|
Name |
Accession |
Description |
Interval |
E-value |
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
122-571 |
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: 739.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 201
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAPGGVEVIDATGKYVLPGGIDPHTHLELPFMGTVTADDFESGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKdHGVNSFLVYMAFKDRFQL 281
Cdd:cd01314 81 AAGGTTTIIDFAIPNKGQSLLEAVEKWRGKADGKSVIDYGFHMIITDWTDSVIEELPELVK-KGISSFKVFMAYKGLLMV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 282 TDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVM 361
Cdd:cd01314 160 DDEELLDVLKRAKELGALVMVHAENGDVIAELQKKLLAQGKTGPEYHALSRPPEVEAEATARAIRLAELAGAPLYIVHVS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 362 SKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSPDpTTPDFLNSLLSCGDLQVTGSAHCTF 441
Cdd:cd01314 240 SKEAADEIARARKKGLPVYGETCPQYLLLDDSDYW-KDWFEGAKYVCSPPLRPK-EDQEALWDGLSSGTLQTVGSDHCPF 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 442 NTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDS 521
Cdd:cd01314 318 NFAQKARGKDDFTKIPNGVPGVETRMPLLWSEGVAKGRITLEKFVELTSTNPAKIFGLYPRKGTIAVGSDADLVIWDPNA 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 308818195 522 VKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSG 571
Cdd:cd01314 398 EKTISADTHHHNVDYNIFEGMKVKGWPVVTISRGKVVVEDGELVGEKGSG 447
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
122-576 |
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: 680.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKAA 201
Cdd:TIGR02033 1 LLIKGGTVVNADDVFQADVLIEGGKIVAVGDNLIPPDAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFTGTKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDRFQL 281
Cdd:TIGR02033 81 AAGGTTTIIDFVVPEKGSSLTEALETWHEKAEGKSVIDYGFHMDITHWNDSVLEEHIPEVKEEGINSFKVFMAYKNLLMV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 282 TDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVM 361
Cdd:TIGR02033 161 DDEELFEILKRLKELGALLQVHAENGDIIAELQARMLAQGITGPEYHALSRPPELEAEAVARAITLAALADAPLYVVHVS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 362 SKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWsKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTF 441
Cdd:TIGR02033 241 TKDAADEIAQARKKGQPVFGETCPQYLVLDDTHYD-KPGFEGAKYVCSPPLR-EPEDQDALWSALSSGALQTVGSDHCTF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 442 NTAQK-AVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 520
Cdd:TIGR02033 319 NFAQKkAIGKDDFTKIPNGGPGVEERMSLLFDEGVAKGRITLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPN 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 308818195 521 SVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 576
Cdd:TIGR02033 399 RTTVISAETHHSNADYNPFEGFKVRGAPVSVLSRGRVVVEDGQLVGTAGAGRFVKR 454
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
121-580 |
0e+00 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 586.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 121 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlivpGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGTKA 200
Cdd:PRK08323 2 STLIKNGTVVTADDTYKADVLIEDGKIAAIGAN----LGDEVIDATGKYVMPGGIDPHTHMEMPFGGTVSSDDFETGTRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 201 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVkDHGVNSFLVYMAFKDRFQ 280
Cdd:PRK08323 78 AACGGTTTIIDFALQPKGQSLREALEAWHGKAAGKAVIDYGFHMIITDWNEVVLDEMPELV-EEGITSFKLFMAYKGALM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 281 LTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKV 360
Cdd:PRK08323 157 LDDDELLRALQRAAELGALPMVHAENGDAIAYLQAKLLAEGKTGPEYHALSRPPEVEGEATNRAIMLAELAGAPLYIVHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 361 MSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCT 440
Cdd:PRK08323 237 SCKEALEAIRRARARGQRVFGETCPQYLLLDESEYDGPDWFEGAKYVMSPPLRD-KEHQDALWRGLQDGDLQVVATDHCP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 441 FNTAQKA-VGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDP 519
Cdd:PRK08323 316 FCFEQKKqLGRGDFTKIPNGTPGVEDRMPLLFSEGVMTGRITLNRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDP 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308818195 520 DSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 580
Cdd:PRK08323 396 NATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVEDGEFRGKAGHGRFLKRKPFQ 456
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
119-580 |
0e+00 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 548.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 119 SDRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSADDFFQGT 198
Cdd:PLN02942 4 STKILIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDDVRVIDATGKFVMPGGIDPHTHLAMPFMGTETIDDFFSGQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 199 KAALAGGTTMIIDHVVPEPGtSLLAAFDQWREWADsKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSFLVYMAFKDR 278
Cdd:PLN02942 84 AAALAGGTTMHIDFVIPVNG-NLLAGYEAYEKKAE-KSCMDYGFHMAITKWDDTVSRDMETLVKEKGINSFKFFMAYKGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 279 FQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYIT 358
Cdd:PLN02942 162 LMVTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKRMIELGITGPEGHALSRPPLLEGEATARAIRLAKFVNTPLYVV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 359 KVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGSHYWSKNWAKAAAFVTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAH 438
Cdd:PLN02942 242 HVMSIDAMEEIARARKSGQRVIGEPVVSGLVLDDSKLWDPDFTIASKYVMSPPIRP-AGHGKALQAALSSGILQLVGTDH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 439 CTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWD 518
Cdd:PLN02942 321 CPFNSTQKAFGKDDFRKIPNGVNGIEERMHLVWDTMVESGQISPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILN 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 308818195 519 PDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPRKPFP 580
Cdd:PLN02942 401 PNSTFTISAKTHHSRIDTNVYEGRRGKGKVEVTISQGRVVWENGELKVVRGSGRYIEMPPFS 462
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
123-576 |
4.42e-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: 372.89 E-value: 4.42e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 123 LIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAAL 202
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEAAEVIDATGLLVLPGLIDLHVHLREP--GLEHKEDIETGTRAAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 203 AGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVkDHGVNSFLVYMAFKD-RFQL 281
Cdd:COG0044 79 AGGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHGALTKGLGENLAELGALA-EAGAVAFKVFMGSDDgNPVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 282 TDCQIYEVLSVIRDIGAIAQVHAENGDIIAEeqqRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVM 361
Cdd:COG0044 158 DDGLLRRALEYAAEFGALVAVHAEDPDLIRG---GVMNEGKTSPRLGLKGRPAEAEEEAVARDIALAEETGARLHIVHVS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 362 SKSSAEVIAQARKKGTVVYGE--P----ITAS-LGTDGSHYwsknwakaaafVTSPPLsPDPTTPDFL-NSLLScGDLQV 433
Cdd:COG0044 235 TAEAVELIREAKARGLPVTAEvcPhhltLTDEdLERYGTNF-----------KVNPPL-RTEEDREALwEGLAD-GTIDV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 434 TGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDAD 513
Cdd:COG0044 302 IATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELVHKGRLSLERLVELLSTNPARIFGL-PRKGRIAVGADAD 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 308818195 514 LVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 576
Cdd:COG0044 378 LVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEV-VGEPRGRFLRR 439
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
122-576 |
6.80e-120 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 366.33 E-value: 6.80e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPD-QGMTSADDFFQGTKA 200
Cdd:PRK13404 6 LVIRGGTVVTATDTFQADIGIRGGRIAALGEGL--GPGAREIDATGRLVLPGGVDSHCHIDQPSgDGIMMADDFYTGTVS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 201 ALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGI-QEEMEALVKDhGVNSFLVYMAFkDRF 279
Cdd:PRK13404 84 AAFGGTTTVIPFAAQHRGQSLREAVEDYHRRAAGKAVIDYAFHLIVADPTEEVlTEELPALIAQ-GYTSFKVFMTY-DDL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 280 QLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITK 359
Cdd:PRK13404 162 KLDDRQILDVLAVARRHGAMVMVHAENHDMIAWLTKRLLAAGLTAPKYHAISRPMLAEREATHRAIALAELVDVPILIVH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 360 VMSKSSAEVIAQARKKGTVVYGEP------ITAS-LGTDGSHywsknwakAAAFVTSPPLSpDPTTPDFLNSLLSCGDLQ 432
Cdd:PRK13404 242 VSGREAAEQIRRARGRGLKIFAETcpqylfLTAEdLDRPGME--------GAKYICSPPPR-DKANQEAIWNGLADGTFE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 433 VTGSAHCTFN---TAQKAVGKDN--FTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIA 507
Cdd:PRK13404 313 VFSSDHAPFRfddTDGKLAAGANpsFKAIANGIPGIETRLPLLFSEGVVKGRISLNRFVALTSTNPAKLYGLYPRKGAIA 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 308818195 508 VGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHVTEGSGRYIPR 576
Cdd:PRK13404 393 IGADADIAIWDPDREVTITNADLHHAADYTPYEGMRVTGWPVTVLSRGRVVVEDGELVAERGSGQFLAR 461
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
122-574 |
7.48e-64 |
|
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: 7.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 201
Cdd:cd01315 2 LVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEP--GRTEWEGFETGTKAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSccdyslHVDISEWH-------KGIQEEMEALVKdhGVNSFLV 271
Cdd:cd01315 80 AAGGITTIID--MPlnsIPPTTTVENLEAKLEAAQGKL------HVDVGFWGglvpgnlDQLRPLDEAGVV--GFKCFLC 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 272 YMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQT 351
Cdd:cd01315 150 PSGVDEFPAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAKGKRDYRDYLASRPVFTEVEAIQRILLLAKET 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 352 NCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWS-------KNwakAAAFVTSPPLSpDPTTPDFLNS 424
Cdd:cd01315 230 GCRLHIVHLSSAEAVPLIREARAEGVDVTVETCP--------HYLTftaedvpDG---GTEFKCAPPIR-DAANQEQLWE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 425 LLSCGDLQVTGSAH--CTfnTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPR 502
Cdd:cd01315 298 ALENGDIDMVVSDHspCT--PELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVNKRGLSLEDIARLMCENPAKLFGLSHQ 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308818195 503 KGRIAVGSDADLVIWDPDSVKTISAkthnSSLEY----NIFEGMECRGSPLVVISQGKIVLEDGTlHVTEGSGRYI 574
Cdd:cd01315 376 KGRIAVGYDADFVVWDPEEEFTVDA----EDLYYknkiSPYVGRTLKGRVHATILRGTVVYQDGE-VVGEPLGQLL 446
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
170-548 |
2.66e-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: 205.32 E-value: 2.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 170 VIPGGIDVHTRFQMPDQGMTSaDDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEw 249
Cdd:cd01302 3 VLPGFIDIHVHLRDPGGTTYK-EDFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHAGIGP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 250 hkGIQEEMEALVKDHGVNSFLVYMAFK--DRFQLTDCQIYEVLSVIRDIGAIAQVHAEngdiiaeeqqrildlgitgpeg 327
Cdd:cd01302 81 --GDVTDELKKLFDAGINSLKVFMNYYfgELFDVDDGTLMRTFLEIASRGGPVMVHAE---------------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 328 hvlsrpeeveaeavnRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITASLGTDGShYWSKNWAKaaaFV 407
Cdd:cd01302 137 ---------------RAAQLAEEAGANVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDES-MLRLNGAW---GK 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 408 TSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDnFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 487
Cdd:cd01302 198 VNPPLRS-KEDREALWEGVKNGKIDTIASDHAPHSKEEKESGKD-IWKAPPGFPGLETRLPILL-TEGVKRGLSLETLVE 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308818195 488 VTSTNAAKVFNLYPrKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSP 548
Cdd:cd01302 275 ILSENPARIFGLYP-KGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKP 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
122-577 |
3.76e-53 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 189.09 E-value: 3.76e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 201
Cdd:PRK02382 4 ALLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVHFREP--GYTHKETWYTGSRSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHvdisewhKGIQEEMEALVK--DHGVNSF-LVYMA---- 274
Cdd:PRK02382 82 AAGGVTTVVDQPNTDPPTVDGESFDEKAELAARKSIVDFGIN-------GGVTGNWDPLESlwERGVFALgEIFMAdstg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 275 ----FKDRFQltdcqiyEVLSVIRDIGAIAQVHAENGDIIaEEQQRILDlGITGPEGHVLSRPEEVEAEAVNRAITIANQ 350
Cdd:PRK02382 155 gmgiDEELFE-------EALAEAARLGVLATVHAEDEDLF-DELAKLLK-GDADADAWSAYRPAAAEAAAVERALEVASE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 351 TNCPLYITKVmskSSAEVIAQARKKGTVVYGEPITASLGTDgshywskNWAKAAAFV-TSPPLSPDPTTPDFLNSLLScG 429
Cdd:PRK02382 226 TGARIHIAHI---STPEGVDAARREGITCEVTPHHLFLSRR-------DWERLGTFGkMNPPLRSEKRREALWERLND-G 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 430 DLQVTGSAHCTFNTAQKAVG-KDnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAV 508
Cdd:PRK02382 295 TIDVVASDHAPHTREEKDADiWD----APSGVPGVETMLPLLL-AAVRKNRLPLERVRDVTAANPARIFGL-DGKGRIAE 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 509 GSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMEcrGS-PLVVISQGKIVLEDGTLHVTEGSGRYIPRK 577
Cdd:PRK02382 369 GYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGME--GVfPELTMVRGTVVWDGDDINAKRGRGEFLRGR 436
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
122-565 |
2.13e-51 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 184.52 E-value: 2.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 201
Cdd:PRK06189 5 LIIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR-EIIDADGLYVFPGMIDVHVHFNEP--GRTHWEGFATGSAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLhvdiseWHKGIQEEMEALVK--DHGVNSFLVYMAFK 276
Cdd:PRK06189 82 AAGGCTTYFD--MPlnsIPPTVTREALDAKAELARQKSAVDFAL------WGGLVPGNLEHLRElaEAGVIGFKAFMSNS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 277 --DRFQLTD-CQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNC 353
Cdd:PRK06189 154 gtDEFRSSDdLTLYEGMKEIAALGKILALHAESDALTRHLTTQARQQGKTDVRDYLESRPVVAELEAVQRALLYAQETGC 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 354 PLYITKVMSKSSAEVIAQARKKGtvvygepITASLGTdGSHY--WSKN--WAKAAAFVTSPPLSpDPTTPDFLNSLLSCG 429
Cdd:PRK06189 234 PLHFVHISSGKAVALIAEAKKRG-------VDVSVET-CPHYllFTEEdfERIGAVAKCAPPLR-SRSQKEELWRGLLAG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 430 DLQVTGSAH--CTFNTAQkavgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIA 507
Cdd:PRK06189 305 EIDMISSDHspCPPELKE----GDDFFLVWGGISGGQSTLLVMLTEGYIERGIPLETIARLLATNPAKRFGL-PQKGRLE 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 308818195 508 VGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLH 565
Cdd:PRK06189 380 VGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQDGEVF 437
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
122-575 |
2.90e-48 |
|
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: 2.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 201
Cdd:TIGR03178 2 LIIRGGRVILPNGEREADVGVKGGKIAAIGPD-ILGPAAKIIDAGGLVVFPGVVDTHVHINEP--GRTEWEGFETGTRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWH-KGIQEEMEALVkdHGVNSFLVYMAFKD 277
Cdd:TIGR03178 79 AAGGITTYID--MPlnsIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNlDDLRELDEAGV--VGFKAFLSPSGDDE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 278 RFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYI 357
Cdd:TIGR03178 155 FPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEEAPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVTGCRVHV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 358 TKVMSKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAK----AAAFVTSPPLSpDPTTPDFLNSLLSCGDLQV 433
Cdd:TIGR03178 235 VHLSSAEAVELITEAKQEGLDVTVETCP--------HYLTLTAEEvpdgGTLAKCAPPIR-DLANQEGLWEALLNGLIDC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 434 TGSAHCTFNTAQKAvgKDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDAD 513
Cdd:TIGR03178 306 VVSDHSPCTPDLKR--AGDFFKAWGGIAGLQSTLDVMFDEAVQKRGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDAD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 308818195 514 LVIWDPDSVKTISakthNSSLEY----NIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYIP 575
Cdd:TIGR03178 383 FVFVDPDESYTLT----PDDLYYrhkvSPYVGRTIGGRVRATYLRGQCIYDDEQF-IGAPKGQLLL 443
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
138-561 |
1.30e-46 |
|
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: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 138 ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIID--HVVP 215
Cdd:TIGR00857 6 VDILVEGGRIKKIGKLRIPPD-AEVIDAKGLLVLPGFIDLHVHLRDP--GEEYKEDIESGSKAAAHGGFTTVADmpNTKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 216 EPGTSllAAFDQWREWADSKSCCDYSLHVDISEWHKGiQEEMEAlvkdhgvnSFLVYMA-----FKDRFQ--LTDCQIYE 288
Cdd:TIGR00857 83 PIDTP--ETLEWKLQRLKKVSLVDVHLYGGVTQGNQG-KELTEA--------YELKEAGavgrmFTDDGSevQDILSMRR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 289 VLSVIRDIGAIAQVHAENGDIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEV 368
Cdd:TIGR00857 152 ALEYAAIAGVPIALHAEDPDLIYGGVMH---EGPSAAQLGLPARPPEAEEVAVARLLELAKHAGCPVHICHISTKESLEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 369 IAQARKkgtvvYGEPITAS------LGTDGSHYWSKNWAKaaafvTSPPLSPdPTTPDFLNSLLSCGDLQVTGSAHCTFN 442
Cdd:TIGR00857 229 IVKAKS-----QGIKITAEvtphhlLLSEEDVARLDGNGK-----VNPPLRE-KEDRLALIEGLKDGIIDIIATDHAPHT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 443 TAQKAVgkdNFTLIPEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSV 522
Cdd:TIGR00857 298 LEEKTK---EFAAAPPGIPGLETALPLLLQ-LLVKGLISLKDLIRMLSINPARIFGL-PDKGTLEEGNPADITVFDLKKE 372
|
410 420 430
....*....|....*....|....*....|....*....
gi 308818195 523 KTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLED 561
Cdd:TIGR00857 373 WTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
170-555 |
5.83e-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: 142.09 E-value: 5.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 170 VIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEw 249
Cdd:cd01318 4 ILPGVIDIHVHFREP--GLTYKEDFVSGSRAAAAGGVTTVMDMPNTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 250 hkgiQEEMEALVKdHGVNSFLVYMA--FKDRFQltdcqIYEVLSVI-RDIGAIAQVHAENGDIIAEEQQRILDLGItgpe 326
Cdd:cd01318 81 ----SEDLEELDK-APPAGYKIFMGdsTGDLLD-----DEETLERIfAEGSVLVTFHAEDEDRLRENRKELKGESA---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 327 gHVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTVvygePITAS--LGTDGSHYWSKNWAKaa 404
Cdd:cd01318 147 -HPRIRDAEAAAVATARALKLARRHGARLHICHVSTPEELKLIKKAKPGVTV----EVTPHhlFLDVEDYDRLGTLGK-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 405 afvTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVI---WDKAVVTGKmd 481
Cdd:cd01318 220 ---VNPPLR-SREDRKALLQALADGRIDVIASDHAPHTLEEKRKGYPA---APSGIPGVETALPLMltlVNKGILSLS-- 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308818195 482 enQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQG 555
Cdd:cd01318 291 --RVVRLTSHNPARIFGI-KNKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
159-549 |
2.40e-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: 131.98 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 159 GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTmiidHVVPEPGTsllaafdqwREWADSKSCC 238
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHLREP--GFEYKETLESGAKAAAAGGFT----TVVCMPNT---------NPVIDNPAVV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 239 DYSLH----VDISEWH------KGIQ----EEMEALvKDHGVNSFlvymaFKDRFQLTDCQI-YEVLSVIRDIGAIAQVH 303
Cdd:cd01317 66 ELLKNrakdVGIVRVLpigaltKGLKgeelTEIGEL-LEAGAVGF-----SDDGKPIQDAELlRRALEYAAMLDLPIIVH 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 304 AENGDIIAEEQqrILDLGITGPEGhVLSRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGtvvygEP 383
Cdd:cd01317 140 PEDPSLAGGGV--MNEGKVASRLG-LPGIPPEAETIMVARDLELAEATGARVHFQHLSTARSLELIRKAKAKG-----LP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 384 ITASLGtdgSHYWS------KNWAkaAAFVTSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIP 457
Cdd:cd01317 212 VTAEVT---PHHLLlddealESYD--TNAKVNPPLR-SEEDREALIEALKDGTIDAIASDHAPHTDEEKDLP---FAEAP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 458 EGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPrkGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYN 537
Cdd:cd01317 283 PGIIGLETALPLLWTLLVKGGLLTLPDLIRALSTNPAKILGLPP--GRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNT 360
|
410
....*....|..
gi 308818195 538 IFEGMECRGSPL 549
Cdd:cd01317 361 PFDGQKLKGRVL 372
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
169-558 |
4.04e-32 |
|
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: 127.23 E-value: 4.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 169 MVIPGGIDVHTRFQM------PDQGMTSADDFFQGTKAALAGGTTMIIDHVV--PEPGTSLLAAFDQW----REWAdsKS 236
Cdd:pfam01979 1 IVLPGLIDAHVHLEMgllrgiPVPPEFAYEALRLGITTMLKSGTTTVLDMGAttSTGIEALLEAAEELplglRFLG--PG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 237 CC---DYSLHVDISEWHKGIQEEMEALVKDHGVnsFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDiiAEE 313
Cdd:pfam01979 79 CSldtDGELEGRKALREKLKAGAEFIKGMADGV--VFVGLAPHGAPTFSDDELKAALEEAKKYGLPVAIHALETK--GEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 314 QQRILDLGITGPEGHVLSRPEEVeaeAVNRAITIANQTNCPLyitkvmSKSSAEVIAQARKKGTVVygepitasLGTDGS 393
Cdd:pfam01979 155 EDAIAAFGGGIEHGTHLEVAESG---GLLDIIKLILAHGVHL------SPTEANLLAEHLKGAGVA--------HCPFSN 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 394 HYWSKNWAKAAAfvtspplspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkaVGKDNFTLIPEGTNGTEERmsviwdk 473
Cdd:pfam01979 218 SKLRSGRIALRK-------------------ALEDGVKVGLGTDGA--------GSGNSLNMLEELRLALELQ------- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 474 AVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSvktisakthnssleYNIFEGMECRGSPLVVIS 553
Cdd:pfam01979 264 FDPEGGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDLDP--------------LAAFFGLKPDGNVKKVIV 329
|
....*
gi 308818195 554 QGKIV 558
Cdd:pfam01979 330 KGKIV 334
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
121-561 |
3.24e-31 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 126.85 E-value: 3.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 121 RLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFQMPDQgmTSADDFFQGTK 199
Cdd:PRK09357 2 MILIKNGRVIDPKGLDEvADVLIDDGKIAAIGENIEAEG-AEVIDATGLVVAPGLVDLHVHLREPGQ--EDKETIETGSR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 200 AALAGGTTMiidhVVPEPGT----SLLAAFDQWREWADSKSCCDysLHV--DISEWHKGIQE-EMEALvKDHGV------ 266
Cdd:PRK09357 79 AAAAGGFTT----VVAMPNTkpviDTPEVVEYVLDRAKEAGLVD--VLPvgAITKGLAGEELtEFGAL-KEAGVvafsdd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 267 -----NSFLVYMAFK--DRFQLTDCQIYEVLSVIRdiGAIAqvhaeNGDIIAEEqqrildLGITGpeghvlsRPEEVEAE 339
Cdd:PRK09357 152 gipvqDARLMRRALEyaKALDLLIAQHCEDPSLTE--GGVM-----NEGEVSAR------LGLPG-------IPAVAEEV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 340 AVNRAITIANQTNCPLYITKVMSKSSAEVIAQARKKGTvvygePITA------------SLGTDGSHYwsknwaKAAafv 407
Cdd:PRK09357 212 MIARDVLLAEATGARVHICHVSTAGSVELIRWAKALGI-----KVTAevtphhllltdeDLLTYDPNY------KVN--- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 408 tsPPLSPDPTTPDFLNSLLScGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVA 487
Cdd:PRK09357 278 --PPLRTEEDREALIEGLKD-GTIDAIATDHAPHAREEKECE---FEAAPFGITGLETALSLLYTTLVKTGLLDLEQLLE 351
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308818195 488 VTSTNAAKVFNLYPrkGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLED 561
Cdd:PRK09357 352 KMTINPARILGLPA--GPLAEGEPADLVIFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVYQD 423
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
122-536 |
7.23e-30 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 123.04 E-value: 7.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLivPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 201
Cdd:PRK08044 5 LIIKNGTVILENEARVVDIAVKGGKIAAIGQDL--GDAKEVMDASGLVVSPGMVDAHTHISEP--GRSHWEGYETGTRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDHvvpePGTSLLAAFDqwREWADSK-SCCDYSLHVDISEWHKGIQEEMEAL--VKDHGVNSFLVYMAF-KD 277
Cdd:PRK08044 81 AKGGITTMIEM----PLNQLPATVD--RASIELKfDAAKGKLTIDAAQLGGLVSYNLDRLheLDEVGVVGFKCFVATcGD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 278 R-----FQ-LTDCQIYEVLSVIRDIGAIAQVHAENG---DIIAEEQQRildLGITGPEGHVLSRPEEVEAEAVNRAITIA 348
Cdd:PRK08044 155 RgidndFRdVNDWQFYKGAQKLGELGQPVLVHCENAlicDELGEEAKR---EGRVTAHDYVASRPVFTEVEAIRRVLYLA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 349 NQTNCPLYITKVMSKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWSKNWAKAAAFVT----SPPLSPDPTTPDFLNS 424
Cdd:PRK08044 232 KVAGCRLHVCHISSPEGVEEVTRARQEGQDVTCESCP--------HYFVLDTDQFEEIGTlakcSPPIRDLENQKGMWEK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 425 LLScGDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLyPRKG 504
Cdd:PRK08044 304 LFN-GEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGL-QQKG 378
|
410 420 430
....*....|....*....|....*....|..
gi 308818195 505 RIAVGSDADLVIWDPDSvktiSAKTHNSSLEY 536
Cdd:PRK08044 379 RIAPGKDADFVFIQPNS----SYVLKNEDLEY 406
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
119-562 |
2.84e-28 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 118.24 E-value: 2.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 119 SDRLLIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQG 197
Cdd:PRK07575 2 MMSLLIRNARILLPSGELLlGDVLVEDGKIVAIAPEISATAVDTVIDAEGLTLLPGVIDPQVHFREP--GLEHKEDLFTA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 198 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISewhkgiQEEMEALVKDHGVNSFLVYMAFKD 277
Cdd:PRK07575 80 SRACAKGGVTSFLEMPNTKPLTTTQAALDDKLARAAEKCVVNYGFFIGAT------PDNLPELLTANPTCGIKIFMGSSH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 278 RFQLTDCQiyEVLSVI--RDIGAIAqVHAENGDIIAEEQQRILdlGITGPEGHVLSRPEEVEAEAVNRAITIANQTNCPL 355
Cdd:PRK07575 154 GPLLVDEE--AALERIfaEGTRLIA-VHAEDQARIRARRAEFA--GISDPADHSQIQDEEAALLATRLALKLSKKYQRRL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 356 YITKVMSKSSAEVIAQArkKGTVVYGEPITASLGTDGSHYwsknwAKAAAFVT-SPPLSpDPTTPDFLNSLLSCGDLQVT 434
Cdd:PRK07575 229 HILHLSTAIEAELLRQD--KPSWVTAEVTPQHLLLNTDAY-----ERIGTLAQmNPPLR-SPEDNEALWQALRDGVIDFI 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 435 GSAHCTFNTAQKAVGKDNftlIPEGTNGTEERMSVIWDKAVvTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADL 514
Cdd:PRK07575 301 ATDHAPHTLEEKAQPYPN---SPSGMPGVETSLPLMLTAAM-RGKCTVAQVVRWMSTAVARAYGI-PNKGRIAPGYDADL 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 308818195 515 VIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDG 562
Cdd:PRK07575 376 VLVDLNTYRPVRREELLTKCGWSPFEGWNLTGWPVTTIVGGQIVFDRG 423
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
122-572 |
1.93e-26 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 112.71 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAA 201
Cdd:PRK09060 7 LILKGGTVVNPDGEGRADIGIRDGRIAAIGDLSGASAG-EVIDCRGLHVLPGVIDSQVHFREP--GLEHKEDLETGSRAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 202 LAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISewHKGIQE--EMEALVKDHGVNsflVYM--AFKD 277
Cdd:PRK09060 84 VLGGVTAVFEMPNTNPLTTTAEALADKLARARHRMHCDFAFYVGGT--RDNADElaELERLPGCAGIK---VFMgsSTGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 278 RFQLTDCQIYEVLSVIRDIGAiaqVHAENGDIIAEEQqrilDLGITG-PEGHVLSRPEEVEAEAVNRAITIANQTNCPLY 356
Cdd:PRK09060 159 LLVEDDEGLRRILRNGRRRAA---FHSEDEYRLRERK----GLRVEGdPSSHPVWRDEEAALLATRRLVRLARETGRRIH 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 357 ITKVMSKSSAEVIAQARKKGTV--------VYGEPITASLGTdgshYWSKNwakaaafvtsPPLSpDPTTPDFLNSLLSC 428
Cdd:PRK09060 232 VLHVSTAEEIDFLADHKDVATVevtphhltLAAPECYERLGT----LAQMN----------PPIR-DARHRDGLWRGVRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 429 GDLQVTGSAHCTFNTAQKAvgkDNFTLIPEGTNGTEERMSVIWDKaVVTGKMDENQFVAVTSTNAAKVFNLyPRKGRIAV 508
Cdd:PRK09060 297 GVVDVLGSDHAPHTLEEKA---KPYPASPSGMTGVQTLVPIMLDH-VNAGRLSLERFVDLTSAGPARIFGI-AGKGRIAV 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308818195 509 GSDADLVIWDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGR 572
Cdd:PRK09060 372 GYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRVMWDGEL-VGPPTGE 434
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
127-576 |
2.35e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 111.87 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 127 GKIVNDDQSFYADIYMEDGLIKQIGENLivpGGVKTIEAHSrMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGT 206
Cdd:PRK01211 5 GNFYYKGKFDYLEIEVEDGKIKSIKKDA---GNIGKKELKG-AILPAATDIHVHFRTP--GETEKEDFSTGTLSAIFGGT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 207 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHvdisewhkgiqeEME----ALVKDHGVNSFLVYMAFKDRFQLT 282
Cdd:PRK01211 79 TFIMDMPNNNIPIKDYNAFSDKLGRVAPKAYVDFSLY------------SMEtgnnALILDERSIGLKVYMGGTTNTNGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 283 DCQIYEVlSVIRDIGAIAQVHAENGDIIAEEQQRILDLgitgpEGHVLSRPEEVEAEAVNRAITIANQtncplyiTKVMS 362
Cdd:PRK01211 147 DIEGGEI-KKINEANIPVFFHAELSECLRKHQFESKNL-----RDHDLARPIECEIKAVKYVKNLDLK-------TKIIA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 363 -KSSAEVIAQARKKGT----VVYGEpitASLGTDGShywsknwakaaafvTSPPLSPDPTTPDFLNSLLScGDLQVTGSA 437
Cdd:PRK01211 214 hVSSIDVIGRFLREVTphhlLLNDD---MPLGSYGK--------------VNPPLRDRWTQERLLEEYIS-GRFDILSSD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 438 HCTFNTAQKAvgkdNFTLIPEGTNGTEERMSVIWdKAVVTGKMDENQFVAVTSTNAAKVFNLypRKGRIAVGSDADLVIW 517
Cdd:PRK01211 276 HAPHTEEDKQ----EFEYAKSGIIGVETRVPLFL-ALVKKKILPLDVLYKTAIERPASLFGI--KKGKIEEGYDADFMAF 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 308818195 518 DPDSVKTISAKTHNSSLEYNIFEGMECRgSPLVVISQGKIVLEDGTLhVTEGSGRYIPR 576
Cdd:PRK01211 349 DFTNIKKINDKRLHSKCPVSPFNGFDAI-FPSHVIMRGEVVIDNYEL-ISERTGKFVPK 405
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
127-574 |
7.92e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 110.24 E-value: 7.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 127 GKIVNDDQSFYADIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTRFQmpDQGMTSADDFFQGTKAALAGGT 206
Cdd:PRK04250 4 GKFLLKGRIVEGGIGIENGRISKISLRDL--KGKEVIKVKGGIILPGLIDVHVHLR--DFEESYKETIESGTKAALHGGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 207 TMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDISEWHKGIQEEMEALVKDHGVNSflVYMAFKDRFQLTdcqi 286
Cdd:PRK04250 80 TLVFDMPNTKPPIMDEKTYEKRMRIAEKKSYADYALNFLIAGNCEKAEEIKADFYKIFMGAS--TGGIFSENFEVD---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 287 YEVLSvirdigAIAQVHAENGDIIAEEqqrildlgitgPEghvlsRPEEVEAEAVNRAITIANQTNCPLYITKVMSKSSA 366
Cdd:PRK04250 154 YACAP------GIVSVHAEDPELIREF-----------PE-----RPPEAEVVAIERALEAGKKLKKPLHICHISTKDGL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 367 EVIAQARKKGTVVYGEPitaslgtdgSH--YWSKNWAKAAAFVTSPPLSpDPTTPDFLNSLLSCGDlqVTGSAHCTFNTA 444
Cdd:PRK04250 212 KLILKSNLPWVSFEVTP---------HHlfLTRKDYERNPLLKVYPPLR-SEEDRKALWENFSKIP--IIASDHAPHTLE 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 445 QKAVGKdnftlipEGTNGTEERMSVIWDkAVVTGKMDENQFVAVTSTNAAKVFNlYPRKGrIAVGSDADLVIWDPDSVKT 524
Cdd:PRK04250 280 DKEAGA-------AGIPGLETEVPLLLD-AANKGMISLFDIVEKMHDNPARIFG-IKNYG-IEEGNYANFAVFDMKKEWT 349
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 308818195 525 ISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLhVTEGSGRYI 574
Cdd:PRK04250 350 IKAEELYTKAGWTPYEGFKLKGKVIMTILRGEVVMEDDEI-IGKPRGVRI 398
|
|
| PLN02795 |
PLN02795 |
allantoinase |
119-577 |
2.64e-25 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 110.25 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 119 SDRLLIKGGKIVNDdqsfyadIYMEDGLIKQIGENLIVPG---GVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFF 195
Cdd:PLN02795 50 SKRVVTPAGVIPGA-------VEVEGGRIVSVTKEEEAPKsqkKPHVLDYGNAVVMPGLIDVHVHLNEP--GRTEWEGFP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 196 QGTKAALAGGTTMIIDhvVP---EPGTSLLAAFDQWREWADSKsccdysLHVDISEWHKGIQE------EMEALVkDHGV 266
Cdd:PLN02795 121 TGTKAAAAGGITTLVD--MPlnsFPSTTSVETLELKIEAAKGK------LYVDVGFWGGLVPEnahnasVLEELL-DAGA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 267 ---NSFLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIAEEQQRILDLgiTGPEGHVLSRPEEVEAEAVNR 343
Cdd:PLN02795 192 lglKSFMCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADP--RSYSTYLKSRPPSWEQEAIRQ 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 344 AITIANQTN-------CPLYITKVM-SKSSAEVIAQARKKGTVVYGEPITaslgtdgsHYWsknwAKAAA--------FV 407
Cdd:PLN02795 270 LLEVAKDTRpggvaegAHVHIVHLSdAESSLELIKEAKAKGDSVTVETCP--------HYL----AFSAEeipdgdtrYK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 408 TSPPLSpDPTTPDFLNSLLSCGDLQVTGSAHCTFNTAQKAVGKDNFTLIPEGTNGTEERMSVIWDKAVVTGkMDENQFVA 487
Cdd:PLN02795 338 CAPPIR-DAANRELLWKALLDGDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAGRAYG-LTLEQLAR 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 488 VTSTNAAKVFNLyPRKGRIAVGSDADLVIWDP------DSVKTISAKTHNSSleynIFEGMECRGSPLVVISQGKIVLED 561
Cdd:PLN02795 416 WWSERPAKLAGL-DSKGAIAPGKDADIVVWDPeaefvlDESYPIYHKHKSLS----PYLGTKLSGKVIATFVRGNLVFLE 490
|
490
....*....|....*.
gi 308818195 562 GtLHVTEGSGRYIPRK 577
Cdd:PLN02795 491 G-KHAKQACGSPILAK 505
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
120-243 |
1.25e-16 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 83.00 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 120 DRLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGID--VHTRfqmpDQGMTSADDFFQG 197
Cdd:PRK09236 2 KRILIKNARIVNEGKIFEGDVLIENGRIAKIASSISAKSADTVIDAAGRYLLPGMIDdqVHFR----EPGLTHKGDIASE 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 308818195 198 TKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLH 243
Cdd:PRK09236 78 SRAAVAGGITSFMEMPNTNPPTTTLEALEAKYQIAAQRSLANYSFY 123
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
122-572 |
1.41e-12 |
|
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: 70.02 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVndDQS----FYADIYMEDGLIKQIGENLIVPGgVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDF--- 194
Cdd:cd01297 2 LVIRNGTVV--DGTgappFTADVGIRDGRIAAIGPILSTSA-REVIDAAGLVVAPGFIDVHTHY---DGQVFWDPDLrps 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 195 -FQGTKAALAG------------GTTMIIDHVVPEPGTSLLAAFDqWREWAD-------SKSCCDYSLHV---DISEWHK 251
Cdd:cd01297 76 sRQGVTTVVLGncgvspapanpdDLARLIMLMEGLVALGEGLPWG-WATFAEyldaleaRPPAVNVAALVghaALRRAVM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 252 GI---------QEEMEALVKDH------GVNSFLVYMafkDRFQLTDCQIYEVLSVIRDIGAIAQVHaengdiIAEEQQR 316
Cdd:cd01297 155 GLdareateeeLAKMRELLREAleagalGISTGLAYA---PRLYAGTAELVALARVAARYGGVYQTH------VRYEGDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 317 ILdlgitgpeghvlsrpeeveaEAVNRAITIANQTNCPLYIT--KVMSKSSAEVIAQ-------ARKKGTVVYGE--PIT 385
Cdd:cd01297 226 IL--------------------EALDELLRLGRETGRPVHIShlKSAGAPNWGKIDRllalieaARAEGLQVTADvyPYG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 386 ASLGTDgshywsknwakAAAFVTSPPlspdpttpdflnsLLSCGDLQVTGSAHCtfntaqkavgkdnftlipeGTNGTEE 465
Cdd:cd01297 286 AGSEDD-----------VRRIMAHPV-------------VMGGSDGGALGKPHP-------------------RSYGDFT 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 466 RMSVIWdkAVVTGKMDENQFVAVTSTNAAKVFNLYPRkGRIAVGSDADLVIWDPDSVK---TISAKTHNSsleynifEGM 542
Cdd:cd01297 323 RVLGHY--VRERKLLSLEEAVRKMTGLPARVFGLADR-GRIAPGYRADIVVFDPDTLAdraTFTRPNQPA-------EGI 392
|
490 500 510
....*....|....*....|....*....|
gi 308818195 543 EcrgspLVVISqGKIVLEDGtLHVTEGSGR 572
Cdd:cd01297 393 E-----AVLVN-GVPVVRDG-AFTGARPGR 415
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
118-527 |
2.60e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 65.75 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 118 QSDRLLIKGGKIVNDDQSFY---ADIYMEDGLIKQIGEN--LIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPD------- 185
Cdd:COG1228 6 QAGTLLITNATLVDGTGGGVienGTVLVEDGKIAAVGPAadLAVPAGAEVIDATGKTVLPGLIDAHTHLGLGGgravefe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 186 --QGMTSADDFFQGT----KAALAGGTTMIIDHvvpePGTSL----------LAAFDQWREWAdskscCDYSLHVDISEW 249
Cdd:COG1228 86 agGGITPTVDLVNPAdkrlRRALAAGVTTVRDL----PGGPLglrdaiiageSKLLPGPRVLA-----AGPALSLTGGAH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 250 HKGIQEEMEAL--VKDHGVNSFLVYMAFKDRfQLTDCQIYEVLSVIRDIGAIAQVHAENGDIIaeeqQRILDLGITGPEg 327
Cdd:COG1228 157 ARGPEEARAALreLLAEGADYIKVFAEGGAP-DFSLEELRAILEAAHALGLPVAAHAHQADDI----RLAVEAGVDSIE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 328 HVLSRpeeveaeavnraitianqtncplyitkvmsksSAEVIAQARKKGTVVYGePiTASLGTDGSHYWSKNWAKAAAFV 407
Cdd:COG1228 231 HGTYL--------------------------------DDEVADLLAEAGTVVLV-P-TLSLFLALLEGAAAPVAAKARKV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 408 tspplspDPTTPDFLNSLLSCGdlqvtgsahCTFntaqkAVGKD-NFTLIPEGTNGTEERMsviwdkaVVTGKMDENQ-F 485
Cdd:COG1228 277 -------REAALANARRLHDAG---------VPV-----ALGTDaGVGVPPGRSLHRELAL-------AVEAGLTPEEaL 328
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 308818195 486 VAVTStNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISA 527
Cdd:COG1228 329 RAATI-NAAKALGLDDDVGSLEPGKLADLVLLDGDPLEDIAY 369
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
122-564 |
2.16e-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: 59.91 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQS---FYADIYMEDGLIKQIGENLIVPG--GVKTIEAHSRMVIPGGIDVHTRFQM------------- 183
Cdd:cd01298 1 ILIRNGTIVTTDPRrvlEDGDVLVEDGRIVAVGPALPLPAypADEVIDAKGKVVMPGLVNTHTHLAMtllrgladdlplm 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 184 --------PDQGMTSADDFFQGTKAALA----GGTTMIIDHVVPEPGTSLLAA-------------FDQWREWADSKscc 238
Cdd:cd01298 81 ewlkdliwPLERLLTEEDVYLGALLALAemirSGTTTFADMYFFYPDAVAEAAeelgiravlgrgiMDLGTEDVEET--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 239 dyslhvdisewhKGIQEEMEALVKD-HGVNSFLVymafkdRFQLTDCQIYEV-LSVIRDIGAIA-------QVH-AENGD 308
Cdd:cd01298 158 ------------EEALAEAERLIREwHGAADGRI------RVALAPHAPYTCsDELLREVAELAreygvplHIHlAETED 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 309 IIAEEQQR--------ILDLGITGPE---GH-VLSRPEEVEaeavnraitIANQTN-----CPlyiTKVMsKSSAEV--I 369
Cdd:cd01298 220 EVEESLEKygkrpveyLEELGLLGPDvvlAHcVWLTDEEIE---------LLAETGtgvahNP---ASNM-KLASGIapV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 370 AQARKKGtvvygepITASLGTDGShywsknwakaaafvtspplspdpttpdflnsllSCGD-LQVTGSAHCTFNTaQKAV 448
Cdd:cd01298 287 PEMLEAG-------VNVGLGTDGA---------------------------------ASNNnLDMFEEMRLAALL-QKLA 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 449 GKDNFTLIPEgtngteermsviwdkavvtgkmdenQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWDPDSVKTISAK 528
Cdd:cd01298 326 HGDPTALPAE-------------------------EALEMATIGGAKALGL-DEIGSLEVGKKADLILIDLDGPHLLPVH 379
|
490 500 510
....*....|....*....|....*....|....*...
gi 308818195 529 THNSSLEYNifegmeCRGSP--LVVISqGKIVLEDGTL 564
Cdd:cd01298 380 DPISHLVYS------ANGGDvdTVIVN-GRVVMEDGEL 410
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
171-571 |
2.60e-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: 59.39 E-value: 2.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 171 IPGGIDVHTrfQMPDQGMTSADDFFQGTKAALAGGTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDYSLHVDIS--E 248
Cdd:cd01316 5 LPGLIDVHV--HLREPGATHKEDFASGTKAALAGGFTMVRAMPNTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATstN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 249 WHKGIQeemealVKDHGVNS-FLVYMAFKDRFQLTDCQIYEVLSVIRDIGAIAqVHAENGDIIAeeqqrILDLgitgpeg 327
Cdd:cd01316 83 AATVGE------LASEAVGLkFYLNETFSTLILDKITAWASHFNAWPSTKPIV-THAKSQTLAA-----VLLL------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 328 hvlsrpeeveAEAVNRAItianqtncplYITKVMSKSSAEVIAQARKKGTVVYGEPITASLgtdgshYWSKNWAKAAAFV 407
Cdd:cd01316 144 ----------ASLHNRSI----------HICHVSSKEEINLIRLAKARGLKVTCEVSPHHL------FLSQDDLPRGQYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 408 TSPPLsPDPTTPDFLNSLLSCGDLQVTGSAHCTFntAQKAVGKdnftlIPEGTNGTEERMSVIWdKAVVTGKMDENQFVA 487
Cdd:cd01316 198 VRPFL-PTREDQEALWENLDYIDCFATDHAPHTL--AEKTGNK-----PPPGFPGVETSLPLLL-TAVHEGRLTIEDIVD 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 488 VTSTNAAKVFNLYPrkgriavgsDADLVI-WDPDSVKTISAKTHNSSLEYNIFEGMECRGSPLVVISQGKIVLEDGTLHV 566
Cdd:cd01316 269 RLHTNPKRIFNLPP---------QSDTYVeVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVA 339
|
....*
gi 308818195 567 TEGSG 571
Cdd:cd01316 340 PPGFG 344
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
122-520 |
8.08e-08 |
|
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: 54.89 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTrfqmpdQG------MTSADDFF 195
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEADEIIDLKGQYLVPGFIDIHI------HGgggadfMDGTAEAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 196 QGTKAALAG-GTTMIIDHVVPEPGTSLLAAFDQWREWADSKSCCDY-SLHVD---ISEWHKGIQEEmEALVKdhgvnsfL 270
Cdd:cd00854 75 KTIAEALAKhGTTSFLPTTVTAPPEEIAKALAAIAEAIAEGQGAEIlGIHLEgpfISPEKKGAHPP-EYLRA-------P 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 271 VYMAFKDRFQLTDcqiyevlSVIRDIgAIAQVHAENGDIIaeeqQRILDLGITGPEGHVLSRPEEVEAeAVNRAITIA-- 348
Cdd:cd00854 147 DPEELKKWLEAAG-------GLIKLV-TLAPELDGALELI----RYLVERGIIVSIGHSDATYEQAVA-AFEAGATHVth 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 349 --NQtncplyitkvMSK-SSAE--VIaqarkkGTVVYGEPITASLGTDGSHywsknwakaaafvtsppLSPDpttpdfln 423
Cdd:cd00854 214 lfNA----------MSPlHHREpgVV------GAALSDDDVYAELIADGIH-----------------VHPA-------- 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 424 sllscgdlqvtgsahcTFNTAQKAVGKDNFTLI---------PEGT---NGTEERM--------------SVI-WDKAVV 476
Cdd:cd00854 253 ----------------AVRLAYRAKGADKIVLVtdamaaaglPDGEyelGGQTVTVkdgvarladgtlagSTLtMDQAVR 316
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 308818195 477 T----GKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 520
Cdd:cd00854 317 NmvkwGGCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLDDD 364
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
486-520 |
3.06e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 53.18 E-value: 3.06e-07
10 20 30
....*....|....*....|....*....|....*
gi 308818195 486 VAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPD 520
Cdd:COG1820 328 VRMASLNPARALGLDDRKGSIAPGKDADLVVLDDD 362
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
138-529 |
4.69e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 52.68 E-value: 4.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 138 ADIYMEDGLIKQIGENLI-VPGGVKTIEAHSRMVIPGGIDVHTRFQMPdqGMTSADDFFQGTKAALAGGTTM--IIDHVV 214
Cdd:PRK07369 22 ADVLIEDGKIQAIEPHIDpIPPDTQIIDASGLILGPGLVDLYSHSGEP--GFEERETLASLAAAAAAGGFTRvaILPDTF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 215 P---EPGTslLAAFDQ---------WREWAD-SKSCCDYSLhvdiSEWhkgiQEEMEAlvkdhGVNSFlvymafkdrfql 281
Cdd:PRK07369 100 PpldNPAT--LARLQQqaqqippvqLHFWGAlTLGGQGKQL----TEL----AELAAA-----GVVGF------------ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 282 TDCQIYEVLSVIRDIGAIAQVH-------------AENGdiIAEEQQRILDLGITGpeghvlsRPEEVEAEAVNRAITIA 348
Cdd:PRK07369 153 TDGQPLENLALLRRLLEYLKPLgkpvalwpcdrslAGNG--VMREGLLALRLGLPG-------DPASAETTALAALLELV 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 349 NQTNCPLYITKVMSKSSAEVIAQARKKGTvvygePITAS-------LGT-DGSHYwSKNWAKAaafvtsPPLsPDPTTPD 420
Cdd:PRK07369 224 AAIGTPVHLMRISTARSVELIAQAKARGL-----PITASttwmhllLDTeALASY-DPNLRLD------PPL-GNPSDRQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 421 FLNSLLSCGDLQVTGSAHCTFNTAQKAVGkdnFTLIPEGTNGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLY 500
Cdd:PRK07369 291 ALIEGVRTGVIDAIAIDHAPYTYEEKTVA---FAEAPPGAIGLELALPLLWQNLVETGELSALQLWQALSTNPARCLGQE 367
|
410 420
....*....|....*....|....*....
gi 308818195 501 PRkgRIAVGSDADLVIWDPDSVKTISAKT 529
Cdd:PRK07369 368 PP--SLAPGQPAELILFDPQKTWTVSAQT 394
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
121-561 |
5.84e-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: 5.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 121 RLLIKGGKIV--NDDQSFYAD--IYMEDGLIKQIGENLIVP---GGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSAD 192
Cdd:COG0402 1 DLLIRGAWVLtmDPAGGVLEDgaVLVEDGRIAAVGPGAELParyPAAEVIDAGGKLVLPGLVNTHTHlPQTLLRGLADDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 193 DFFQ--------------------GTKAA----LAGGTTMIIDHvvpepGTSLLAAFDQWREWAD--------SKSCCDY 240
Cdd:COG0402 81 PLLDwleeyiwplearldpedvyaGALLAlaemLRSGTTTVADF-----YYVHPESADALAEAAAeagiravlGRGLMDR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 241 SLHVDISEWHKGIQEEMEALVKD-HGVNSFLVymafkdRFQLTDCQIYEV-LSVIRDIGAIA-------QVH-----AEN 306
Cdd:COG0402 156 GFPDGLREDADEGLADSERLIERwHGAADGRI------RVALAPHAPYTVsPELLRAAAALArelglplHTHlaetrDEV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 307 GDIIAEEQQRILD----LGITGPE---GH-VLSRPEEVEAEAVNRAiTIAnqtNCPLyitkvmskSSAEV------IAQA 372
Cdd:COG0402 230 EWVLELYGKRPVEyldeLGLLGPRtllAHcVHLTDEEIALLAETGA-SVA---HCPT--------SNLKLgsgiapVPRL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 373 RKKGtvvygepITASLGTDGshywsknwakaaafvtspplSPDPTTPDFLNSLLSCGDLqvtgsahctfntaQKAVGKDn 452
Cdd:COG0402 298 LAAG-------VRVGLGTDG--------------------AASNNSLDMFEEMRLAALL-------------QRLRGGD- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 453 ftlipegtngtEERMSviWDKAvvtgkmdenqFVAVTsTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSvktisakTHNS 532
Cdd:COG0402 337 -----------PTALS--AREA----------LEMAT-LGGARALGLDDEIGSLEPGKRADLVVLDLDA-------PHLA 385
|
490 500 510
....*....|....*....|....*....|.
gi 308818195 533 SLEYNIFEGMECRGSPLV--VISQGKIVLED 561
Cdd:COG0402 386 PLHDPLSALVYAADGRDVrtVWVAGRVVVRD 416
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
122-194 |
1.09e-06 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 51.39 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT--------RFQMP------- 184
Cdd:PRK09237 1 LLLRGGRVIDPANGIDGviDIAIEDGKIAAVAGDIDGSQAKKVIDLSGLYVSPGWIDLHVhvypgstpYGDEPdevgvrs 80
|
90
....*....|....*.
gi 308818195 185 ------DQGMTSADDF 194
Cdd:PRK09237 81 gvttvvDAGSAGADNF 96
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
486-541 |
1.81e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.91 E-value: 1.81e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 308818195 486 VAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDSVKTISAKTHNSSLEYNIFEG 541
Cdd:pfam07969 405 LALYTSGPAKALGLEDRKGTLGVGKDADLVVLDDDPLTVDPPAIADIRVRLTVVDG 460
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
123-179 |
3.56e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 46.63 E-value: 3.56e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 308818195 123 LIKGGKIVNDDQSFY-ADIYMEDGLIKQIGENliVPGGVKTIEAHSRMVIPGGIDVHT 179
Cdd:COG1820 1 AITNARIFTGDGVLEdGALLIEDGRIAAIGPG--AEPDAEVIDLGGGYLAPGFIDLHV 56
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
103-209 |
4.37e-05 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 46.61 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 103 IRRASGKEALQNINDQSDRLLIKGGKIVNDDQSFYA--DIYMEDGLIKQIGENLIvpGGVKTIEAHSRMVIPGGIDVHTr 180
Cdd:PRK09061 2 AKVAVLSLLLMPASMAPYDLVIRNGRVVDPETGLDAvrDVGIKGGKIAAVGTAAI--EGDRTIDATGLVVAPGFIDLHA- 78
|
90 100
....*....|....*....|....*....
gi 308818195 181 fqmpdQGMTSADDFFQgtkaALAGGTTMI 209
Cdd:PRK09061 79 -----HGQSVAAYRMQ----AFDGVTTAL 98
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
139-534 |
9.26e-05 |
|
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: 45.01 E-value: 9.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 139 DIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHTR-FQMPDQGMTSADDFfqgtkaALAGGTTMIIDhvvpeP 217
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHvYQGGTRYGDRPDMI------GVKSGVTTVVD-----A 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 218 GTSLLAAFDQWREWADSKSCCDYSLHVDISEWhkGIqeemealvkdhgvnsflvyMAFKDRFQLTDCqiyevlsvirDIG 297
Cdd:cd01307 70 GSAGADNIDGFRYTVIERSATRVYAFLNISRV--GL-------------------VAQDELPDPDNI----------DED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 298 AIAQVHAENGDIIAEEQQRIlDLGITGPEGhvlsrpeeveAEAVNRAITIANQTNCPLYitkVMSKSS----AEVIAQAR 373
Cdd:cd01307 119 AVVAAAREYPDVIVGLKARA-SKSVVGEWG----------IKPLELAKKIAKEADLPLM---VHIGSPppilDEVVPLLR 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 374 KkgtvvyGEPITaslgtdgsHYWSknwAKAAAFVTSpplspdptTPDFLNSLLSCGDLQVT-----GSAHCTFNTAQKAV 448
Cdd:cd01307 185 R------GDVLT--------HCFN---GKPNGIVDE--------EGEVLPLVRRARERGVIfdvghGTASFSFRVARAAI 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 449 GKDnftLIPEgTNGTE----ERMSV-IWDKAVVTGK-----MDENQFVAVTSTNAAKVFNLyPRKGRIAVGSDADLVIWD 518
Cdd:cd01307 240 AAG---LLPD-TISSDihgrNRTNGpVYALATTLSKllalgMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFD 314
|
410
....*....|....*.
gi 308818195 519 PDSVKTISAKTHNSSL 534
Cdd:cd01307 315 LKDGRVELVDSEGDTL 330
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
121-218 |
1.11e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 45.05 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 121 RLLIKGGKIVN-----DDQsfyADIYMEDGLIKQIGEnliVPGGV---KTIEAHSRMVIPGGIDVHTRFQMPdqGMTSAD 192
Cdd:PRK07627 2 KIHIKGGRLIDpaagtDRQ---ADLYVAAGKIAAIGQ---APAGFnadKTIDASGLIVCPGLVDLSARLREP--GYEYKA 73
|
90 100 110
....*....|....*....|....*....|.
gi 308818195 193 DFFQGTKAALAGGTTMII-----DHVVPEPG 218
Cdd:PRK07627 74 TLESEMAAAVAGGVTSLVcppdtDPVLDEPG 104
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
122-179 |
1.41e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 44.80 E-value: 1.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308818195 122 LLIKGGKI------VNDDQsfyADIYMEDGlikQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 179
Cdd:COG1229 3 LIIKNGRVydpangIDGEV---MDIAIKDG---KIVEEPSDPKDAKVIDASGKVVMAGGVDIHT 60
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
461-521 |
1.90e-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: 1.90e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 308818195 461 NGTEERMSVIWDKAVVTGKMDENQFVAVTSTNAAKVFNLYPRKGRIAVGSDADLVIWDPDS 521
Cdd:cd01296 291 SSPTSSMPLVMHLACRLMRMTPEEALTAATINAAAALGLGETVGSLEVGKQADLVILDAPS 351
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
121-208 |
2.66e-04 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 43.63 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 121 RLLIKGGKIVNDDQSFYADIYMEDGLIKQIGENLIVPGGvkTIEAHSRMVIPGGIDVHT----RFQMP--------DQGM 188
Cdd:PRK15446 3 EMILSNARLVLPDEVVDGSLLIEDGRIAAIDPGASALPG--AIDAEGDYLLPGLVDLHTdnleKHLAPrpgvdwpaDAAL 80
|
90 100
....*....|....*....|
gi 308818195 189 TSADdffqgTKAALAGGTTM 208
Cdd:PRK15446 81 AAHD-----AQLAAAGITTV 95
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
122-578 |
3.39e-04 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 43.62 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVN--DDQSFYADIYMEDGLIKQIGeNLIVPGGVKTIEAHSRMVIPGGIDVHT--RFQMP-DQGMTSadDFFQ 196
Cdd:COG3653 4 LLIRGGTVVDgtGAPPFRADVAIKGGRIVAVG-DLAAAEAARVIDATGLVVAPGFIDIHThyDLQLLwDPRLEP--SLRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 197 GTkaalaggTTMII----DHVVPEPGTSLLAAFDQWREWADSKSCCDYSlhvdiseWHkGIQEEMEALVKDH-GVN--SF 269
Cdd:COG3653 81 GV-------TTVVMgncgVSFAPVRPEDRDRLIDLMEGVEGIPEGLDWD-------WE-SFGEYLDALERRGlGVNvaSL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 270 L------VY-MAFKDRfQLTDCQIYEVLSVIR---DIGA---------IAQVHAENGDIIAeeqqrildLG-ITGPEGHV 329
Cdd:COG3653 146 VghgtlrAYvMGLDDR-PPTPEELARMRALLReamEAGAlglstgliyVPGTYASTDELVA--------LAkVVAEYGGV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 330 L---SRPEEVEA-EAVNRAITIANQTNCPLYIT--KVMSK----SSAEVIA---QARKKGTVV----YGEPIT------- 385
Cdd:COG3653 217 YqshMRDEGDGLlEAVDELIRIGREAGVPVHIShlKAAGKpnwgKADEVLAlieAARAEGLDVtadvYPYPAGstglgal 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 386 -----ASLGTDG------------------SHYWSKNWAKAAAF-----VTSPPLSP---------------DP------ 416
Cdd:COG3653 297 lppwaAAGGLDErlarlrdpatrariraeiEEGLPDNLLGRGGWdniliSDSPPNEPlvgkslaeiaaergvDPadaald 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 417 ---------------TTPDFLNSLLS------CGDLQVTGSAHC-TFNTAQKAVGK---DN--FTLipegtngtEE---R 466
Cdd:COG3653 377 llleedgrvlivyfiMSEEDVRELLRhpwvmiGSDGGLGGKAHPrAYGTFPRVLGHyvrERgvLSL--------EEavrK 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 467 MsviwdkavvTGKmdenqfvavtstnAAKVFNLYPRkGRIAVGSDADLVIWDPDSVKtiSAKTHNSSLEYNifEGMECrg 546
Cdd:COG3653 449 L---------TSL-------------PADRLGLKDR-GLLRPGYRADLVVFDPATLA--DRATFDLPAQRA--DGIRA-- 499
|
570 580 590
....*....|....*....|....*....|..
gi 308818195 547 splVVISqGKIVLEDGTlHVTEGSGRYIPRKP 578
Cdd:COG3653 500 ---VIVN-GVVVVEDGK-PTGARPGRVLRGGG 526
|
|
| ureB |
PRK13985 |
urease subunit alpha; |
124-206 |
4.09e-04 |
|
urease subunit alpha;
Pssm-ID: 184438 [Multi-domain] Cd Length: 568 Bit Score: 43.35 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 124 IKGGKIVNDDQSFYADiyMEDGlikqIGENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQGMTSaddFFQGTKAALA 203
Cdd:PRK13985 87 IKDGKIAGIGKGGNKD--MQDG----VKNNLSVGPATEALAGEGLIVTAGGIDTHIHFISPQQIPTA---FASGVTTMIG 157
|
...
gi 308818195 204 GGT 206
Cdd:PRK13985 158 GGT 160
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
122-183 |
4.31e-04 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 43.25 E-value: 4.31e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 308818195 122 LLIKGGKIVNDD--QSFYADIYMEDGLIKQIGENLIVPGGvKTIEAHSRMVIPGGIDVHTRFQM 183
Cdd:PRK08393 3 ILIKNGYVIYGEnlKVIRADVLIEGNKIVEVKRNINKPAD-TVIDASGSVVSPGFINAHTHSPM 65
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
91-210 |
5.67e-04 |
|
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: 43.09 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 91 GEPSVESGRKVeIRRASGKEALQNINDQSDrLLIKGGKIVNDDQSFYADIYMEDGLIKQIG------------ENLIVPG 158
Cdd:cd00375 38 GDEVKFGGGKV-LRDGMGQSSGYTREDVLD-LVITNALIIDYTGIYKADIGIKDGRIVAIGkagnpdimdgvtPNMIVGP 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 308818195 159 GVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGGTTMII 210
Cdd:cd00375 116 STEVIAGEGKIVTAGGIDTHVHFICPQQ-----------IEEALASGITTMI 156
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
120-217 |
7.34e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 42.68 E-value: 7.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 120 DRLLIKGGKIVNDDQSF----YADIYMEDGLIKQIGENlIVPGGVKTIEAHSRMVIPGGIDVH-------TRFQMPD--- 185
Cdd:PRK08204 2 KRTLIRGGTVLTMDPAIgdlpRGDILIEGDRIAAVAPS-IEAPDAEVVDARGMIVMPGLVDTHrhtwqsvLRGIGADwtl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 308818195 186 -----------QGMTSADDFFQGTKA----ALAGGTTMIID--HVVPEP 217
Cdd:PRK08204 81 qtyfreihgnlGPMFRPEDVYIANLLgaleALDAGVTTLLDwsHINNSP 129
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
144-520 |
8.53e-04 |
|
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238634 [Multi-domain] Cd Length: 359 Bit Score: 42.30 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 144 DGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT---------RFQMPDQGMTSAD--------DFFQ----GTKAAL 202
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVIDAKGKHVTPGLIDAHShlgldeeggVRETSDANEETDPvtphvraiDGINpddeAFKRAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 203 AGGTTMIidHVVPEP-----GTSLLAAFDQW-------REWADSKSCCDYslHVDISEWHKGI---------QEEMEALV 261
Cdd:cd01309 81 AGGVTTV--QVLPGSanligGQGVVIKTDGGtiedmfiKAPAGLKMALGE--NPKRVYGGKGKepatrmgvaALLRDAFI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 262 K-DHGVNSFLVYMAFKDRFQLTDCQIYEVLSVIRdiGAI-AQVHAengdiiaeeqqrildlgitgpeghvlSRPEEVEAe 339
Cdd:cd01309 157 KaQEYGRKYDLGKNAKKDPPERDLKLEALLPVLK--GEIpVRIHA--------------------------HRADDILT- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 340 avnrAITIANQTNCPLYITKVM-SKSSAEVIAQARKKgtVVYGEPITASLGTDGSHYwskNWAKAAAFVTSPPLSPDPTT 418
Cdd:cd01309 208 ----AIRIAKEFGIKITIEHGAeGYKLADELAKHGIP--VIYGPTLTLPKKVEEVND---AIDTNAYLLKKGGVAFAISS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 419 pdflnsllscgDLQVTGSAHCTFNTAqkavgkdnftlipegtngteermsviwdKAVVTGKMDENQFVAVTStNAAKVFN 498
Cdd:cd01309 279 -----------DHPVLNIRNLNLEAA----------------------------KAVKYGLSYEEALKAITI-NPAKILG 318
|
410 420
....*....|....*....|..
gi 308818195 499 LYPRKGRIAVGSDADLVIWDPD 520
Cdd:cd01309 319 IEDRVGSLEPGKDADLVVWNGD 340
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
488-528 |
1.05e-03 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 41.99 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 308818195 488 VTSTNAAKVFNLYPrKGRIAVGSDADLVIWDPD-SVKTISAK 528
Cdd:cd01308 330 VITSNVARILKLRK-KGEIQPGFDADLVILDKDlDINSVIAK 370
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
138-179 |
2.60e-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: 2.60e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 308818195 138 ADIYMEDGLIKQIGENLIVPGGVKTIEAHSRMVIPGGIDVHT 179
Cdd:cd01293 15 VDIAIEDGRIAAIGPALAVPPDAEEVDAKGRLVLPAFVDPHI 56
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
122-211 |
3.22e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 40.47 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 122 LLIKGGKIVN--DDQSFYADIYMEDGLIKQIGEnlIVPGGVKTIEAHSRMVIPGGIDVHTRFqmpDQGMTSADDFfqgTK 199
Cdd:COG1001 7 LVIKNGRLVNvfTGEILEGDIAIAGGRIAGVGD--YIGEATEVIDAAGRYLVPGFIDGHVHI---ESSMVTPAEF---AR 78
|
90
....*....|...
gi 308818195 200 AALAGGTT-MIID 211
Cdd:COG1001 79 AVLPHGTTtVIAD 91
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
488-572 |
3.51e-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: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 488 VTSTNAAKVFNLyPRKGRIAVGSDADLVIW--DPDSVKTisakthnssLEYNIFEGMECRgsPLVVISQGKIVLEDGTLh 565
Cdd:cd01304 435 MTRAGPAKLLGL-SDKGHLGVGADADIAIYddDPDQVDP---------SDYEKVEKAFSR--AAYVLKDGEIVVKDGEV- 501
|
....*..
gi 308818195 566 VTEGSGR 572
Cdd:cd01304 502 VAEPWGR 508
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
138-209 |
4.29e-03 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 40.08 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 308818195 138 ADIYMEDGLIKQIG------------ENLIVPGGVKTIEAHSRMVIPGGIDVHTRFQMPDQgmtsaddffqgTKAALAGG 205
Cdd:PRK13308 87 GDIGIRDGRIVGIGkagnpdimdgvdPRLVVGPGTDVRPAEGLIATPGAIDVHVHFDSAQL-----------VDHALASG 155
|
....*
gi 308818195 206 -TTMI 209
Cdd:PRK13308 156 iTTML 160
|
|
| |
