 PEMLEAG-------VNVGLGTDGA---------------------------------ASNNnLDMFEEMRLAALL-QKLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 344 GKDNFTLIPEgtngteermsviwdkavvtgkmdenQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAK 423
Cdd:cd01298 326 HGDPTALPAE-------------------------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVH 379
|
490 500 510
....*....|....*....|....*....|....*...
gi 4503377 424 THNSSLEYNifegmeCRGSP--LVVISqGKIVLEDGTL 459
Cdd:cd01298 380 DPISHLVYS------ANGGDvdTVIVN-GRVVMEDGEL 410
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
17-415 |
1.84e-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: 53.35 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTrfqmpdQG------MTSADDFF 90
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHI------HGgggadfMDGTAEAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 91 QGTKAALAG-GTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDY-SLHVD---ISEWHKGIQEEmEALVKdhgvnsfL 165
Cdd:cd00854 75 KTIAEALAKhGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEIlGIHLEgpfISPEKKGAHPP-EYLRA-------P 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 166 VYMAFKDRFQLTDcqiyevlSVIRDIgAIAQVHAENGDIIaeeqQRILDLGITGPEGHVLSRPEEVEAeAVNRAITIA-- 243
Cdd:cd00854 147 DPEELKKWLEAAG-------GLIKLV-TLAPELDGALELI----RYLVERGIIVSIGHSDATYEQAVA-AFEAGATHVth 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 244 --NQtncplyitkvMSK-SSAE--VIaqarkkGTVVYGEPITASLGTDGSHywsknwakaaafvtsppLSPDpttpdfln 318
Cdd:cd00854 214 lfNA----------MSPlHHREpgVV------GAALSDDDVYAELIADGIH-----------------VHPA-------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 319 sllscgdlqvtgsahcTFNTAQKAVGKDNFTLI---------PEGT---NGTEERM--------------SVI-WDKAVV 371
Cdd:cd00854 253 ----------------AVRLAYRAKGADKIVLVtdamaaaglPDGEyelGGQTVTVkdgvarladgtlagSTLtMDQAVR 316
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 4503377 372 T----GKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 415
Cdd:cd00854 317 NmvkwGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
381-415 |
2.94e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 52.79 E-value: 2.94e-07
10 20 30
....*....|....*....|....*....|....*
gi 4503377 381 VAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 415
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
33-424 |
3.67e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 52.68 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 33 ADIYMEDGLIKQIGENLI-VPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTM--IIDHVV 109
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRvaILPDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 110 P---EPGTslLAAFDQ---------WREWAD-SKSCCDYSLhvdiSEWhkgiQEEMEAlvkdhGVNSFlvymafkdrfql 176
Cdd:PRK07369 100 PpldNPAT--LARLQQqaqqippvqLHFWGAlTLGGQGKQL----TEL----AELAAA-----GVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 177 TDCQIYEVLSVIRDIGAIAQVH-------------AENGdiIAEEQQRILDLGITGpeghvlsRPEEVEAEAVNRAITIA 243
Cdd:PRK07369 153 TDGQPLENLALLRRLLEYLKPLgkpvalwpcdrslAGNG--VMREGLLALRLGLPG-------DPASAETTALAALLELV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 244 NQTNCPLYITKVMSKSSAEVIAQARKKGTvvygePITAS-------LGT-DGSHYwSKNWAKAaafvtsPPLsPDPTTPD 315
Cdd:PRK07369 224 AAIGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD------PPL-GNPSDRQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 316 FLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLY 395
Cdd:PRK07369 291 ALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQE 367
|
410 420
....*....|....*....|....*....
gi 4503377 396 PRkgRIAVGSDADLVIWDPDSVKTISAKT 424
Cdd:PRK07369 368 PP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
16-456 |
4.58e-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: 52.52 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 16 RLLIKGGKIV--NDDQSFYAD--IYMEDGLIKQIGENLIVP---GGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSAD 87
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 88 DFFQ--------------------GTKAA----LAGGTTMIIDHvvpepGTSLLAAFDQWREWAD--------SKSCCDY 135
Cdd:COG0402 81 PLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADF-----YYVHPESADALAEAAAeagiravlGRGLMDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 136 SLHVDISEWHKGIQEEMEALVKD-HGVNSFLVymafkdRFQLTDCQIYEV-LSVIRDIGAIA-------QVH-----AEN 201
Cdd:COG0402 156 GFPDGLREDADEGLADSERLIERwHGAADGRI------RVALAPHAPYTVsPELLRAAAALArelglplHTHlaetrDEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 202 GDIIAEEQQRILD----LGITGPE---GH-VLSRPEEVEAEAVNRAiTIAnqtNCPLyitkvmskSSAEV------IAQA 267
Cdd:COG0402 230 EWVLELYGKRPVEyldeLGLLGPRtllAHcVHLTDEEIALLAETGA-SVA---HCPT--------SNLKLgsgiapVPRL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 268 RKKGtvvygepITASLGTDGshywsknwakaaafvtspplSPDPTTPDFLNSLLSCGDLqvtgsahctfntaQKAVGKDn 347
Cdd:COG0402 298 LAAG-------VRVGLGTDG--------------------AASNNSLDMFEEMRLAALL-------------QRLRGGD- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 348 ftlipegtngtEERMSviWDKAvvtgkmdenqFVAVTsTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSvktisakTHNS 427
Cdd:COG0402 337 -----------PTALS--AREA----------LEMAT-LGGARALGLDDEIGSLEPGKRADLVVLDLDA-------PHLA 385
|
490 500 510
....*....|....*....|....*....|.
gi 4503377 428 SLEYNIFEGMECRGSPLV--VISQGKIVLED 456
Cdd:COG0402 386 PLHDPLSALVYAADGRDVrtVWVAGRVVVRD 416
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
17-89 |
1.06e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.00 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT--------RFQMP------- 79
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVhvypgstpYGDEPdevgvrs 80
|
90
....*....|....*.
gi 4503377 80 ------DQGMTSADDF 89
Cdd:PRK09237 81 gvttvvDAGSAGADNF 96
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
381-436 |
1.62e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.53 E-value: 1.62e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 4503377 381 VAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEG 436
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
18-74 |
3.43e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.25 E-value: 3.43e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 4503377 18 LIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENliVPGGVKTIEAHSRMVIPGGIDVHT 74
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
16-113 |
7.32e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.44 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 16 RLLIKGGKIVN-----DDQsfyADIYMEDGLIKQIGEnliVPGGV---KTIEAHSRMVIPGGIDVHTRFQMPdqGMTSAD 87
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110
....*....|....*....|....*....|.
gi 4503377 88 DFFQGTKAALAGGTTMII-----DHVVPEPG 113
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPG 104
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
396-474 |
9.05e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 45.07 E-value: 9.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 396 PRKGRIAVGSDADLVIWDPDSVK---TISAKTHNSsleynifEGMEcrgsplVVISQGKIVLEDGTLHVTEGSGRYIpRK 472
Cdd:PRK09061 441 RRKGRLQAGADADIVVFDPETITdraTFEDPNRPS-------EGVR------HVLVNGVPVVSNGELVRDARPGRPV-RR 506
|
..
gi 4503377 473 PF 474
Cdd:PRK09061 507 PV 508
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
34-429 |
1.17e-04 |
|
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: 44.63 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 34 DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSADDFfqgtkaALAGGTTMIIDhvvpeP 112
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHvYQGGTRYGDRPDMI------GVKSGVTTVVD-----A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 113 GTSLLAAFDQWREWADSKSCCDYSLHVDISEWhkGIqeemealvkdhgvnsflvyMAFKDRFQLTDCqiyevlsvirDIG 192
Cdd:cd01307 70 GSAGADNIDGFRYTVIERSATRVYAFLNISRV--GL-------------------VAQDELPDPDNI----------DED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 193 AIAQVHAENGDIIAEEQQRIlDLGITGPEGhvlsrpeeveAEAVNRAITIANQTNCPLYitkVMSKSS----AEVIAQAR 268
Cdd:cd01307 119 AVVAAAREYPDVIVGLKARA-SKSVVGEWG----------IKPLELAKKIAKEADLPLM---VHIGSPppilDEVVPLLR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 269 KkgtvvyGEPITaslgtdgsHYWSknwAKAAAFVTSpplspdptTPDFLNSLLSCGDLQVT-----GSAHCTFNTAQKAV 343
Cdd:cd01307 185 R------GDVLT--------HCFN---GKPNGIVDE--------EGEVLPLVRRARERGVIfdvghGTASFSFRVARAAI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 344 GKDnftLIPEgTNGTE----ERMSV-IWDKAVVTGK-----MDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWD 413
Cdd:cd01307 240 AAG---LLPD-TISSDihgrNRTNGpVYALATTLSKllalgMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
410
....*....|....*.
gi 4503377 414 PDSVKTISAKTHNSSL 429
Cdd:cd01307 315 LKDGRVELVDSEGDTL 330
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
17-74 |
1.40e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 44.80 E-value: 1.40e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503377 17 LLIKGGKI------VNDDQsfyADIYMEDGlikQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 74
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHT 60
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
356-416 |
1.63e-04 |
|
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third step in the histidine degradation pathway, the hydrolysis of (S)-3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate to N-formimidoyl-L-glutamate. In bacteria, the enzyme is part of histidine utilization (hut) operon.
Pssm-ID: 238621 [Multi-domain] Cd Length: 371 Bit Score: 44.17 E-value: 1.63e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503377 356 NGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDS 416
Cdd:cd01296 291 SSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPS 351
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
16-103 |
1.96e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 44.01 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 16 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvkTIEAHSRMVIPGGIDVHT----RFQMP--------DQGM 83
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHTdnleKHLAPrpgvdwpaDAAL 80
|
90 100
....*....|....*....|
gi 4503377 84 TSADdffqgTKAALAGGTTM 103
Cdd:PRK15446 81 AAHD-----AQLAAAGITTV 95
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
17-473 |
2.39e-04 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 44.01 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVN--DDQSFYADIYMEDGLIKQIGeNLIVPGGVKTIEAHSRMVIPGGIDVHT--RFQMP-DQGMTSadDFFQ 91
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFIDIHThyDLQLLwDPRLEP--SLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 92 GTkaalaggTTMII----DHVVPEPGTSLLAAFDQWREWADSKSCCDYSlhvdiseWHkGIQEEMEALVKDH-GVN--SF 164
Cdd:COG3653 81 GV-------TTVVMgncgVSFAPVRPEDRDRLIDLMEGVEGIPEGLDWD-------WE-SFGEYLDALERRGlGVNvaSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 165 L------VY-MAFKDRfQLTDCQIYEVLSVIR---DIGA---------IAQVHAENGDIIAeeqqrildLG-ITGPEGHV 224
Cdd:COG3653 146 VghgtlrAYvMGLDDR-PPTPEELARMRALLReamEAGAlglstgliyVPGTYASTDELVA--------LAkVVAEYGGV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 225 L---SRPEEVEA-EAVNRAITIANQTNCPLYIT--KVMSK----SSAEVIA---QARKKGTVV----YGEPIT------- 280
Cdd:COG3653 217 YqshMRDEGDGLlEAVDELIRIGREAGVPVHIShlKAAGKpnwgKADEVLAlieAARAEGLDVtadvYPYPAGstglgal 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 281 -----ASLGTDG------------------SHYWSKNWAKAAAF-----VTSPPLSP---------------DP------ 311
Cdd:COG3653 297 lppwaAAGGLDErlarlrdpatrariraeiEEGLPDNLLGRGGWdniliSDSPPNEPlvgkslaeiaaergvDPadaald 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 312 ---------------TTPDFLNSLLS------CGDLQVTGSAHC-TFNTAQKAVGK---DN--FTLipegtngtEE---R 361
Cdd:COG3653 377 llleedgrvlivyfiMSEEDVRELLRhpwvmiGSDGGLGGKAHPrAYGTFPRVLGHyvrERgvLSL--------EEavrK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 362 MsviwdkavvTGKmdenqfvavtstnAAKVFNLYPRkGRIAVGSDADLVIWDPDSVKtiSAKTHNSSLEYNifEGMECrg 441
Cdd:COG3653 449 L---------TSL-------------PADRLGLKDR-GLLRPGYRADLVVFDPATLA--DRATFDLPAQRA--DGIRA-- 499
|
570 580 590
....*....|....*....|....*....|..
gi 4503377 442 splVVISqGKIVLEDGTlHVTEGSGRYIPRKP 473
Cdd:COG3653 500 ---VIVN-GVVVVEDGK-PTGARPGRVLRGGG 526
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
16-104 |
2.43e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 43.92 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 16 RLLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTrfqmpdQGMTSADDFFQgt 93
Cdd:PRK09061 20 DLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHA------HGQSVAAYRMQ-- 89
|
90
....*....|.
gi 4503377 94 kaALAGGTTMI 104
Cdd:PRK09061 90 --AFDGVTTAL 98
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
19-101 |
3.62e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 43.35 E-value: 3.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 19 IKGGKIVNDDQSFYADiyMEDGlikqIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSaddFFQGTKAALA 98
Cdd:PRK13985 87 IKDGKIAGIGKGGNKD--MQDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGVTTMIG 157
|
...
gi 4503377 99 GGT 101
Cdd:PRK13985 158 GGT 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
17-78 |
4.36e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 42.87 E-value: 4.36e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503377 17 LLIKGGKIVNDD--QSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQM 78
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
15-112 |
5.87e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 42.68 E-value: 5.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 15 DRLLIKGGKIVNDDQSF----YADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVH-------TRFQMPD--- 80
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHrhtwqsvLRGIGADwtl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 4503377 81 -----------QGMTSADDFFQGTKA----ALAGGTTMIID--HVVPEP 112
Cdd:PRK08204 81 qtyfreihgnlGPMFRPEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
383-423 |
9.52e-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: 41.61 E-value: 9.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 4503377 383 VTSTNAAKVFNLYPrKGRIAVGSDADLVIWDPD-SVKTISAK 423
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-415 |
1.02e-03 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 41.53 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 39 DGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT---------RFQMPDQGMTSAD--------DFFQ----GTKAAL 97
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHShlgldeeggVRETSDANEETDPvtphvraiDGINpddeAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 98 AGGTTMIidHVVPEP-----GTSLLAAFDQW-------REWADSKSCCDYslHVDISEWHKGI---------QEEMEALV 156
Cdd:cd01309 81 AGGVTTV--QVLPGSanligGQGVVIKTDGGtiedmfiKAPAGLKMALGE--NPKRVYGGKGKepatrmgvaALLRDAFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 157 K-DHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRdiGAI-AQVHAengdiiaeeqqrildlgitgpeghvlSRPEEVEAe 234
Cdd:cd01309 157 KaQEYGRKYDLGKNAKKDPPERDLKLEALLPVLK--GEIpVRIHA--------------------------HRADDILT- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 235 avnrAITIANQTNCPLYITKVM-SKSSAEVIAQARKKgtVVYGEPITASLGTDGSHYwskNWAKAAAFVTSPPLSPDPTT 313
Cdd:cd01309 208 ----AIRIAKEFGIKITIEHGAeGYKLADELAKHGIP--VIYGPTLTLPKKVEEVND---AIDTNAYLLKKGGVAFAISS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 314 pdflnsllscgDLQVTGSAHCTFNTAqkavgkdnftlipegtngteermsviwdKAVVTGKMDENQFVAVTStNAAKVFN 393
Cdd:cd01309 279 -----------DHPVLNIRNLNLEAA----------------------------KAVKYGLSYEEALKAITI-NPAKILG 318
|
410 420
....*....|....*....|..
gi 4503377 394 LYPRKGRIAVGSDADLVIWDPD 415
Cdd:cd01309 319 IEDRVGSLEPGKDADLVVWNGD 340
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
33-105 |
1.55e-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: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 33 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 100
Cdd:cd00375 83 ADIGIKDGRIVAIGkagnpdimdgvtPNMIVGPSTEVIAGEGKIVTAGGIDTHVHFICPQQ-----------IEEALASG 151
|
....*
gi 4503377 101 TTMII 105
Cdd:cd00375 152 ITTMI 156
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-74 |
2.02e-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: 2.02e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4503377 12 ITSDRLLIKGGKIVnddqsfyaDIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 74
Cdd:cd01293 2 LRNARLADGGTALV--------DIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHI 56
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
17-106 |
3.09e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.47 E-value: 3.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 17 LLIKGGKIVN--DDQSFYADIYMEDGLIKQIGEnlIVPGGVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDFfqgTK 94
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHI---ESSMVTPAEF---AR 78
|
90
....*....|...
gi 4503377 95 AALAGGTT-MIID 106
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
383-467 |
3.12e-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: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 383 VTSTNAAKVFNLyPRKGRIAVGSDADLVIW--DPDSVKTisakthnssLEYNIFEGMECRgsPLVVISQGKIVLEDGTLh 460
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYddDPDQVDP---------SDYEKVEKAFSR--AAYVLKDGEIVVKDGEV- 501
|
....*..
gi 4503377 461 VTEGSGR 467
Cdd:cd01304 502 VAEPWGR 508
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
33-104 |
3.27e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.46 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503377 33 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 100
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL-----------VDHALASG 155
|
....*
gi 4503377 101 -TTMI 104
Cdd:PRK13308 156 iTTML 160
|
|
| |
