|
Name |
Accession |
Description |
Interval |
E-value |
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
9-456 |
0e+00 |
|
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: 684.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 9 DHVIINGANKPAtivYSTESGTILDVLeGSVVMEKTEITKYEIHTLENVSPCTILPGLVDSHVHLNEPGRTSWEGFETGT 88
Cdd:cd01315 1 DLVIKNGRVVTP---DGVREADIAVKG-GKIAAIGPDIANTEAEEVIDAGGLVVMPGLIDTHVHINEPGRTEWEGFETGT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 89 QAAISGGVTTVVDMPLNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHNLPDLIPLVKAGVRGFKGFLLDSGVEEF 168
Cdd:cd01315 77 KAAAAGGITTIIDMPLNSIPPTTTVENLEAKLEAAQGKLHVDVGFWGGLVPGNLDQLRPLDEAGVVGFKCFLCPSGVDEF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 169 PPIGKEYIEEALKVLAEEDTMMMFHAELPKAHEDQQQPEQS--HREYSSFLSSRPDSFEIDAINLILECLRARNgpvPPV 246
Cdd:cd01315 157 PAVDDEQLEEAMKELAKTGSVLAVHAENPEITEALQEQAKAkgKRDYRDYLASRPVFTEVEAIQRILLLAKETG---CRL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 247 HIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSP 326
Cdd:cd01315 234 HIVHLSSAEAVPLIREARAEGVDVTVETCPHYLTFTAEDVPDGGTEFKCAPPIRDAANQEQLWEALENGDIDMVVSDHSP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 327 CTPELKNLQKGDFFDSWGGIASVGLGLPLMFTQGC-----SLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFDTA 401
Cdd:cd01315 314 CTPELKLLGKGDFFKAWGGISGLQLGLPVMLTEAVnkrglSLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPE 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 398364693 402 SKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTNaNGVSKTPLGQTLL 456
Cdd:cd01315 394 EEFTVDAEDLYYKNKISPYVGRTLKGRVHATILRGTVVYQD-GEVVGEPLGQLLL 447
|
|
| allantoinase |
TIGR03178 |
allantoinase; This enzyme carries out the first step in the degradation of allantoin, a ... |
5-456 |
8.75e-169 |
|
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: 481.88 E-value: 8.75e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 5 AITSDHVIINGANKPATIVysTESGTIldvlegsvvmekTEITKYEIHT---LENVSPCTILPGLVDSHVHLNEPGRTSW 81
Cdd:TIGR03178 3 IIRGGRVILPNGEREADVG--VKGGKI------------AAIGPDILGPaakIIDAGGLVVFPGVVDTHVHINEPGRTEW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 82 EGFETGTQAAISGGVTTVVDMPLNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHNLPDLIPLVKAGVRGFKGFLL 161
Cdd:TIGR03178 69 EGFETGTRAAAAGGITTYIDMPLNSIPATTTRASLEAKFEAAKGKLAVDVGFWGGLVPYNLDDLRELDEAGVVGFKAFLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 162 DSGVEEFPPIGKEYIEEALKVLAEEDTMMMFHAELPKAHEDQQQ--PEQSHREYSSFLSSRPDSFEIDAINLILECLRAR 239
Cdd:TIGR03178 149 PSGDDEFPHVDDWQLYKGMRELARLGQLLLVHAENPAITSALGEeaPPQGGVGADAYLASRPVFAEVEAIRRTLALAKVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 240 NGpvpPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGS 319
Cdd:TIGR03178 229 GC---RVHVVHLSSAEAVELITEAKQEGLDVTVETCPHYLTLTAEEVPDGGTLAKCAPPIRDLANQEGLWEALLNGLIDC 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 320 VVSDHSPCTPELKnlQKGDFFDSWGGIASVGLGLPLMFTQ-----GCSLVDIVTWCCKNTSHQVGLsHQKGTIAPGYDAD 394
Cdd:TIGR03178 306 VVSDHSPCTPDLK--RAGDFFKAWGGIAGLQSTLDVMFDEavqkrGLPLEDIARLMATNPAKRFGL-AQKGRIAPGKDAD 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364693 395 LVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTNANgVSKTPLGQTLL 456
Cdd:TIGR03178 383 FVFVDPDESYTLTPDDLYYRHKVSPYVGRTIGGRVRATYLRGQCIYDDEQ-FIGAPKGQLLL 443
|
|
| PLN02795 |
PLN02795 |
allantoinase |
6-456 |
1.84e-151 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 440.37 E-value: 1.84e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 6 ITSDHVIINGANKPATIvySTESGTILDVLEGS---VVMEKTEITKYeihtlenvSPCTILPGLVDSHVHLNEPGRTSWE 82
Cdd:PLN02795 48 LYSKRVVTPAGVIPGAV--EVEGGRIVSVTKEEeapKSQKKPHVLDY--------GNAVVMPGLIDVHVHLNEPGRTEWE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 83 GFETGTQAAISGGVTTVVDMPLNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVP---HNLPDLIPLVKAGVRGFKGF 159
Cdd:PLN02795 118 GFPTGTKAAAAGGITTLVDMPLNSFPSTTSVETLELKIEAAKGKLYVDVGFWGGLVPenaHNASVLEELLDAGALGLKSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 160 LLDSGVEEFPPIGKEYIEEALKVLAEEDTMMMFHAELPKAHEDQQQPEQSHREYSSFLSSRPDSFEIDAINLILECLR-A 238
Cdd:PLN02795 198 MCPSGINDFPMTTATHIKAALPVLAKYGRPLLVHAEVVSPVESDSRLDADPRSYSTYLKSRPPSWEQEAIRQLLEVAKdT 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 239 RNGPVPP---VHIVHLASMK-AIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALRE 314
Cdd:PLN02795 278 RPGGVAEgahVHIVHLSDAEsSLELIKEAKAKGDSVTVETCPHYLAFSAEEIPDGDTRYKCAPPIRDAANRELLWKALLD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 315 GVIGSVVSDHSPCTPELKNLQKGDFFDSWGGIASVGLGLPLMFTQ----GCSLVDIVTWCCKNTSHQVGLsHQKGTIAPG 390
Cdd:PLN02795 358 GDIDMLSSDHSPSPPDLKLLEEGNFLRAWGGISSLQFVLPATWTAgrayGLTLEQLARWWSERPAKLAGL-DSKGAIAPG 436
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364693 391 YDADLVVFDTASKHKI-SNSSVYFKNK-LTAYNGMTVKGTVLKTILRGQVVYTNANgVSKTPLGQTLL 456
Cdd:PLN02795 437 KDADIVVWDPEAEFVLdESYPIYHKHKsLSPYLGTKLSGKVIATFVRGNLVFLEGK-HAKQACGSPIL 503
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
60-455 |
3.11e-132 |
|
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: 388.68 E-value: 3.11e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVP 139
Cdd:COG0044 46 LLVLPGLIDLHVHLREPGLEHKEDIETGTRAAAAGGVTTVVDMP-NTNPVTDTPEALEFKLARAEEKALVDVGPHGALTK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 140 ---HNLPDLIPLVKAGVRGFKGFLLDSGVEefPPIGKEYIEEALKVLAEEDTMMMFHAELPKAHeDQQQPEQSHREYSSF 216
Cdd:COG0044 125 glgENLAELGALAEAGAVAFKVFMGSDDGN--PVLDDGLLRRALEYAAEFGALVAVHAEDPDLI-RGGVMNEGKTSPRLG 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 217 LSSRPDSFEIDAINLILECLRARNGPVppvHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCC 296
Cdd:COG0044 202 LKGRPAEAEEEAVARDIALAEETGARL---HIVHVSTAEAVELIREAKARGLPVTAEVCPHHLTLTDEDLERYGTNFKVN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 297 PPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNlqkGDFFDSWGGIASVGLGLPLMFTQG-----CSLVDIVTWCC 371
Cdd:COG0044 279 PPLRTEEDREALWEGLADGTIDVIATDHAPHTLEEKE---LPFAEAPNGIPGLETALPLLLTELvhkgrLSLERLVELLS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 372 KNTSHQVGLsHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTNANGVSKtPL 451
Cdd:COG0044 356 TNPARIFGL-PRKGRIAVGADADLVLFDPDAEWTVTAEDLHSKSKNTPFEGRELTGRVVATIVRGRVVYEDGEVVGE-PR 433
|
....
gi 398364693 452 GQTL 455
Cdd:COG0044 434 GRFL 437
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
62-458 |
4.63e-121 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 360.56 E-value: 4.63e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPLNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHN 141
Cdd:PRK06189 52 VFPGMIDVHVHFNEPGRTHWEGFATGSAALAAGGCTTYFDMPLNSIPPTVTREALDAKAELARQKSAVDFALWGGLVPGN 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 142 LPDLIPLVKAGVRGFKGFLLDSGVEEFPPIGKEYIEEALKVLAEEDTMMMFHAELPK--AHEDQQQPEQSHREYSSFLSS 219
Cdd:PRK06189 132 LEHLRELAEAGVIGFKAFMSNSGTDEFRSSDDLTLYEGMKEIAALGKILALHAESDAltRHLTTQARQQGKTDVRDYLES 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 220 RPDSFEIDAINLILECLRARNGpvpPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCCPPI 299
Cdd:PRK06189 212 RPVVAELEAVQRALLYAQETGC---PLHFVHISSGKAVALIAEAKKRGVDVSVETCPHYLLFTEEDFERIGAVAKCAPPL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 300 RSESNRQGLWDALREGVIGSVVSDHSPCTPELKnlQKGDFFDSWGGIASVGLGLPLMFTQGC-----SLVDIVTWCCKNT 374
Cdd:PRK06189 289 RSRSQKEELWRGLLAGEIDMISSDHSPCPPELK--EGDDFFLVWGGISGGQSTLLVMLTEGYiergiPLETIARLLATNP 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 375 SHQVGLShQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTNaNGVSKTPLGQT 454
Cdd:PRK06189 367 AKRFGLP-QKGRLEVGADADFVLVDLDETYTLTKEDLFYRHKQSPYEGRTFPGRVVATYLRGQCVYQD-GEVFPPPRGQL 444
|
....
gi 398364693 455 LLDS 458
Cdd:PRK06189 445 LRPS 448
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
64-456 |
1.31e-92 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 287.52 E-value: 1.31e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 64 PGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPLNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHNLP 143
Cdd:PRK08044 53 PGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNLD 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 144 DLIPLVKAGVRGFKGFLL---DSGVE-EFPPIGKEYIEEALKVLAEEDTMMMFHAELPK-----AHEDQQQPEQSHREYs 214
Cdd:PRK08044 133 RLHELDEVGVVGFKCFVAtcgDRGIDnDFRDVNDWQFYKGAQKLGELGQPVLVHCENALicdelGEEAKREGRVTAHDY- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 215 sfLSSRPDSFEIDAINLILECLRARNGpvpPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFK 294
Cdd:PRK08044 212 --VASRPVFTEVEAIRRVLYLAKVAGC---RLHVCHISSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAK 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 295 CCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNlqkGDFFDSWGGIASVGLGLPLMFTQ-----GCSLVDIVTW 369
Cdd:PRK08044 287 CSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKA---GNIMEAWGGIAGLQNCMDVMFDEavqkrGMSLPMFGKL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 370 CCKNTSHQVGLSHqKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTNANGVSKT 449
Cdd:PRK08044 364 MATNAADIFGLQQ-KGRIAPGKDADFVFIQPNSSYVLKNEDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVA 442
|
....*..
gi 398364693 450 PLGQTLL 456
Cdd:PRK08044 443 PKGQFIL 449
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
60-436 |
1.88e-72 |
|
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: 232.61 E-value: 1.88e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVP 139
Cdd:cd01318 2 LLILPGVIDIHVHFREPGLTYKEDFVSGSRAAAAGGVTTVMDMP-NTKPPTTTAEALYEKLRLAAAKSVVDYGLYFGVTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 140 HnlPDLIPLVKAGVRGFKGFLLDSgvEEFPPIGKEYIEEAlkvLAEEDTMMMFHAELP---KAHEDQQQPEQSHREYssf 216
Cdd:cd01318 81 S--EDLEELDKAPPAGYKIFMGDS--TGDLLDDEETLERI---FAEGSVLVTFHAEDEdrlRENRKELKGESAHPRI--- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 217 lssRPDSFEIDAINLILEcLRARNGpvPPVHIVHLASMKAIPLIRKARASglpVTTETCFHYLCIAAEQIPDGATYFKCC 296
Cdd:cd01318 151 ---RDAEAAAVATARALK-LARRHG--ARLHICHVSTPEELKLIKKAKPG---VTVEVTPHHLFLDVEDYDRLGTLGKVN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 297 PPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKnlqKGDFFDSWGGIASVGLGLPLMFTQ----GCSLVDIVTWCCK 372
Cdd:cd01318 222 PPLRSREDRKALLQALADGRIDVIASDHAPHTLEEK---RKGYPAAPSGIPGVETALPLMLTLvnkgILSLSRVVRLTSH 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364693 373 NTSHQVGLShQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRG 436
Cdd:cd01318 299 NPARIFGIK-NKGRIAEGYDADLTVVDLKEERTIRAEEFHSKAGWTPFEGFEVTGFPVMTIVRG 361
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
60-432 |
1.11e-65 |
|
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: 214.18 E-value: 1.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEPGRTSWEG-FETGTQAAISGGVTTVVDMPLNAIPPTTNVENF-RIKLeaAEGQMWCDVGFWGGL 137
Cdd:cd01302 1 LLVLPGFIDIHVHLRDPGGTTYKEdFESGSRAAAAGGVTTVIDMPNTGPPPIDLPAIElKIKL--AEESSYVDFSFHAGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 138 VP-HNLPDLIPLVKAGVRGFKGFLLDSGVEEFPpIGKEYIEEALKVLAEEDTMMMFHAELpkahedqqqpeqshreyssf 216
Cdd:cd01302 79 GPgDVTDELKKLFDAGINSLKVFMNYYFGELFD-VDDGTLMRTFLEIASRGGPVMVHAER-------------------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 217 lssrpdsfeidAINLILECLRarngpvpPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCC 296
Cdd:cd01302 138 -----------AAQLAEEAGA-------NVHIAHVSSGEALELIKFAKNKGVKVTCEVCPHHLFLDESMLRLNGAWGKVN 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 297 PPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLQKgDFFDSWGGIASVGLGLPLMFTQ----GCSLVDIVTWCCK 372
Cdd:cd01302 200 PPLRSKEDREALWEGVKNGKIDTIASDHAPHSKEEKESGK-DIWKAPPGFPGLETRLPILLTEgvkrGLSLETLVEILSE 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 373 NTSHQVGLsHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKT 432
Cdd:cd01302 279 NPARIFGL-YPKGTIAVGYDADLVIVDPKKEWKVTAEEIESKADWTPFEGMEVTGKPVST 337
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
11-442 |
1.56e-65 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 217.73 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 11 VIINGankpaTIVysTESGTIL-DVL-EGSVVmekTEITKYEIHTLENVSPCTILPGLVDSHVHLNEP--GRTSWEGFET 86
Cdd:PRK08323 4 LIKNG-----TVV--TADDTYKaDVLiEDGKI---AAIGANLGDEVIDATGKYVMPGGIDPHTHMEMPfgGTVSSDDFET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 87 GTQAAISGGVTTVVDMplnAIPPTTnvENFRIKLEA----AEGQMWCDVGF------WGGLVPHNLPDlipLVKAGVRGF 156
Cdd:PRK08323 74 GTRAAACGGTTTIIDF---ALQPKG--QSLREALEAwhgkAAGKAVIDYGFhmiitdWNEVVLDEMPE---LVEEGITSF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 157 KGFL-------LDSGVeefppigkeyIEEALKVLAEEDTMMMFHAElpkaHED-----QQQPEQSHR---EYSSFlsSRP 221
Cdd:PRK08323 146 KLFMaykgalmLDDDE----------LLRALQRAAELGALPMVHAE----NGDaiaylQAKLLAEGKtgpEYHAL--SRP 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 222 DSFEIDAINlileclRARN-----GpvPPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAE--QIPD---GAT 291
Cdd:PRK08323 210 PEVEGEATN------RAIMlaelaG--APLYIVHVSCKEALEAIRRARARGQRVFGETCPQYLLLDESeyDGPDwfeGAK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 292 YFkCCPPIRSESNRQGLWDALREGVIGSVVSDHSP-CTPELKNLQKGDFfdSW--GGIASVGLGLPLMFTQGC-----SL 363
Cdd:PRK08323 282 YV-MSPPLRDKEHQDALWRGLQDGDLQVVATDHCPfCFEQKKQLGRGDF--TKipNGTPGVEDRMPLLFSEGVmtgriTL 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364693 364 VDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTN 442
Cdd:PRK08323 359 NRFVELTSTNPAKIFGLYPRKGTIAVGADADIVIWDPNATKTISASTLHSNVDYNPYEGFEVTGWPVTTLSRGEVVVED 437
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
62-440 |
1.50e-62 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 209.51 E-value: 1.50e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGlVPHN 141
Cdd:PRK02382 52 LLPGGIDVHVHFREPGYTHKETWYTGSRSAAAGGVTTVVDQP-NTDPPTVDGESFDEKAELAARKSIVDFGINGG-VTGN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 142 LPDLIPLVKAGVRGFkG--FLLDS----GVEEfppigkEYIEEALKVLAEEDTMMMFHAELPKAHEDQQQPEQSHREYSS 215
Cdd:PRK02382 130 WDPLESLWERGVFAL-GeiFMADStggmGIDE------ELFEEALAEAARLGVLATVHAEDEDLFDELAKLLKGDADADA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 216 FLSSRPDSFEIDAINLILEC---LRARngpvppVHIVHLASMKAIPLIRKARasglpVTTETCFHYLCIAAEQIPDGATY 292
Cdd:PRK02382 203 WSAYRPAAAEAAAVERALEVaseTGAR------IHIAHISTPEGVDAARREG-----ITCEVTPHHLFLSRRDWERLGTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 293 FKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLqkgDFFDSWGGIASVGLGLPLMFTQGCS-------LVD 365
Cdd:PRK02382 272 GKMNPPLRSEKRREALWERLNDGTIDVVASDHAPHTREEKDA---DIWDAPSGVPGVETMLPLLLAAVRKnrlplerVRD 348
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398364693 366 IVTWcckNTSHQVGLShQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLkTILRGQVVY 440
Cdd:PRK02382 349 VTAA---NPARIFGLD-GKGRIAEGYDADLVLVDPDAAREIRGDDLHSKAGWTPFEGMEGVFPEL-TMVRGTVVW 418
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
60-444 |
6.25e-62 |
|
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: 207.84 E-value: 6.25e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEP--GRTSWEGFETGTQAAISGGVTTVVDM--PLNAIPPTTNVENFRiklEAAEGQMWCDVGFWG 135
Cdd:cd01314 47 KYVLPGGIDPHTHLELPfmGTVTADDFESGTRAAAAGGTTTIIDFaiPNKGQSLLEAVEKWR---GKADGKSVIDYGFHM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 136 GLV--PHNLPDLIP-LVKAGVRGFKGFLL--DSGVeefppIGKEYIEEALKVLAEEDTMMMFHAE--------------- 195
Cdd:cd01314 124 IITdwTDSVIEELPeLVKKGISSFKVFMAykGLLM-----VDDEELLDVLKRAKELGALVMVHAEngdviaelqkkllaq 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 196 ---LPKAHEdqqqpeqshreyssflSSRPDSFEIDAINLIleCLRARNGPVPpVHIVHLASMKAIPLIRKARASGLPVTT 272
Cdd:cd01314 199 gktGPEYHA----------------LSRPPEVEAEATARA--IRLAELAGAP-LYIVHVSSKEAADEIARARKKGLPVYG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 273 ETCFHYLCIAAEQI----PDGATYFkCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLQKGDFFDSWGGIAS 348
Cdd:cd01314 260 ETCPQYLLLDDSDYwkdwFEGAKYV-CSPPLRPKEDQEALWDGLSSGTLQTVGSDHCPFNFAQKARGKDDFTKIPNGVPG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 349 VGLGLPLMFTQG--------CSLVDIVtwcCKNTSHQVGLSHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAY 420
Cdd:cd01314 339 VETRMPLLWSEGvakgritlEKFVELT---STNPAKIFGLYPRKGTIAVGSDADLVIWDPNAEKTISADTHHHNVDYNIF 415
|
410 420
....*....|....*....|....
gi 398364693 421 NGMTVKGTVLKTILRGQVVYTNAN 444
Cdd:cd01314 416 EGMKVKGWPVVTISRGKVVVEDGE 439
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
62-442 |
5.46e-58 |
|
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: 196.51 E-value: 5.46e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGlVPHN 141
Cdd:TIGR00857 37 VLPGFIDLHVHLRDPGEEYKEDIESGSKAAAHGGFTTVADMP-NTKPPIDTPETLEWKLQRLKKVSLVDVHLYGG-VTQG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 142 LPDLIpLVKAGVRGFKGFLLDSGVEEFPPIGK-EYIEEALKVLAEEDTMMMFHAELP------KAHEDQQQPeqshreyS 214
Cdd:TIGR00857 115 NQGKE-LTEAYELKEAGAVGRMFTDDGSEVQDiLSMRRALEYAAIAGVPIALHAEDPdliyggVMHEGPSAA-------Q 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 215 SFLSSRPDSFEIDAINLILECLRARNGpvpPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFK 294
Cdd:TIGR00857 187 LGLPARPPEAEEVAVARLLELAKHAGC---PVHICHISTKESLELIVKAKSQGIKITAEVTPHHLLLSEEDVARLDGNGK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 295 CCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLQkgdFFDSWGGIASVGLGLPLMFTQGC----SLVDIVTWC 370
Cdd:TIGR00857 264 VNPPLREKEDRLALIEGLKDGIIDIIATDHAPHTLEEKTKE---FAAAPPGIPGLETALPLLLQLLVkgliSLKDLIRML 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364693 371 CKNTSHQVGLShQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTN 442
Cdd:TIGR00857 341 SINPARIFGLP-DKGTLEEGNPADITVFDLKKEWTINAETFYSKAKNTPFEGMSLKGKPIATILRGKVVYED 411
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
60-432 |
3.02e-57 |
|
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: 193.22 E-value: 3.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVP 139
Cdd:cd01317 10 KILAPGLVDLHVHLREPGFEYKETLESGAKAAAAGGFTTVVCMP-NTNPVIDNPAVVELLKNRAKDVGIVRVLPIGALTK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 140 ----HNLPDLIPLVKAGVRGFKgfllDSGveeFPPIGKEYIEEALKVLAEEDTMMMFHAELPK------AHEDqqqpeqs 209
Cdd:cd01317 89 glkgEELTEIGELLEAGAVGFS----DDG---KPIQDAELLRRALEYAAMLDLPIIVHPEDPSlagggvMNEG------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 210 hrEYSSF--LSSRPDSFEIDAINLILECLRARNGPVppvHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIP 287
Cdd:cd01317 155 --KVASRlgLPGIPPEAETIMVARDLELAEATGARV---HFQHLSTARSLELIRKAKAKGLPVTAEVTPHHLLLDDEALE 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 288 DGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLqkgDFFDSWGGIASVGLGLPLMFT-----QGCS 362
Cdd:cd01317 230 SYDTNAKVNPPLRSEEDREALIEALKDGTIDAIASDHAPHTDEEKDL---PFAEAPPGIIGLETALPLLWTllvkgGLLT 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 363 LVDIVTWCCKNTSHQVGLShqKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKT 432
Cdd:cd01317 307 LPDLIRALSTNPAKILGLP--PGRLEVGAPADLVLFDPDAEWIVDEETFRSKSKNTPFDGQKLKGRVLAT 374
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
61-439 |
9.14e-55 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 188.98 E-value: 9.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 61 TILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPH 140
Cdd:PRK09060 53 HVLPGVIDSQVHFREPGLEHKEDLETGSRAAVLGGVTAVFEMP-NTNPLTTTAEALADKLARARHRMHCDFAFYVGGTRD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 141 NLPDLIPLVKA-GVRGFKGF-------LL---DSGVEefppigkeyieealKVLAEEDTMMMFHAElpkaHEDQQQPEQS 209
Cdd:PRK09060 132 NADELAELERLpGCAGIKVFmgsstgdLLvedDEGLR--------------RILRNGRRRAAFHSE----DEYRLRERKG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 210 HRE---YSSFLSSRPDSFEIDAINLILEcLRARNGpvPPVHIVHLASMKAIPLIRKARASglpVTTETCFHYLCIAAEQI 286
Cdd:PRK09060 194 LRVegdPSSHPVWRDEEAALLATRRLVR-LARETG--RRIHVLHVSTAEEIDFLADHKDV---ATVEVTPHHLTLAAPEC 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 287 PDG-ATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKnlQKgDFFDSWGGIASVGLGLPLMFT---QG-C 361
Cdd:PRK09060 268 YERlGTLAQMNPPIRDARHRDGLWRGVRQGVVDVLGSDHAPHTLEEK--AK-PYPASPSGMTGVQTLVPIMLDhvnAGrL 344
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364693 362 SLVDIVTWCCKNTSHQVGLShQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVV 439
Cdd:PRK09060 345 SLERFVDLTSAGPARIFGIA-GKGRIAVGYDADFTIVDLKRRETITNEWIASRCGWTPYDGKEVTGWPVGTIVRGQRV 421
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
29-440 |
9.87e-55 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 188.10 E-value: 9.87e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 29 GTILDVL-EGSVVmekTEITKYEIHTLENVSPCT---ILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPl 104
Cdd:PRK09357 17 DEVADVLiDDGKI---AAIGENIEAEGAEVIDATglvVAPGLVDLHVHLREPGQEDKETIETGSRAAAAGGFTTVVAMP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 105 NAIPPTTNVENFRIKLEAAEGQMWCDVgFW-----GGLVPHNLPDLIPLVKAGVRGFK--GF-LLDSGVeefppigkeyI 176
Cdd:PRK09357 93 NTKPVIDTPEVVEYVLDRAKEAGLVDV-LPvgaitKGLAGEELTEFGALKEAGVVAFSddGIpVQDARL----------M 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 177 EEALKVLAEEDTMMMFHAELPK------AHEDqqqpeqshrEYSSFL--SSRPDSFEIDAInlileclrARN-------G 241
Cdd:PRK09357 162 RRALEYAKALDLLIAQHCEDPSlteggvMNEG---------EVSARLglPGIPAVAEEVMI--------ARDvllaeatG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 242 PvpPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVV 321
Cdd:PRK09357 225 A--RVHICHVSTAGSVELIRWAKALGIKVTAEVTPHHLLLTDEDLLTYDPNYKVNPPLRTEEDREALIEGLKDGTIDAIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 322 SDHSPCTPELKNlqkGDFFDSWGGIASVGLGLPLMFTQ-----GCSLVDIVTWCCKNTSHQVGLSHqkGTIAPGYDADLV 396
Cdd:PRK09357 303 TDHAPHAREEKE---CEFEAAPFGITGLETALSLLYTTlvktgLLDLEQLLEKMTINPARILGLPA--GPLAEGEPADLV 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 398364693 397 VFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVY 440
Cdd:PRK09357 378 IFDPEAEWTVDGEDFASKGKNTPFIGMKLKGKVVYTIVDGKIVY 421
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
60-444 |
6.22e-52 |
|
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: 181.43 E-value: 6.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEP--GRTSWEGFETGTQAAISGGVTTVVDM--PLNAIPPTTNVENFRiklEAAEGQMWCDVGFWG 135
Cdd:TIGR02033 47 KYVLPGGIDVHTHLEMPfgGTTTADDFFTGTKAAAAGGTTTIIDFvvPEKGSSLTEALETWH---EKAEGKSVIDYGFHM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 136 GLV---PHNLPDLIP-LVKAGVRGFKGFLLDSGVEEfppIGKEYIEEALKVLAEEDTMMMFHAE---------------- 195
Cdd:TIGR02033 124 DIThwnDSVLEEHIPeVKEEGINSFKVFMAYKNLLM---VDDEELFEILKRLKELGALLQVHAEngdiiaelqarmlaqg 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 196 --LPKAHEdqqqpeqshreyssflSSRPDSFEIDAINLILECLRARNGPVppvHIVHLASMKAIPLIRKARASGLPVTTE 273
Cdd:TIGR02033 201 itGPEYHA----------------LSRPPELEAEAVARAITLAALADAPL---YVVHVSTKDAADEIAQARKKGQPVFGE 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 274 TCFHYLCIAAEQIP----DGATYFkCCPPIRSESNRQGLWDALREGVIGSVVSDHSP-CTPELKNLQKGDFFDSWGGIAS 348
Cdd:TIGR02033 262 TCPQYLVLDDTHYDkpgfEGAKYV-CSPPLREPEDQDALWSALSSGALQTVGSDHCTfNFAQKKAIGKDDFTKIPNGGPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 349 VGLGLPLMFTQGC-----SLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGM 423
Cdd:TIGR02033 341 VEERMSLLFDEGVakgriTLEKFVEVTSTNPAKIFNLYPRKGTIAVGSDADIVIWDPNRTTVISAETHHSNADYNPFEGF 420
|
410 420
....*....|....*....|.
gi 398364693 424 TVKGTVLKTILRGQVVYTNAN 444
Cdd:TIGR02033 421 KVRGAPVSVLSRGRVVVEDGQ 441
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
26-442 |
2.36e-50 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 176.79 E-value: 2.36e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 26 TESGTILDVLEGSVVMEKTEITKYEIHTLenvspctiLPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlN 105
Cdd:PRK07575 26 VEDGKIVAIAPEISATAVDTVIDAEGLTL--------LPGVIDPQVHFREPGLEHKEDLFTASRACAKGGVTSFLEMP-N 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 106 AIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHNLPDLipLVKAGVRGFKGFLLDSG----VEEfppigkeyiEEAL- 180
Cdd:PRK07575 97 TKPLTTTQAALDDKLARAAEKCVVNYGFFIGATPDNLPEL--LTANPTCGIKIFMGSSHgpllVDE---------EAALe 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 181 KVLAEEDTMMMFHAElpkaheDQQQPEQSHREYSSflSSRPDSF-----EIDAINLILECLRARNGPVPPVHIVHLASMK 255
Cdd:PRK07575 166 RIFAEGTRLIAVHAE------DQARIRARRAEFAG--ISDPADHsqiqdEEAALLATRLALKLSKKYQRRLHILHLSTAI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 256 AIPLIRKARASGlpVTTETCFHYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLq 335
Cdd:PRK07575 238 EAELLRQDKPSW--VTAEVTPQHLLLNTDAYERIGTLAQMNPPLRSPEDNEALWQALRDGVIDFIATDHAPHTLEEKAQ- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 336 kgDFFDSWGGIASVGLGLPLMFTQG----CSLVDIVTWCCKNTSHQVGLSHqKGTIAPGYDADLVVFDTASKHKISNSSV 411
Cdd:PRK07575 315 --PYPNSPSGMPGVETSLPLMLTAAmrgkCTVAQVVRWMSTAVARAYGIPN-KGRIAPGYDADLVLVDLNTYRPVRREEL 391
|
410 420 430
....*....|....*....|....*....|.
gi 398364693 412 YFKNKLTAYNGMTVKGTVLKTILRGQVVYTN 442
Cdd:PRK07575 392 LTKCGWSPFEGWNLTGWPVTTIVGGQIVFDR 422
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
61-439 |
1.27e-46 |
|
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: 164.21 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 61 TILPGLVDSHVHLN--------EPGRTSWEGFETGTQAAISGGVTTVVDMPlnaippTTNVENFRIKLEAAEgQMWCDVG 132
Cdd:pfam01979 1 IVLPGLIDAHVHLEmgllrgipVPPEFAYEALRLGITTMLKSGTTTVLDMG------ATTSTGIEALLEAAE-ELPLGLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 133 FWGG-------LVPHNLPDLIPLVKAGVRGFKGFLlDSGV------EEFPPIGKEYIEEALKVLAEEDTMMMFHA-ELPK 198
Cdd:pfam01979 74 FLGPgcsldtdGELEGRKALREKLKAGAEFIKGMA-DGVVfvglapHGAPTFSDDELKAALEEAKKYGLPVAIHAlETKG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 199 AHEDQQQPEQSHREYSSFLSSRPDSFEIDAINLILEclrarngpvppvHIVHLASMKAIPLIRKARASGLPvttetcfhy 278
Cdd:pfam01979 153 EVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILA------------HGVHLSPTEANLLAEHLKGAGVA--------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 279 LCIAAEQIpdgatyfkccppirSESNRQGLWDALREGVIGSVVSDHSPCtpelknlqkGDFFDSWGGIAsVGLGLPLMFT 358
Cdd:pfam01979 212 HCPFSNSK--------------LRSGRIALRKALEDGVKVGLGTDGAGS---------GNSLNMLEELR-LALELQFDPE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 359 QGCSLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFDTaskhkisnssvyfkNKLTAYNGMTVKGTVLKTILRGQV 438
Cdd:pfam01979 268 GGLSPLEALRMATINPAKALGLDDKVGSIEVGKDADLVVVDL--------------DPLAAFFGLKPDGNVKKVIVKGKI 333
|
.
gi 398364693 439 V 439
Cdd:pfam01979 334 V 334
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
62-455 |
2.41e-45 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 164.49 E-value: 2.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEP---GRTSWEGFETGTQAAISGGVTTV-------VDMPLNAIppttnVENFRIKleaAEGQMWCDV 131
Cdd:PRK13404 52 VLPGGVDSHCHIDQPsgdGIMMADDFYTGTVSAAFGGTTTVipfaaqhRGQSLREA-----VEDYHRR---AAGKAVIDY 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 132 GFwgGLV-----PHNLPDLIP-LVKAGVRGFKGFLLDSGVEefppIGKEYIEEALKVLAEEDTMMMFHAE-------LPK 198
Cdd:PRK13404 124 AF--HLIvadptEEVLTEELPaLIAQGYTSFKVFMTYDDLK----LDDRQILDVLAVARRHGAMVMVHAEnhdmiawLTK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 199 AHEDQQQPEQSHREyssflSSRPDSFEIDAINLILECLRARNgpvPPVHIVHLASMKAIPLIRKARASGLPVTTETCFHY 278
Cdd:PRK13404 198 RLLAAGLTAPKYHA-----ISRPMLAEREATHRAIALAELVD---VPILIVHVSGREAAEQIRRARGRGLKIFAETCPQY 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 279 LCIAAEQIP----DGATYFkCCPPIRSESNRQGLWDALREGVIGSVVSDHSPC---TPELKNLQKGD--FFDSWGGIASV 349
Cdd:PRK13404 270 LFLTAEDLDrpgmEGAKYI-CSPPPRDKANQEAIWNGLADGTFEVFSSDHAPFrfdDTDGKLAAGANpsFKAIANGIPGI 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 350 GLGLPLMFTQGC-----SLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMT 424
Cdd:PRK13404 349 ETRLPLLFSEGVvkgriSLNRFVALTSTNPAKLYGLYPRKGAIAIGADADIAIWDPDREVTITNADLHHAADYTPYEGMR 428
|
410 420 430
....*....|....*....|....*....|.
gi 398364693 425 VKGTVLKTILRGQVVYTNANGVSKTPLGQTL 455
Cdd:PRK13404 429 VTGWPVTVLSRGRVVVEDGELVAERGSGQFL 459
|
|
| PRK01211 |
PRK01211 |
dihydroorotase; Provisional |
62-453 |
3.21e-41 |
|
dihydroorotase; Provisional
Pssm-ID: 179247 [Multi-domain] Cd Length: 409 Bit Score: 151.55 E-value: 3.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHN 141
Cdd:PRK01211 44 ILPAATDIHVHFRTPGETEKEDFSTGTLSAIFGGTTFIMDMP-NNNIPIKDYNAFSDKLGRVAPKAYVDFSLYSMETGNN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 142 lpdlIPLVKAGVRGFKGFLLDSGveefPPIGKEYIEEALKVLAEEDTMMMFHAELPKAHEDQQQPEQSHREYSsflSSRP 221
Cdd:PRK01211 123 ----ALILDERSIGLKVYMGGTT----NTNGTDIEGGEIKKINEANIPVFFHAELSECLRKHQFESKNLRDHD---LARP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 222 DSFEIDAINLIleclraRNGPVPPVHIVHLASMKAIPlirkarasglPVTTETCFHYLCIAAEqIPDGaTYFKCCPPIRS 301
Cdd:PRK01211 192 IECEIKAVKYV------KNLDLKTKIIAHVSSIDVIG----------RFLREVTPHHLLLNDD-MPLG-SYGKVNPPLRD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 302 ESNRQGLWDALREGVIGSVVSDHSPCTPElknlQKGDFFDSWGGIASVGLGLPLMF---TQGCSLVDI-VTWCCKNTSHQ 377
Cdd:PRK01211 254 RWTQERLLEEYISGRFDILSSDHAPHTEE----DKQEFEYAKSGIIGVETRVPLFLalvKKKILPLDVlYKTAIERPASL 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364693 378 VGLshQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTV--KGTVlktILRGQVVYTNANGVSKtPLGQ 453
Cdd:PRK01211 330 FGI--KKGKIEEGYDADFMAFDFTNIKKINDKRLHSKCPVSPFNGFDAifPSHV---IMRGEVVIDNYELISE-RTGK 401
|
|
| PRK04250 |
PRK04250 |
dihydroorotase; Provisional |
34-455 |
1.01e-39 |
|
dihydroorotase; Provisional
Pssm-ID: 235265 [Multi-domain] Cd Length: 398 Bit Score: 147.22 E-value: 1.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 34 VLEGSVVMEKTEITKYEIHTLE-----NVSPCTILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIP 108
Cdd:PRK04250 12 IVEGGIGIENGRISKISLRDLKgkeviKVKGGIILPGLIDVHVHLRDFEESYKETIESGTKAALHGGITLVFDMP-NTKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 109 PTTNVENFRIKLEAAEGQMWCDVgFWGGLVPHNLPDLIPlVKAGVrgFKGFLLdsgveefPPIGKEYIEEALKVLAEEDT 188
Cdd:PRK04250 91 PIMDEKTYEKRMRIAEKKSYADY-ALNFLIAGNCEKAEE-IKADF--YKIFMG-------ASTGGIFSENFEVDYACAPG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 189 MMMFHAELPkahedqqqpeqshrEYSSFLSSRPDSFEIDAINlilECLRARNGPVPPVHIVHLASMKAIPLIRKaraSGL 268
Cdd:PRK04250 160 IVSVHAEDP--------------ELIREFPERPPEAEVVAIE---RALEAGKKLKKPLHICHISTKDGLKLILK---SNL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 269 P-VTTETCFHYLCIAAEQIPDGaTYFKCCPPIRSESNRQGLWDALREgvIGSVVSDHSPCTPELKnlQKGDffdswGGIA 347
Cdd:PRK04250 220 PwVSFEVTPHHLFLTRKDYERN-PLLKVYPPLRSEEDRKALWENFSK--IPIIASDHAPHTLEDK--EAGA-----AGIP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 348 SVGLGLPLMF---TQG-CSLVDIVTWCCKNTSHQVGLSHqKGtIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGM 423
Cdd:PRK04250 290 GLETEVPLLLdaaNKGmISLFDIVEKMHDNPARIFGIKN-YG-IEEGNYANFAVFDMKKEWTIKAEELYTKAGWTPYEGF 367
|
410 420 430
....*....|....*....|....*....|..
gi 398364693 424 TVKGTVLKTILRGQVVYTNANGVSKtPLGQTL 455
Cdd:PRK04250 368 KLKGKVIMTILRGEVVMEDDEIIGK-PRGVRI 398
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
63-459 |
3.27e-37 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 141.55 E-value: 3.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 63 LPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHNL 142
Cdd:PRK09236 53 LPGMIDDQVHFREPGLTHKGDIASESRAAVAGGITSFMEMP-NTNPPTTTLEALEAKYQIAAQRSLANYSFYFGATNDNL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 143 PDLIPLVKAGVRGFKGFLLDS-G---VEEfppigkeyiEEAL-KVLAEEDTMMMFHAElpkaHED--QQQPEQSHREYSs 215
Cdd:PRK09236 132 DEIKRLDPKRVCGVKVFMGAStGnmlVDN---------PETLeRIFRDAPTLIATHCE----DTPtiKANLAKYKEKYG- 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 216 flssrpDSFEIDAINLILE---CLR-------------ARngpvppVHIVHLASMKAIPLIRKARASGLPVTTETCFHYL 279
Cdd:PRK09236 198 ------DDIPAEMHPLIRSaeaCYKssslavslakkhgTR------LHVLHISTAKELSLFENGPLAEKRITAEVCVHHL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 280 CIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKnlqKGDFFDSWGGIASVGLGLPLMF-- 357
Cdd:PRK09236 266 WFDDSDYARLGNLIKCNPAIKTASDREALRQALADDRIDVIATDHAPHTWEEK---QGPYFQAPSGLPLVQHALPALLel 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 358 -TQG-CSLVDIVtwccKNTSHQVGLS---HQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKT 432
Cdd:PRK09236 343 vHEGkLSLEKVV----EKTSHAPAILfdiKERGFIREGYWADLVLVDLNSPWTVTKENILYKCGWSPFEGRTFRSRVATT 418
|
410 420
....*....|....*....|....*..
gi 398364693 433 ILRGQVVYTNaNGVSKTPLGQTLLDSR 459
Cdd:PRK09236 419 FVNGQLVYHN-GQLVESCRGQRLEFDR 444
|
|
| pyrC |
PRK00369 |
dihydroorotase; Provisional |
62-446 |
7.16e-33 |
|
dihydroorotase; Provisional
Pssm-ID: 234738 [Multi-domain] Cd Length: 392 Bit Score: 128.34 E-value: 7.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGlVPHN 141
Cdd:PRK00369 45 ILPGAIDLHVHLRGLKLSYKEDVASGTSEAAYGGVTLVADMP-NTIPPLNTPEAITEKLAELEYYSRVDYFVYSG-VTKD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 142 LPDLIPLvkaGVRGFKGFLLDsgVEEfppigkeyiEEALKVLAEEDTMMMFHAELPKAhedqQQPEQSHReyssflssRP 221
Cdd:PRK00369 123 PEKVDKL---PIAGYKIFPED--LER---------EETFRVLLKSRKLKILHPEVPLA----LKSNRKLR--------RN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 222 DSFEIDAINLILECLRarngpvppVHIVHLASmkaIPLIRKARASGLpvTTETCFHYLCIAAEqipdGATYFKCCPPIRS 301
Cdd:PRK00369 177 CWYEIAALYYVKDYQN--------VHITHASN---PRTVRLAKELGF--TVDITPHHLLVNGE----KDCLTKVNPPIRD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 302 ESNRQGLWDALREgvIGSVVSDHSPCTPElknlQKGDFFDSW-GGIASVGLGLP----LMFTQGCSLVDIVTWCCKNTSH 376
Cdd:PRK00369 240 INERLWLLQALSE--VDAIASDHAPHSSF----EKLQPYEVCpPGIAALSFTPPfiytLVSKGILSIDRAVELISTNPAR 313
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 377 QVGLSHqkGTIAPGYDADLVVFdtaSKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTNANGV 446
Cdd:PRK00369 314 ILGIPY--GEIKEGYRANFTVI---QFEDWRYSTKYSKVIETPLDGFELKASVYATIVQGKLAYLEGEVF 378
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
62-442 |
5.61e-30 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 121.87 E-value: 5.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEP--GRTSWEGFETGTQAAISGGVTTVVDMplnAIPPTTNV----ENFRIKLEAAEgqmwCDVGF-- 133
Cdd:PLN02942 55 VMPGGIDPHTHLAMPfmGTETIDDFFSGQAAALAGGTTMHIDF---VIPVNGNLlagyEAYEKKAEKSC----MDYGFhm 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 134 ----WGGLVPHnlpDLIPLVKA-GVRGFKGFLLDSGVEEfppIGKEYIEEALKVLAEEDTMMMFHAELPKAHEDQQQ--- 205
Cdd:PLN02942 128 aitkWDDTVSR---DMETLVKEkGINSFKFFMAYKGSLM---VTDELLLEGFKRCKSLGALAMVHAENGDAVFEGQKrmi 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 206 ------PEqSHReyssflSSRPDSFEIDAINLILECLRARNgpvPPVHIVHLASMKAIPLIRKARASGLPVTTETCFHYL 279
Cdd:PLN02942 202 elgitgPE-GHA------LSRPPLLEGEATARAIRLAKFVN---TPLYVVHVMSIDAMEEIARARKSGQRVIGEPVVSGL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 280 CIAAEQI--PD--GATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSP-CTPElKNLQKGDFFDSWGGIASVGLGLP 354
Cdd:PLN02942 272 VLDDSKLwdPDftIASKYVMSPPIRPAGHGKALQAALSSGILQLVGTDHCPfNSTQ-KAFGKDDFRKIPNGVNGIEERMH 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 355 LMFTQGC-----SLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTV 429
Cdd:PLN02942 351 LVWDTMVesgqiSPTDYVRVTSTECAKIFNIYPRKGAILAGSDADIIILNPNSTFTISAKTHHSRIDTNVYEGRRGKGKV 430
|
410
....*....|...
gi 398364693 430 LKTILRGQVVYTN 442
Cdd:PLN02942 431 EVTISQGRVVWEN 443
|
|
| CAD_DHOase |
cd01316 |
The eukaryotic CAD protein is a trifunctional enzyme of carbamoylphosphate ... |
62-452 |
9.67e-30 |
|
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: 118.71 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHN 141
Cdd:cd01316 4 RLPGLIDVHVHLREPGATHKEDFASGTKAALAGGFTMVRAMP-NTNPSIVDVASLKLVQSLAQAKARCDYAFSIGATSTN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 142 LPDLIPLVKAGVrGFKGFLLdsgvEEFPPIGKEyieealKVLAEEDTMMMFHAELP-KAHEDQQqpeqshreyssflssr 220
Cdd:cd01316 83 AATVGELASEAV-GLKFYLN----ETFSTLILD------KITAWASHFNAWPSTKPiVTHAKSQ---------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 221 pdsfEIDAInLILECLRARNgpvppVHIVHLASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGAtyFKCCPPIR 300
Cdd:cd01316 136 ----TLAAV-LLLASLHNRS-----IHICHVSSKEEINLIRLAKARGLKVTCEVSPHHLFLSQDDLPRGQ--YEVRPFLP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 301 SESNRQGLWDALreGVIGSVVSDHSPCTPELKNLQKGDFfdswgGIASVGLGLPLMFT---QG-CSLVDIVTWCCKNTSH 376
Cdd:cd01316 204 TREDQEALWENL--DYIDCFATDHAPHTLAEKTGNKPPP-----GFPGVETSLPLLLTavhEGrLTIEDIVDRLHTNPKR 276
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364693 377 QVGLSHQKGTIapgydadlVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVYTNANGVSKTPLG 452
Cdd:cd01316 277 IFNLPPQSDTY--------VEVDLDEEWTIPKNPLQSKKGWTPFEGKKVKGKVQRVVLRGETAFIDGEIVAPPGFG 344
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
30-432 |
6.57e-28 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 114.70 E-value: 6.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 30 TILDVLEGSVVMEKTEITKYEIHTLENVSPCT--IL-PGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNA 106
Cdd:PRK07369 20 RIADVLIEDGKIQAIEPHIDPIPPDTQIIDASglILgPGLVDLYSHSGEPGFEERETLASLAAAAAAGGFTRVAILP-DT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 107 IPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVPHN----LPDLIPLVKAGVRGFKgfllDSGVEEFPPIgkeyIEEALKV 182
Cdd:PRK07369 99 FPPLDNPATLARLQQQAQQIPPVQLHFWGALTLGGqgkqLTELAELAAAGVVGFT----DGQPLENLAL----LRRLLEY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 183 LAEEDTMMMFHAELPkahedQQQPEQSHRE-YSSF---LSSRPDSFEIDAINLILECLRARNgpvPPVHIVHLASMKAIP 258
Cdd:PRK07369 171 LKPLGKPVALWPCDR-----SLAGNGVMREgLLALrlgLPGDPASAETTALAALLELVAAIG---TPVHLMRISTARSVE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 259 LIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLQkgd 338
Cdd:PRK07369 243 LIAQAKARGLPITASTTWMHLLLDTEALASYDPNLRLDPPLGNPSDRQALIEGVRTGVIDAIAIDHAPYTYEEKTVA--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 339 FFDSWGGIASVGLGLPLMFTQgcsLVDIVTWC--------CKNTSHQVGLSHqkGTIAPGYDADLVVFDTASKHKISNSS 410
Cdd:PRK07369 320 FAEAPPGAIGLELALPLLWQN---LVETGELSalqlwqalSTNPARCLGQEP--PSLAPGQPAELILFDPQKTWTVSAQT 394
|
410 420
....*....|....*....|..
gi 398364693 411 VYFKNKLTAYNGMTVKGTVLKT 432
Cdd:PRK07369 395 LHSLSRNTPWLGQTLKGRVLQT 416
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
60-443 |
5.88e-26 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 109.38 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVdmplnaIPPTTN--------VENFRIKLEAAEGQMWCDV 131
Cdd:PRK07627 51 LIVCPGLVDLSARLREPGYEYKATLESEMAAAVAGGVTSLV------CPPDTDpvldepglVEMLKFRARNLNQAHVYPL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 132 G-FWGGLVPHNLPDLIPLVKAGVRGFkgflldsGVEEFPPIGKEYIEEALKV---------LAEEDtmmMFHAELPKAHE 201
Cdd:PRK07627 125 GaLTVGLKGEVLTEMVELTEAGCVGF-------SQANVPVVDTQVLLRALQYastfgftvwLRPLD---AFLGRGGVAAS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 202 DqqqpeqshrEYSSF--LSSRPDSFEIDAINLILECLR---ARngpvppVHIVHLASMKAIPLIRKARASGLPVTTETCF 276
Cdd:PRK07627 195 G---------AVASRlgLSGVPVAAETIALHTIFELMRvtgAR------VHLARLSSAAGVALVRAAKAEGLPVTCDVGV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 277 HYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLQkgdFFDSWGGIASVGLGLPLM 356
Cdd:PRK07627 260 NHVHLIDVDIGYFDSQFRLDPPLRSQRDREAIRAALADGTIDAICSDHTPVDDDEKLLP---FAEATPGATGLELLLPLT 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 357 FTQGC-SLVDIVTWCCKNTSHQVG-LSHQKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLKTIL 434
Cdd:PRK07627 337 LKWADeAKVPLARALARITSAPARvLGLPAGRLAEGAPADLCVFDPDAHWRVEPRALKSQGKNTPFLGYELPGRVRATLV 416
|
....*....
gi 398364693 435 RGQVVYTNA 443
Cdd:PRK07627 417 AGQVAFERR 425
|
|
| PRK09059 |
PRK09059 |
dihydroorotase; Validated |
61-441 |
1.39e-21 |
|
dihydroorotase; Validated
Pssm-ID: 181631 [Multi-domain] Cd Length: 429 Bit Score: 96.64 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 61 TILPGLVDSHVHLNEPGRTSWEGFETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQmwcdvgfwgGLVph 140
Cdd:PRK09059 57 AVAPGLVDARVFVGEPGAEHRETIASASRAAAAGGVTSIIMMP-DTDPVIDDVALVEFVKRTARDT---------AIV-- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 141 NLPDLIPLVKaGVRGFK----GFLLDSGVEEFppigkeyiEEALKVLAeeDTMMMFHA-------ELPKAHEDQQ----- 204
Cdd:PRK09059 125 NIHPAAAITK-GLAGEEmtefGLLRAAGAVAF--------TDGRRSVA--NTQVMRRAltyardfDAVIVHETRDpdlgg 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 205 QPEQSHREYSSFL--SSRPDsfEIDAINL-----ILECLRARngpvppVHIVHLASMKAIPLIRKARASGLPVTTETCFH 277
Cdd:PRK09059 194 NGVMNEGLFASWLglSGIPR--EAEVIPLerdlrLAALTRGR------YHAAQISCAESAEALRRAKDRGLKVTAGVSIN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 278 YLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPELKNLQkgdFFDSWGGiaSVGL------ 351
Cdd:PRK09059 266 HLSLNENDIGEYRTFFKLSPPLRTEDDRVAMVEAVASGTIDIIVSSHDPQDVDTKRLP---FSEAAAG--AIGLetllaa 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 352 GLPLMFTQGCSLVDIVTWCCKNTSHQVGLShqKGTIAPGYDADLVVFDTASKHKISNSSVYFKNKLTAYNGMTVKGTVLK 431
Cdd:PRK09059 341 ALRLYHNGEVPLLRLIEALSTRPAEIFGLP--AGTLKPGAPADIIVIDLDEPWVVDPEDLKSRSKNTPFEEARFQGRVVR 418
|
410
....*....|
gi 398364693 432 TILRGQVVYT 441
Cdd:PRK09059 419 TIVAGKTVYE 428
|
|
| PRK08417 |
PRK08417 |
metal-dependent hydrolase; |
251-440 |
4.36e-20 |
|
metal-dependent hydrolase;
Pssm-ID: 236262 [Multi-domain] Cd Length: 386 Bit Score: 91.69 E-value: 4.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 251 LASMKAIPLIRKARASGLPVTTETCFHYLCIAAEQIPDGATYFKCCPPIRSESNRQGLWDALREGVIGSVVSDHSPCTPE 330
Cdd:PRK08417 203 LALPRSLELLDKFKSEGEKLLKEVSIHHLILDDSACENFNTAAKLNPPLRSKEDRLALLEALKEGKIDFLTSLHSAKSNS 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 331 LKNLQkgdFFDSWGGIASVGLGLPLMFT----QG-CSLVDIVTWCCKNTSHQVGLshQKGTIAPGYDADLVVFDtaskhk 405
Cdd:PRK08417 283 KKDLA---FDEAAFGIDSICEYFSLCYTylvkEGiITWSELSRFTSYNPAQFLGL--NSGEIEVGKEADLVLFD------ 351
|
170 180 190
....*....|....*....|....*....|....*
gi 398364693 406 iSNSSVYFKNKLTAYNGMTVKGTVLKTILRGQVVY 440
Cdd:PRK08417 352 -PNESTIIDDNFSLYSGDELYGKIEAVIIKGKLYL 385
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
66-271 |
7.42e-14 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 71.60 E-value: 7.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 66 LVDSHVHL----NEPGRTSWEG--------------FETGTQAAISGGVTTVVDMPlNAIPPTTNVENFRIKLEAAEGQM 127
Cdd:cd01292 1 FIDTHVHLdgsaLRGTRLNLELkeaeelspedlyedTLRALEALLAGGVTTVVDMG-STPPPTTTKAAIEAVAEAARASA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 128 WCDVGFWGGL-----------VPHNLPDLIPLVKAGVRGFKGFLLDSGVEEFPpigkEYIEEALKVLAEEDTMMMFHAEL 196
Cdd:cd01292 80 GIRVVLGLGIpgvpaavdedaEALLLELLRRGLELGAVGLKLAGPYTATGLSD----ESLRRVLEEARKLGLPVVIHAGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 197 PKAH-----EDQQQPEQSHREYSSfLSSRPDSFEidainliLECLRARNGPV---PPVHIVHLASMKAIPLIRKARASGL 268
Cdd:cd01292 156 LPDPtraleDLVALLRLGGRVVIG-HVSHLDPEL-------LELLKEAGVSLevcPLSNYLLGRDGEGAEALRRLLELGI 227
|
...
gi 398364693 269 PVT 271
Cdd:cd01292 228 RVT 230
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
62-399 |
5.28e-09 |
|
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: 57.71 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 62 ILPGLVDSHVHL--------------NE------PGRTSWEGF---ETGTQAAISGGVTTVVDMPLNAippttNVEnfri 118
Cdd:cd01309 27 VTPGLIDAHSHLgldeeggvretsdaNEetdpvtPHVRAIDGInpdDEAFKRARAGGVTTVQVLPGSA-----NLI---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 119 kleaaeGQMWCDVGFWGGLVPHNLPDliplvkaGVRGFKGFLldsgvEEFPPI--GKEYIEEALKVlaeeDTMMMFHAEL 196
Cdd:cd01309 98 ------GGQGVVIKTDGGTIEDMFIK-------APAGLKMAL-----GENPKRvyGGKGKEPATRM----GVAALLRDAF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 197 PKAHEDqqqpeqsHREYSSFLSSRPDSFEIDainLILECL-RARNGPVPpVHI-VHLAS-MKAipLIRKARASGLPVTTE 273
Cdd:cd01309 156 IKAQEY-------GRKYDLGKNAKKDPPERD---LKLEALlPVLKGEIP-VRIhAHRADdILT--AIRIAKEFGIKITIE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 274 TCFH-YLC---IAAEQIP--DGATYFkccPPIRSESNRQGLWDA--LRE--GVIGSVVSDHSPCTPELKNLQKGdffdsw 343
Cdd:cd01309 223 HGAEgYKLadeLAKHGIPviYGPTLT---LPKKVEEVNDAIDTNayLLKkgGVAFAISSDHPVLNIRNLNLEAA------ 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 398364693 344 ggiASVGLGLPLmfTQGCSLVDIvtwcckNTSHQVGLSHQKGTIAPGYDADLVVFD 399
Cdd:cd01309 294 ---KAVKYGLSY--EEALKAITI------NPAKILGIEDRVGSLEPGKDADLVVWN 338
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
60-399 |
6.82e-07 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 51.11 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNEPGRTSWEGFETGT---------------QAAISGGVTTVVDMPLNaippttnveNFRIKLEAAE 124
Cdd:COG1228 61 KTVLPGLIDAHTHLGLGGGRAVEFEAGGGitptvdlvnpadkrlRRALAAGVTTVRDLPGG---------PLGLRDAIIA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 125 GQMWCDVG-----------FWGGLVPHNLPDLIPLV----KAGVRGFKGFlLDSGVEEFPPigkeyiEEALKVLAEE--- 186
Cdd:COG1228 132 GESKLLPGprvlaagpalsLTGGAHARGPEEARAALrellAEGADYIKVF-AEGGAPDFSL------EELRAILEAAhal 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 187 DTMMMFHAElpkahedqqqpeqshreyssflssrpdsfEIDAINLILEClrarnGpvppVH-IVHLASMKAiPLIRKARA 265
Cdd:COG1228 205 GLPVAAHAH-----------------------------QADDIRLAVEA-----G----VDsIEHGTYLDD-EVADLLAE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 266 SGLPVTTETCFHYLCIAAEQIPDGATyfkccppiRSESNRQGLWDALRE----GV---IGsvvSDHspctpelknlqkgd 338
Cdd:COG1228 246 AGTVVLVPTLSLFLALLEGAAAPVAA--------KARKVREAALANARRlhdaGVpvaLG---TDA-------------- 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 398364693 339 ffdswGGIASVGLGLPLMFTQGC----SLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFD 399
Cdd:COG1228 301 -----GVGVPPGRSLHRELALAVeaglTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVLLD 360
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
60-406 |
3.75e-06 |
|
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: 48.86 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 60 CTILPGLVDSHVHLNepgrtsWEGFETGTQA---AISGGVTTVVDMplnAIPPTTNVENFRIKL-EAAEGQMWC--DVGF 133
Cdd:cd01307 30 CYVSPGWIDLHVHVY------QGGTRYGDRPdmiGVKSGVTTVVDA---GSAGADNIDGFRYTViERSATRVYAflNISR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 134 WGGLVPHNLPDL----IPLVKAGVRGFKGFL----LDSGVEEFPPIGKEYIEEALKVLAEEDTMMMfhaelpkAHEDQQQ 205
Cdd:cd01307 101 VGLVAQDELPDPdnidEDAVVAAAREYPDVIvglkARASKSVVGEWGIKPLELAKKIAKEADLPLM-------VHIGSPP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 206 PEQShrEYSSFLssRPDsfeidaiNLILECLRAR-NGPVPPVHIVHlasmkaiPLIRKARASGLPV-----TTETCFHyl 279
Cdd:cd01307 174 PILD--EVVPLL--RRG-------DVLTHCFNGKpNGIVDEEGEVL-------PLVRRARERGVIFdvghgTASFSFR-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 280 ciAAEQipdgatyfkccppirsesnrqglwdALREGVIGSVVSDHSPCtpelKNLQKGDFFDswggiasvglGLPLM--- 356
Cdd:cd01307 234 --VARA-------------------------AIAAGLLPDTISSDIHG----RNRTNGPVYA----------LATTLskl 272
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 398364693 357 FTQGCSLVDIVTWCCKNTSHQVGLSHqKGTIAPGYDADLVVFDTASKHKI 406
Cdd:cd01307 273 LALGMPLEEVIEAVTANPARMLGLAE-IGTLAVGYDADLTVFDLKDGRVE 321
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
360-399 |
7.71e-06 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 47.79 E-value: 7.71e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 398364693 360 GCSLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFD 399
Cdd:COG1820 321 GLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLD 360
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
360-399 |
1.17e-05 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 47.19 E-value: 1.17e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 398364693 360 GCSLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFD 399
Cdd:cd00854 323 GCPLEEAVRMASLNPAKLLGLDDRKGSLKPGKDADLVVLD 362
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
376-440 |
2.47e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 46.72 E-value: 2.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364693 376 HQVGLSHQKGTIAPGYDADLVVFD----TASKHKISNSsvyfknkltayngmtvkgTVLKTILRGQVVY 440
Cdd:COG1574 482 YAAFEEDEKGSLEPGKLADFVVLDrdplTVPPEEIKDI------------------KVLLTVVGGRVVY 532
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
93-440 |
3.04e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 46.37 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 93 SGGVTTVVDMPLNAIPPTTNVENFRIKLEAAEGQMWCDVGFWGGLVP--HNLPDLIPLVKAGVRGFKGFLLDSGVEEFPP 170
Cdd:pfam07969 162 GFGITSVDGGGGNVHSLDDYEPLRELTAAEKLKELLDAPERLGLPHSiyELRIGAMKLFADGVLGSRTAALTEPYFDAPG 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 171 IG-KEYIEEALKVLAEedtmmmfhaelpKAHEDQQQPEQsHREYSSFLSSRPDSFEIdainlilecLRARNGPVPPVHIV 249
Cdd:pfam07969 242 TGwPDFEDEALAELVA------------AARERGLDVAI-HAIGDATIDTALDAFEA---------VAEKLGNQGRVRIE 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 250 HLASMKAIP--LIRKARASGLPVTTETCFHYLCIAAEQIPDGAtyfkccppirsesNRQGLWDALRE----GVIGSVVSD 323
Cdd:pfam07969 300 HAQGVVPYTysQIERVAALGGAAGVQPVFDPLWGDWLQDRLGA-------------ERARGLTPVKEllnaGVKVALGSD 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 324 hSPCTPelknlqkgdfFDSWGGI------ASVGLGLPLMFTQGCSLVDIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVV 397
Cdd:pfam07969 367 -APVGP----------FDPWPRIgaavmrQTAGGGEVLGPDEELSLEEALALYTSGPAKALGLEDRKGTLGVGKDADLVV 435
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 398364693 398 FDtaskhkisnssvyfknkltaYNGMTVK------GTVLKTILRGQVVY 440
Cdd:pfam07969 436 LD--------------------DDPLTVDppaiadIRVRLTVVDGRVVY 464
|
|
| ureC |
PRK13308 |
urease subunit alpha; Reviewed |
64-157 |
3.01e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 183965 [Multi-domain] Cd Length: 569 Bit Score: 43.16 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 64 PGLVDSHVHLNEPGRtswegfetgTQAAISGGVTTVVDMPLNAIPP--TTNVENFRIKLEAAEGqmW-CDVGFWGGLVPH 140
Cdd:PRK13308 133 PGAIDVHVHFDSAQL---------VDHALASGITTMLGGGLGPTVGidSGGPFNTGRMLQAAEA--WpVNFGFLGRGNSS 201
|
90
....*....|....*..
gi 398364693 141 NLPDLIPLVKAGVRGFK 157
Cdd:PRK13308 202 KPAALIEQVEAGACGLK 218
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
247-402 |
5.60e-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: 41.86 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 247 HIVHLaSMKAIPLIRKARASG--LPVTTetcfHYLCiaaeqipdgATYfkccPPIRsesnrqglwDALREGVIGSVVSDH 324
Cdd:cd01296 235 HLEHT-SDEGIAALAEAGTVAvlLPGTA----FSLR---------ETY----PPAR---------KLIDAGVPVALGTDF 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 325 SPCTPelknlqkgdFFDSwggiasvglgLPLMFTQGCSLV-----DIVTWCCKNTSHQVGLSHQKGTIAPGYDADLVVFD 399
Cdd:cd01296 288 NPGSS---------PTSS----------MPLVMHLACRLMrmtpeEALTAATINAAAALGLGETVGSLEVGKQADLVILD 348
|
...
gi 398364693 400 TAS 402
Cdd:cd01296 349 APS 351
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
56-101 |
1.35e-03 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 40.92 E-value: 1.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 398364693 56 NVSPCTILPGLVDSHVHLNePGRTSWegfetGTQA---AISGGVTTVVD 101
Cdd:COG3964 46 DASGLYVTPGLIDLHTHVF-PGGTDY-----GVDPdgvGVRSGVTTVVD 88
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
245-274 |
1.88e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.45 E-value: 1.88e-03
10 20 30
....*....|....*....|....*....|....*.
gi 398364693 245 PVHIVHLASM------KAIPLIRKARASGLPVTTET 274
Cdd:PRK09061 247 HMHICHVNSTslrdidRCLALVEKAQAQGLDVTTEA 282
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
56-101 |
2.71e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 39.83 E-value: 2.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 398364693 56 NVSPCTILPGLVDSHVHlNEPGRTSWE------GFETgtqaaisgGVTTVVD 101
Cdd:PRK09237 45 DLSGLYVSPGWIDLHVH-VYPGSTPYGdepdevGVRS--------GVTTVVD 87
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
61-102 |
3.33e-03 |
|
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The function of this subgroup is unknown.
Pssm-ID: 238624 [Multi-domain] Cd Length: 342 Bit Score: 39.58 E-value: 3.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 398364693 61 TILPGLVDSHVHL---NEPGRTSWEG---FETGT-----QAAISGGVTTVVDM 102
Cdd:cd01299 10 TLMPGLIDAHTHLgsdPGDLPLDLALpveYRTIRatrqaRAALRAGFTTVRDA 62
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
65-157 |
3.51e-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: 39.62 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 65 GLVDSHVHLNEPgRTSWEGFETGTQAAISGGvTTVVDmPLNAIPPTTNVENFRIKLEAAEGqMWCDVGFWGGLVPHNLPD 144
Cdd:cd00375 130 GGIDTHVHFICP-QQIEEALASGITTMIGGG-TGPAA-GTKATTCTPGPWNIKRMLQAADG-LPVNIGFLGKGNGSSPDA 205
|
90
....*....|...
gi 398364693 145 LIPLVKAGVRGFK 157
Cdd:cd00375 206 LAEQIEAGACGLK 218
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
359-422 |
3.67e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 39.70 E-value: 3.67e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364693 359 QGCSLVDIVTWCCKNTSHQVGLSHqKGTIAPGYDADLVVFDTASKHKIsnSSVYFKNKLTAYNG 422
Cdd:COG1001 282 LGLDPVTAIQMATLNAAEHFGLKD-LGAIAPGRRADIVLLDDLEDFKV--EKVYADGKLVAEDG 342
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
12-100 |
5.84e-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: 38.91 E-value: 5.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364693 12 IINGANkpatiVYSTESGTILDVLEGS----VVMEKTEITKYEIHTLENVSPCTILPGLVDSHVHLNEPGRTSweGFETG 87
Cdd:cd01308 3 LIKNAE-----VYAPEYLGKKDILIAGgkilAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEG--GPSTR 75
|
90
....*....|....*...
gi 398364693 88 T-----QAAISGGVTTVV 100
Cdd:cd01308 76 TpevtlSDLTTAGVTTVV 93
|
|
| |
