|
Name |
Accession |
Description |
Interval |
E-value |
| EF_0837 |
TIGR03583 |
probable amidohydrolase EF_0837/AHA_3915; Members of this family of relatively uncommon ... |
2-367 |
0e+00 |
|
probable amidohydrolase EF_0837/AHA_3915; Members of this family of relatively uncommon proteins are found in both Gram-positive (e.g. Enterococcus faecalis) and Gram-negative (e.g. Aeromonas hydrophila) bacteria, as part of a cluster of conserved proteins. These proteins resemble aminohydrolases (see pfam01979), including dihydroorotases. The function is unknown. [Hypothetical proteins, Conserved]
Pssm-ID: 132622 Cd Length: 365 Bit Score: 577.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 2 FDTLIKNGRLVDGSKIEVAIEKGMIKAVAAEINQPAQEVVDLEGKYYLSAGWIDDHVHCYEKMNLYYDYPDQIGVEKGVT 81
Cdd:TIGR03583 1 YDLLIKNGRTVNGTPVDIAIEDGKIAAVGTTITGSAKQTIDLEGETYVSAGWIDDHTHCFPKSALYYDEPDEIGVKTGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 82 TVIDAGTTGAENIREFYQLTKSVKTNVYALMNISKWGIVKQDELADLTKIQEDLVSTALAELPEFIVGIKARMSKTVVGE 161
Cdd:TIGR03583 81 TVVDAGSTGADDIDDFYRLAQQAKTNVFALLNISRIGLVAQDELADLSNLDASAVKQAVERYPDFIVGLKARMSKSVVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 162 NGIKPLELAKKIQTENNDLPLMVHIGSAPPELEEVLSRMERGDVLTHCFNGKPNGILDPkTDQIKNFVWDAYNNGVVFDI 241
Cdd:TIGR03583 161 NGIEPLEIAKQIQQENLELPLMVHIGSAPPELDEILALMEKGDVLTHCFNGKPNGILRE-TGEVKPSVLEAYNRGVILDV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 242 GHGTDSFNFHVAETALKAGMKATSISTDIYIRNRTNGPVFDLATTLEKLRVVGYSWEEIIEKVTAVPARNFHLKNKGQLA 321
Cdd:TIGR03583 240 GHGTASFSFHVAEKAKRAGIFPDTISTDIYIRNRINGPVYSLATVMSKFLALGYSLEEVIEKVTKNAAEILKLTQKGRLQ 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 488217097 322 VNYDADLTIFEIVENEKELKDSNGFTRIAKEQILPIKTIIGGVIYD 367
Cdd:TIGR03583 320 EGYDADLTIFTVKAEPKKLTDSEGDSRIAEEQIKPLAVIIGGEYYE 365
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
18-356 |
0e+00 |
|
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: 530.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 18 EVAIEKGMIKAVAAEINQPAQEVVDLEGKYYLSAGWIDDHVHCYEKMNLYYDYPDQIGVEKGVTTVIDAGTTGAENIREF 97
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPDMIGVKSGVTTVVDAGSAGADNIDGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 98 -YQLTKSVKTNVYALMNISKWGIVKQDELADLTKIQEDLVSTALAELPEFIVGIKARMSKTVVGENGIKPLELAKKIQTE 176
Cdd:cd01307 81 rYTVIERSATRVYAFLNISRVGLVAQDELPDPDNIDEDAVVAAAREYPDVIVGLKARASKSVVGEWGIKPLELAKKIAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 177 NnDLPLMVHIGSAPPELEEVLSRMERGDVLTHCFNGKPNGILDPKTdQIKNFVWDAYNNGVVFDIGHGTDSFNFHVAETA 256
Cdd:cd01307 161 A-DLPLMVHIGSPPPILDEVVPLLRRGDVLTHCFNGKPNGIVDEEG-EVLPLVRRARERGVIFDVGHGTASFSFRVARAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 257 LKAGMKATSISTDIYIRNRTNGPVFDLATTLEKLRVVGYSWEEIIEKVTAVPARNFHLKNKGQLAVNYDADLTIFEIVEN 336
Cdd:cd01307 239 IAAGLLPDTISSDIHGRNRTNGPVYALATTLSKLLALGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDLKDG 318
|
330 340
....*....|....*....|
gi 488217097 337 EKELKDSNGFTRIAKEQILP 356
Cdd:cd01307 319 RVELVDSEGDTLIAERLLVP 338
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-368 |
0e+00 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 506.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 5 LIKNGRLVD-----GSKIEVAIEKGMIKAVAAEINQP-AQEVVDLEGkYYLSAGWIDDHVHCYEKMNLYYDYPDQIGVEK 78
Cdd:PRK09237 2 LLRGGRVIDpangiDGVIDIAIEDGKIAAVAGDIDGSqAKKVIDLSG-LYVSPGWIDLHVHVYPGSTPYGDEPDEVGVRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 79 GVTTVIDAGTTGAENIREFYQLT-KSVKTNVYALMNISKWGIVKQDELADLTKIQEDLVSTALAELPEFIVGIKARMSKT 157
Cdd:PRK09237 81 GVTTVVDAGSAGADNFDDFRKLTiEASKTRVLAFLNISRIGLLAQDELADLEDIDADAVAEAVKRNPDFIVGIKARMSSS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 158 VVGENGIKPLELAKKIQtENNDLPLMVHIGSAPPELEEVLSRMERGDVLTHCFNGKPNGILDPkTDQIKNFVWDAYNNGV 237
Cdd:PRK09237 161 VVGDNGIEPLELAKAIA-AEANLPLMVHIGNPPPSLEEILELLRPGDILTHCFNGKPNRILDE-DGELRPSVLEALERGV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 238 VFDIGHGTDSFNFHVAETALKAGMKATSISTDIYIRNRTNGPVFDLATTLEKLRVVGYSWEEIIEKVTAVPARNFHLKNK 317
Cdd:PRK09237 239 RLDVGHGTASFSFKVAEAAIAAGILPDTISTDIYCRNRINGPVYSLATVMSKFLALGMPLEEVIAAVTKNAADALRLPEL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488217097 318 GQLAVNYDADLTIFEIVENEKELKDSNGFTRIAKEQILPIKTIIGGVIYDN 368
Cdd:PRK09237 319 GRLQVGSDADLTLFTLKDGPFTLTDSEGDSLIGERLLTPLATVRGGKVVLT 369
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
3-367 |
2.36e-173 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 486.98 E-value: 2.36e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 3 DTLIKNGRLVDGS-----KIEVAIEKGMIKAVAAEINQP-AQEVVDLEGkYYLSAGWIDDHVHCYEKMNLYYDYPDQIGV 76
Cdd:COG3964 1 DLLIKGGRVIDPAngidgVMDIAIKDGKIAAVAKDIDAAeAKKVIDASG-LYVTPGLIDLHTHVFPGGTDYGVDPDGVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 77 EKGVTTVIDAGTTGAENIREFYQ-LTKSVKTNVYALMNISKWGIVKQDELADLTKIQEDLVSTALAELPEFIVGIKARMS 155
Cdd:COG3964 80 RSGVTTVVDAGSAGAANFDGFRKyVIDPSKTRVLAFLNISGIGLVGGNELQDLDDIDPDATAAAAEANPDFIVGIKVRAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 156 KTVVGENGIKPLELAKKIQTENNdLPLMVHIGSAPPELEEVLSRMERGDVLTHCFNGKPNGILDPkTDQIKNFVWDAYNN 235
Cdd:COG3964 160 KGVVGDNGIEPLKRAKEAAKEAG-LPLMVHIGNPPPPLDEVLDLLRPGDILTHCFNGKPNGILDE-DGKVRPSVREARKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 236 GVVFDIGHGTDSFNFHVAETALKAGMKATSISTDIYIRNrTNGPVFDLATTLEKLRVVGYSWEEIIEKVTAVPARNFHLK 315
Cdd:COG3964 238 GVLFDVGHGGASFSFKVAEPAIAQGFLPDTISTDLHTRN-MNGPVFDLATVMSKFLALGMPLEEVIAAVTWNPARAIGLP 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 488217097 316 NKGQLAVNYDADLTIFEIVENEKELKDSNGFTRIAKEQILPIKTIIGGVIYD 367
Cdd:COG3964 317 ELGTLSVGADADITIFDLREGPFGFTDSEGETLEGDRLLEPEATVRGGKVVY 368
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
2-365 |
7.69e-49 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 168.79 E-value: 7.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 2 FDTLIKNGRLVD---GSKI--EVAIEKGMIKAVAAEINQPAQEVVDLEGKYYLSaGWIDDHVH-CYEKMNLYYDyPDQIG 75
Cdd:PRK12394 3 NDILITNGHIIDparNINEinNLRIINDIIVDADKYPVASETRIIHADGCIVTP-GLIDYHAHvFYDGTEGGVR-PDMYM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 76 VEKGVTTVIDAGTTGAENIREFYqltKSV----KTNVYALMNISKWGIV--KQDELADLTKIQEDLVSTALAELPEFIVG 149
Cdd:PRK12394 81 PPNGVTTVVDAGSAGTANFDAFY---RTVicasKVRIKAFLTVSPPGQTwsGYQENYDPDNIDENKIHALFRQYRNVLQG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 150 IKARMSKTVVGENGIKPL----ELAKKIQTenndlPLMVHIGSAPPELEEVLSRMERGDVLTHCFNGKPNGILDPKtDQI 225
Cdd:PRK12394 158 LKLRVQTEDIAEYGLKPLtetlRIANDLRC-----PVAVHSTHPVLPMKELVSLLRRGDIIAHAFHGKGSTILTEE-GAV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 226 KNFVWDAYNNGVVFDIGHGTDSFNFHVAETALKAGMKATSISTDIYIRNRTNGPVFDLATTLEKLRVVGYSWEEIIEKVT 305
Cdd:PRK12394 232 LAEVRQARERGVIFDAANGRSHFDMNVARRAIANGFLPDIISSDLSTITKLAWPVYSLPWVLSKYLALGMALEDVINACT 311
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488217097 306 AVPARNFHLKNK-GQLAVNYDADLTIFEIVENEKELKDSNGFTRIAKEQILPIKTIIGGVI 365
Cdd:PRK12394 312 HTPAVLMGMAAEiGTLAPGAFADIAIFKLKNRHVEFADIHGETLTGTHVLVPQMTIKSGEI 372
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
5-368 |
5.21e-16 |
|
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: 78.98 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 5 LIKNGRLVDGSKIE---VAIEKGMIKAVAAEINQP-AQEVVDLEGKYyLSAGWIDDHVHCYEkmnlyydypdQIGVEK-- 78
Cdd:COG0044 1 LIKNGRVVDPGGLEradVLIEDGRIAAIGPDLAAPeAAEVIDATGLL-VLPGLIDLHVHLRE----------PGLEHKed 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 79 -----------GVTTVID-----AGTTGAENIREFYQLTKSVktnvyALMNISKWGIVKQDELADLTKIQEdlvstaLAE 142
Cdd:COG0044 70 ietgtraaaagGVTTVVDmpntnPVTDTPEALEFKLARAEEK-----ALVDVGPHGALTKGLGENLAELGA------LAE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 143 LPefIVGIKARMS----KTVVGENGIKP-LELAKKiqtenNDLPLMVH------IGSA----------------PPELEE 195
Cdd:COG0044 139 AG--AVAFKVFMGsddgNPVLDDGLLRRaLEYAAE-----FGALVAVHaedpdlIRGGvmnegktsprlglkgrPAEAEE 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 196 V-------LSRM-----------------------ERG-----DVLTH--CFN------GKPNGILDP----KTDQIKnf 228
Cdd:COG0044 212 EavardiaLAEEtgarlhivhvstaeavelireakARGlpvtaEVCPHhlTLTdedlerYGTNFKVNPplrtEEDREA-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 229 VWDAYNNGVVfD-IghGTDsfnfHVAETA-LKAgmkatsistdiyirnrtnGPVFD-----------LATTLEKLRVVGY 295
Cdd:COG0044 290 LWEGLADGTI-DvI--ATD----HAPHTLeEKE------------------LPFAEapngipgletaLPLLLTELVHKGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 296 -SWEEIIEKVTAVPARNFHLKNKGQLAVNYDADLTIFeivenekelkDSNGFTRIAKEQIL----------------PIK 358
Cdd:COG0044 345 lSLERLVELLSTNPARIFGLPRKGRIAVGADADLVLF----------DPDAEWTVTAEDLHskskntpfegreltgrVVA 414
|
490
....*....|.
gi 488217097 359 TIIGG-VIYDN 368
Cdd:COG0044 415 TIVRGrVVYED 425
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
3-368 |
4.56e-15 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 75.77 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 3 DTLIKNGRLVDGSK---IE---VAIEKGMIKAV--AAEINQPAQ-EVVDLEGKYyLSAGWIDDHVHcyekMNLYYDYPDQ 73
Cdd:COG1228 9 TLLITNATLVDGTGggvIEngtVLVEDGKIAAVgpAADLAVPAGaEVIDATGKT-VLPGLIDAHTH----LGLGGGRAVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 74 IGVEKGVTTVIDAGTTGAENIREF---------------YQLTKSVKTNVYALmnISKWGIVKQDELADLTK-IQEDLVS 137
Cdd:COG1228 84 FEAGGGITPTVDLVNPADKRLRRAlaagvttvrdlpggpLGLRDAIIAGESKL--LPGPRVLAAGPALSLTGgAHARGPE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 138 TALAELPEFIVG----IKARMSKtvvGENGIKPLELAKKIQTE-NNDLPLMVHIGSAppelEEVLSRMERG-DVLTHCFN 211
Cdd:COG1228 162 EARAALRELLAEgadyIKVFAEG---GAPDFSLEELRAILEAAhALGLPVAAHAHQA----DDIRLAVEAGvDSIEHGTY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 212 GKPNGIldpktDQIK--NFVW-----------DAYNNGVVFDIGHGTDSFNFHVAETALKAGMKaTSISTDIyirNRTNG 278
Cdd:COG1228 235 LDDEVA-----DLLAeaGTVVlvptlslflalLEGAAAPVAAKARKVREAALANARRLHDAGVP-VALGTDA---GVGVP 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 279 PVFDLATTLEKLRVVGYSWEEIIEKVTAVPARNFHLKNK-GQLAVNYDADLTIFeivenekelkDSNGFTRIAKEQiLPI 357
Cdd:COG1228 306 PGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLL----------DGDPLEDIAYLE-DVR 374
|
410
....*....|.
gi 488217097 358 KTIIGGVIYDN 368
Cdd:COG1228 375 AVMKDGRVVDR 385
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
1-84 |
9.25e-11 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 62.88 E-value: 9.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 1 MFDTLIKNGRLVDGS-----KIEVAIEKGMIKAVAAEINQPAQEVVDLEGKyYLSAGWIDDHVHcyekmnlyYDYP---D 72
Cdd:COG3653 1 MFDLLIRGGTVVDGTgappfRADVAIKGGRIVAVGDLAAAEAARVIDATGL-VVAPGFIDIHTH--------YDLQllwD 71
|
90
....*....|....*
gi 488217097 73 QIGVEK---GVTTVI 84
Cdd:COG3653 72 PRLEPSlrqGVTTVV 86
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
48-365 |
8.78e-10 |
|
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: 59.44 E-value: 8.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 48 YLSAGWIDDHVHCYEKMNLYYDYPDQ-------IGVEK----GVTTVIDAGTTGAENIREFYQLTKSVKTNVYALmnISK 116
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEfayealrLGITTmlksGTTTVLDMGATTSTGIEALLEAAEELPLGLRFL--GPG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 117 WGIVKQDELADLTKIQEDLVSTALAELPEFIVGIKARMSK---TVVGENGIKP-LELAKKIqtennDLPLMVHIGSAPPE 192
Cdd:pfam01979 79 CSLDTDGELEGRKALREKLKAGAEFIKGMADGVVFVGLAPhgaPTFSDDELKAaLEEAKKY-----GLPVAIHALETKGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 193 LEEVLSR-MERGDVLTHCFNGKPNGILDPKTDQIKNFVW-----------DAYNNGVV------FDIGHGTDSfnfhvAE 254
Cdd:pfam01979 154 VEDAIAAfGGGIEHGTHLEVAESGGLLDIIKLILAHGVHlspteanllaeHLKGAGVAhcpfsnSKLRSGRIA-----LR 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 255 TALKAGMKaTSISTDIYIRNRtNGPVFD---LATTLEKLRVVGYSWEEIIEKVTAVPARNFHL-KNKGQLAVNYDADLTI 330
Cdd:pfam01979 229 KALEDGVK-VGLGTDGAGSGN-SLNMLEelrLALELQFDPEGGLSPLEALRMATINPAKALGLdDKVGSIEVGKDADLVV 306
|
330 340 350
....*....|....*....|....*....|....*
gi 488217097 331 FEIVENEKELKDSNGFTriakeqilPIKTIIGGVI 365
Cdd:pfam01979 307 VDLDPLAAFFGLKPDGN--------VKKVIVKGKI 333
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
3-365 |
1.22e-09 |
|
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: 59.23 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 3 DTLIKNGRLVDGS-----KIEVAIEKGMIKAVAAEINQPAQEVVDLEGKyYLSAGWIDDHVHCYEKMNLYYDYPDQIGve 77
Cdd:cd01297 1 DLVIRNGTVVDGTgappfTADVGIRDGRIAAIGPILSTSAREVIDAAGL-VVAPGFIDVHTHYDGQVFWDPDLRPSSR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 78 KGVTTVIDaGTTGAENIREFYQLTKSVKTNV---YALMNISKWGIVKQDELADltkiqedlvstALAELPE-----FIVG 149
Cdd:cd01297 78 QGVTTVVL-GNCGVSPAPANPDDLARLIMLMeglVALGEGLPWGWATFAEYLD-----------ALEARPPavnvaALVG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 150 IKArMSKTVVGENGIKP--------LELAKK--------IQTENNDLPLMvhiGSAPPELEEVlsrmerGDVLTHCfngk 213
Cdd:cd01297 146 HAA-LRRAVMGLDAREAteeelakmRELLREaleagalgISTGLAYAPRL---YAGTAELVAL------ARVAARY---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 214 pNGILDPKTDQIKNFVWDAYNN----------GVVFDIGHGTDSFNFHVAETAL----KAGMKATSISTDIYirNRTNG- 278
Cdd:cd01297 212 -GGVYQTHVRYEGDSILEALDEllrlgretgrPVHISHLKSAGAPNWGKIDRLLalieAARAEGLQVTADVY--PYGAGs 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 279 -------------PVF-D-LATTLEKLRVVGY---------------SWEEIIEKVTAVPARNFHLKNKGQLAVNYDADL 328
Cdd:cd01297 289 eddvrrimahpvvMGGsDgGALGKPHPRSYGDftrvlghyvrerkllSLEEAVRKMTGLPARVFGLADRGRIAPGYRADI 368
|
410 420 430
....*....|....*....|....*....|....*...
gi 488217097 329 TIFeiveNEKELKDSNGFTRIAKEQIlPIK-TIIGGVI 365
Cdd:cd01297 369 VVF----DPDTLADRATFTRPNQPAE-GIEaVLVNGVP 401
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
2-112 |
6.59e-09 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 57.42 E-value: 6.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 2 FDTLIKNGRLVD---GSKIE--VAIEKGMIKAVAAEInQPAQEVVDLEGKyYLSAGWIDDHVHC---------YEKMNLy 67
Cdd:COG1001 5 ADLVIKNGRLVNvftGEILEgdIAIAGGRIAGVGDYI-GEATEVIDAAGR-YLVPGFIDGHVHIessmvtpaeFARAVL- 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 488217097 68 ydyPdqigveKGVTTVI-D----AGTTGAENIREFYQLTKSVKTNVYALM 112
Cdd:COG1001 82 ---P------HGTTTVIaDpheiANVLGLEGVRYMLEAAEGLPLDIFVML 122
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-59 |
4.22e-08 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 54.49 E-value: 4.22e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488217097 1 MFDTLIKNGRLVDGSKIEVA---IEKGMIKAVAAEI-NQPAQEVVDLEGKYYLSaGWIDDHVH 59
Cdd:PRK09236 1 MKRILIKNARIVNEGKIFEGdvlIENGRIAKIASSIsAKSADTVIDAAGRYLLP-GMIDDQVH 62
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-59 |
4.39e-08 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 54.71 E-value: 4.39e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488217097 1 MFDTLIKNGRLV--DGS-KIEVAIEKGMIKAVAAEINQPAQEVVDLEGKYYLSaGWIDDHVH 59
Cdd:PRK06189 2 MYDLIIRGGKVVtpEGVyRADIGIKNGKIAEIAPEISSPAREIIDADGLYVFP-GMIDVHVH 62
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
4-130 |
9.52e-08 |
|
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: 53.38 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 4 TLIKNGRLVDGSKI---EVAIEKGMIKAVAAEIN-QPAQEVVDLEGKYYLSAGwIDDHVHCY-EKMNLY----YDYPDQI 74
Cdd:cd01314 1 LIIKNGTIVTADGSfkaDILIEDGKIVAIGPNLEaPGGVEVIDATGKYVLPGG-IDPHTHLElPFMGTVtaddFESGTRA 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488217097 75 GVEKGVTTVID-----AGTTGAENIREFYQLTKSVKTNVYAL-MNISKWGIVKQDELADLTK 130
Cdd:cd01314 80 AAAGGTTTIIDfaipnKGQSLLEAVEKWRGKADGKSVIDYGFhMIITDWTDSVIEELPELVK 141
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
3-207 |
1.10e-07 |
|
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: 53.45 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 3 DTLIKNGRLVDGSKIE---VAIEKGMIKAVAAEI-NQPAQEVVDLEGKYyLSAGWIDDHVHCYEKmnlyyDYPDQIGVEK 78
Cdd:cd01315 1 DLVIKNGRVVTPDGVReadIAVKGGKIAAIGPDIaNTEAEEVIDAGGLV-VMPGLIDTHVHINEP-----GRTEWEGFET 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 79 --------GVTTVID------AGTTGAENIREFYQLTKSvKTNV-YALmniskWGIVKQDELADLTKIQEDLVstalael 143
Cdd:cd01315 75 gtkaaaagGITTIIDmplnsiPPTTTVENLEAKLEAAQG-KLHVdVGF-----WGGLVPGNLDQLRPLDEAGV------- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 144 pefiVGIKARMSKTVVGE----NGIKPLELAKKIQTEnnDLPLMVHIGSAPP--ELEEVLSRMERGDVLT 207
Cdd:cd01315 142 ----VGFKCFLCPSGVDEfpavDDEQLEEAMKELAKT--GSVLAVHAENPEIteALQEQAKAKGKRDYRD 205
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
4-59 |
1.54e-07 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 52.89 E-value: 1.54e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 4 TLIKNGRLVDGSKIE----VAIEKGMIKAVAAEINQPAQEVVDLEGKyYLSAGWIDDHVH 59
Cdd:PRK09357 3 ILIKNGRVIDPKGLDevadVLIDDGKIAAIGENIEAEGAEVIDATGL-VVAPGLVDLHVH 61
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-59 |
1.89e-07 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 52.71 E-value: 1.89e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 1 MFDTLIKNGRLVDGSK-IEVAIEKGMIKAVAAEINQPAQEVVDLEGkYYLSAGWIDDHVH 59
Cdd:PRK07572 1 MFDLIVRNANLPDGRTgIDIGIAGGRIAAVEPGLQAEAAEEIDAAG-RLVSPPFVDPHFH 59
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
2-59 |
9.11e-07 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 50.56 E-value: 9.11e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488217097 2 FDTLIKNGRLVDGS---KIEVAIEKGMIKAVAAeinQPAQEVVDLEGKYYLSAGwIDDHVH 59
Cdd:PRK08323 1 MSTLIKNGTVVTADdtyKADVLIEDGKIAAIGA---NLGDEVIDATGKYVMPGG-IDPHTH 57
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
1-367 |
9.85e-07 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 50.42 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 1 MFDTLIKNGRLVDGSKI---EVAIEKGMIKAVAAEIN-QPAQEVVDLEGKYYLSAGwIDDHVHCYEkmnlyydyPDQIGV 76
Cdd:PRK02382 1 MRDALLKDGRVYYNNSLqprDVRIDGGKITAVGKDLDgSSSEEVIDARGMLLLPGG-IDVHVHFRE--------PGYTHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 77 EK-----------GVTTVID-----AGTTGAENIREfyqltksvKTNVYALMNISKWGI--------VKQDEL------- 125
Cdd:PRK02382 72 ETwytgsrsaaagGVTTVVDqpntdPPTVDGESFDE--------KAELAARKSIVDFGInggvtgnwDPLESLwergvfa 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 126 ------ADLT---KIQEDLVSTALAELPEfiVGIKArmskTVVGENGIKPLELAKKIQTENN------------------ 178
Cdd:PRK02382 144 lgeifmADSTggmGIDEELFEEALAEAAR--LGVLA----TVHAEDEDLFDELAKLLKGDADadawsayrpaaaeaaave 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 179 -------DLPLMVHIG--SAPPELE---------EV------LSRMERGDVLTHcfnGKPNGILDPKTDqiKNFVWDAYN 234
Cdd:PRK02382 218 ralevasETGARIHIAhiSTPEGVDaarregitcEVtphhlfLSRRDWERLGTF---GKMNPPLRSEKR--REALWERLN 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 235 NGVVFDIghGTDsfnfHVAETALKagmKATSistdiyIRNRTNGpVFDLATT----LEKLRVVGYSWEEIIEKVTAVPAR 310
Cdd:PRK02382 293 DGTIDVV--ASD----HAPHTREE---KDAD------IWDAPSG-VPGVETMlpllLAAVRKNRLPLERVRDVTAANPAR 356
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488217097 311 NFHLKNKGQLAVNYDADLTIFEIVENEK----ELKDSNGFTRI-AKEQILPIKTII-GGVIYD 367
Cdd:PRK02382 357 IFGLDGKGRIAEGYDADLVLVDPDAAREirgdDLHSKAGWTPFeGMEGVFPELTMVrGTVVWD 419
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
54-310 |
1.53e-06 |
|
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: 49.25 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 54 IDDHVH----------------CYEKMNLYYDYPDQIGVEK-----GVTTVIDAGTTGAENIREfyQLTKSVKTNVYALM 112
Cdd:cd01292 2 IDTHVHldgsalrgtrlnlelkEAEELSPEDLYEDTLRALEallagGVTTVVDMGSTPPPTTTK--AAIEAVAEAARASA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 113 NISKWGIVK-QDELADLTKIQEDLVSTALAELPEF-IVGIKARMSKTVVG---ENGIKPLELAKKIqtennDLPLMVHIG 187
Cdd:cd01292 80 GIRVVLGLGiPGVPAAVDEDAEALLLELLRRGLELgAVGLKLAGPYTATGlsdESLRRVLEEARKL-----GLPVVIHAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 188 SAPPELEEV-----LSRMERGDVLTHCFNGKPNGILDPKTDQIKnFVWDAYNNGVVFDIGHGTDSFNfhvaeTALKAGMK 262
Cdd:cd01292 155 ELPDPTRALedlvaLLRLGGRVVIGHVSHLDPELLELLKEAGVS-LEVCPLSNYLLGRDGEGAEALR-----RLLELGIR 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488217097 263 ATsISTD-IYIRNRTNgpVFDLATTLEKLRVVGYSWEEIIEKVTAVPAR 310
Cdd:cd01292 229 VT-LGTDgPPHPLGTD--LLALLRLLLKVLRLGLSLEEALRLATINPAR 274
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
4-331 |
4.17e-06 |
|
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: 48.34 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 4 TLIKNGRLVDGSKIE---VAIEKGMIKAVAAEI-NQPAQEVVDLEGKYyLSAGWIDDHVH-------------CYEKMNL 66
Cdd:cd00854 1 LIIKNARILTPGGLEdgaVLVEDGKIVAIGPEDeLEEADEIIDLKGQY-LVPGFIDIHIHggggadfmdgtaeALKTIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 67 YYdypdqigVEKGVT----TVIdagTTGAENIRE-FYQLTKSVKTNVYALM----------NISKWGIvkQDEladltki 131
Cdd:cd00854 80 AL-------AKHGTTsflpTTV---TAPPEEIAKaLAAIAEAIAEGQGAEIlgihlegpfiSPEKKGA--HPP------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 132 qEDLVSTALAELPEFIvgikarmsktVVGENGIKPLELAKKIQTENNDLPLMVH------IGSAPPELEEVLSRMERG-D 204
Cdd:cd00854 141 -EYLRAPDPEELKKWL----------EAAGGLIKLVTLAPELDGALELIRYLVErgiivsIGHSDATYEQAVAAFEAGaT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 205 VLTHCFNG-------KPNGIldpktdqiknfvwdaynnGVVFDIGHGTDSF---NFHVAETALKAGMKATSIS-----TD 269
Cdd:cd00854 210 HVTHLFNAmsplhhrEPGVV------------------GAALSDDDVYAELiadGIHVHPAAVRLAYRAKGADkivlvTD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 270 ------------------IYIRNRTN--------GPVFDLATTLEKL-RVVGYSWEEIIEKVTAVPARNFHL-KNKGQLA 321
Cdd:cd00854 272 amaaaglpdgeyelggqtVTVKDGVArladgtlaGSTLTMDQAVRNMvKWGGCPLEEAVRMASLNPAKLLGLdDRKGSLK 351
|
410
....*....|
gi 488217097 322 VNYDADLTIF 331
Cdd:cd00854 352 PGKDADLVVL 361
|
|
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
4-332 |
7.62e-06 |
|
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: 47.38 E-value: 7.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 4 TLIKNGRLVDGS---KIEVAIEKGMIKAVAAEINQP---AQEVVDLEGKYyLSAGWIDDHVHCyekmnlyydypdqIG-- 75
Cdd:cd01308 2 TLIKNAEVYAPEylgKKDILIAGGKILAIEDQLNLPgyeNVTVVDLHGKI-LVPGFIDQHVHI-------------IGgg 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 76 -----------------VEKGVTTVIDA-GTTG----------------AENIREF-----YQ-----LTKSVKTNVYAL 111
Cdd:cd01308 68 geggpstrtpevtlsdlTTAGVTTVVGClGTDGisrsmedllakaraleEEGITCFvytgsYEvptrtITGSIRKDLLLI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 112 MNISKWGIV-------KQDELADLTKIQEDLVSTALaelpefiVGIKARMSKTVVGeNGIKPLELAKKIqTENNDLP--- 181
Cdd:cd01308 148 DKVIGVGEIaisdhrsSQPTVEELARIAAEARVGGL-------LGGKAGIVHIHLG-DGKRALSPIFEL-IEETEIPitq 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 182 -LMVHIGSAPPELEEVLSRMERGdvlthcfngkpnGILDPKTDQIKNFVWDAYNNgvvfdighgtdsfnfhvAETALKAG 260
Cdd:cd01308 219 fLPTHINRTAPLFEQGVEFAKMG------------GTIDLTSSIDPQFRKEGEVR-----------------PSEALKRL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 261 MKATSISTDIYIRNRTNG--PVFD------------LATTLEKLRVV----GYSWEEIIEKVTAVPARNFHLKNKGQLAV 322
Cdd:cd01308 270 LEQGVPLERITFSSDGNGslPKFDengnlvglgvgsVDTLLREVREAvkcgDIPLEVALRVITSNVARILKLRKKGEIQP 349
|
410
....*....|
gi 488217097 323 NYDADLTIFE 332
Cdd:cd01308 350 GFDADLVILD 359
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
52-344 |
1.33e-05 |
|
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: 46.62 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 52 GWIDDHVHCYEkMNLYYDYPDQI-----GVEKGVTTVIDAGTTGAENIREFYQLTKSVKTNVYALMNISKW-GIVKQDEL 125
Cdd:cd01302 6 GFIDIHVHLRD-PGGTTYKEDFEsgsraAAAGGVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFHaGIGPGDVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 126 ADLTK-IQEDLVS-------TALAELPEFIVGIKARMSKTV-VGENGIKPLELAKKIQTENNDLPLMVHIgSAPPELEEV 196
Cdd:cd01302 85 DELKKlFDAGINSlkvfmnyYFGELFDVDDGTLMRTFLEIAsRGGPVMVHAERAAQLAEEAGANVHIAHV-SSGEALELI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 197 LSRMERG-DV-----LTHCF-----------NGKPNGILDPKTDQIknFVWDAYNNGVVFDIGhgTDSfNFHVAETALKA 259
Cdd:cd01302 164 KFAKNKGvKVtcevcPHHLFldesmlrlngaWGKVNPPLRSKEDRE--ALWEGVKNGKIDTIA--SDH-APHSKEEKESG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 260 GMkatsistdiyIRNRTNG-PVFD--LATTLEKLRVVGYSWEEIIEKVTAVPARNFHLKNKGQLAVNYDADLTIFEiVEN 336
Cdd:cd01302 239 KD----------IWKAPPGfPGLEtrLPILLTEGVKRGLSLETLVEILSENPARIFGLYPKGTIAVGYDADLVIVD-PKK 307
|
....*...
gi 488217097 337 EKELKDSN 344
Cdd:cd01302 308 EWKVTAEE 315
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
234-365 |
1.66e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 46.37 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 234 NNGVVFDIGHGTDSFNFHVAEtALKAGMKaTSISTDIYIRNRTNGPVFDLATTLEK---LRVVG----YSWEEIIEKVTA 306
Cdd:pfam07969 333 GDWLQDRLGAERARGLTPVKE-LLNAGVK-VALGSDAPVGPFDPWPRIGAAVMRQTaggGEVLGpdeeLSLEEALALYTS 410
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488217097 307 VPARNFHL-KNKGQLAVNYDADLTIFEIvenekelkdsNGFTRIAKE--QILPIKTIIGGVI 365
Cdd:pfam07969 411 GPAKALGLeDRKGTLGVGKDADLVVLDD----------DPLTVDPPAiaDIRVRLTVVDGRV 462
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
296-363 |
3.46e-05 |
|
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: 45.40 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 296 SWEEIIEKVTAVPARNFHLKNKGQLAVNYDADLTIFeivenekelkDSNGFTRIAKEQIL----------------PIKT 359
Cdd:cd01318 288 SLSRVVRLTSHNPARIFGIKNKGRIAEGYDADLTVV----------DLKEERTIRAEEFHskagwtpfegfevtgfPVMT 357
|
....
gi 488217097 360 IIGG 363
Cdd:cd01318 358 IVRG 361
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
2-59 |
8.21e-05 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 44.30 E-value: 8.21e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488217097 2 FDTLIKNGRLV---DGSKIEVAIEKGMIKAVAAEINqPAQEVVDLEGKYYLSAGwIDDHVH 59
Cdd:PRK13404 4 FDLVIRGGTVVtatDTFQADIGIRGGRIAALGEGLG-PGAREIDATGRLVLPGG-VDSHCH 62
|
|
| TatD_DNase |
pfam01026 |
TatD related DNase; This family of proteins are related to a large superfamily of ... |
54-212 |
2.04e-04 |
|
TatD related DNase; This family of proteins are related to a large superfamily of metalloenzymes. TatD, a member of this family has been shown experimentally to be a DNase enzyme.
Pssm-ID: 425997 [Multi-domain] Cd Length: 253 Bit Score: 42.25 E-value: 2.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 54 IDDHVHCYEKmNLYYDYPDQI--GVEKGVTTVIDAGTTgAENIREFYQLTKSVKTNVYALmniskWGI----VKQDELAD 127
Cdd:pfam01026 1 IDTHCHLDFK-DFDEDRDEVIerAREAGVTGVVVVGTD-LEDFLRVLELAEKYPDRVYAA-----VGVhpheADEASEDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 128 LTKIQEdlvstaLAELPEfIVGIkarmsktvvGENG------------------IKPLELAKKiqtenNDLPLMVHIGSA 189
Cdd:pfam01026 74 LEALEK------LAEHPK-VVAI---------GEIGldyyyvdespkeaqeevfRRQLELAKE-----LGLPVVIHTRDA 132
|
170 180
....*....|....*....|....*
gi 488217097 190 PPELEEVLSRM--ERGDVLTHCFNG 212
Cdd:pfam01026 133 EEDLLEILKEAgaPGARGVLHCFTG 157
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-59 |
2.83e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 42.60 E-value: 2.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488217097 1 MFDTLIKNGRLV--DGS-KIEVAIEKGMIKAVAAEINQPAQEVVDLEGKYYLsAGWIDDHVH 59
Cdd:PRK09060 4 TFDLILKGGTVVnpDGEgRADIGIRDGRIAAIGDLSGASAGEVIDCRGLHVL-PGVIDSQVH 64
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
296-337 |
3.79e-04 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 42.21 E-value: 3.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 488217097 296 SWEEIIEKVTAVPARNFHLKNKGQLAVNYDADLTIF-----EIVENE 337
Cdd:PRK09060 345 SLERFVDLTSAGPARIFGIAGKGRIAVGYDADFTIVdlkrrETITNE 391
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
295-342 |
4.86e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 42.10 E-value: 4.86e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 488217097 295 YSWEEIIEKVTAVPARNFHLKNKGQLAVNYDADLTIFEIVENEKELKD 342
Cdd:COG1229 429 YSLYEIAIMTRAGPAKALGLADRGHLGVGADADIAIYDINPDDKDYED 476
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
3-141 |
8.07e-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: 41.16 E-value: 8.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 3 DTLIKNGRLVDGS---KIEVAIEKGMIKAVAAEINQ-------------PAQEVVDLEGKYYlSAGWIDDHVHcyekmnl 66
Cdd:cd00375 66 DLVITNALIIDYTgiyKADIGIKDGRIVAIGKAGNPdimdgvtpnmivgPSTEVIAGEGKIV-TAGGIDTHVH------- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 67 yYDYPDQI--GVEKGVTTVIDAGT------------TGAENIREFYQLTKSVKTNVYALmniSKWGIVKQDELADLT--- 129
Cdd:cd00375 138 -FICPQQIeeALASGITTMIGGGTgpaagtkattctPGPWNIKRMLQAADGLPVNIGFL---GKGNGSSPDALAEQIeag 213
|
170
....*....|....*.
gi 488217097 130 ----KIQEDLVSTALA 141
Cdd:cd00375 214 acglKLHEDWGATPAA 229
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
1-85 |
1.25e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 40.83 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 1 MFDTLIKNGRLVD-GSKIE----VAIEKGMIKAV-AAEINqpAQEVVDLEGKyYLSAGWIDDHVHCYEKMNlyydypDQI 74
Cdd:PRK09061 18 PYDLVIRNGRVVDpETGLDavrdVGIKGGKIAAVgTAAIE--GDRTIDATGL-VVAPGFIDLHAHGQSVAA------YRM 88
|
90
....*....|.
gi 488217097 75 GVEKGVTTVID 85
Cdd:PRK09061 89 QAFDGVTTALE 99
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
283-347 |
1.90e-03 |
|
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: 39.91 E-value: 1.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488217097 283 LATTLEKLRVVGY-SWEEIIEKVTAVPARNFHLkNKGQLAVNYDADLTIF----EIVENEKELKDSNGFT 347
Cdd:cd01317 292 LPLLWTLLVKGGLlTLPDLIRALSTNPAKILGL-PPGRLEVGAPADLVLFdpdaEWIVDEETFRSKSKNT 360
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
308-368 |
3.47e-03 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 39.27 E-value: 3.47e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488217097 308 PARNFHLKNKGQLAVNYDADLTI-----FEIVENEkELKDSNGFTRIAKEQIL--PIKTIIGG-VIYDN 368
Cdd:PRK07575 355 VARAYGIPNKGRIAPGYDADLVLvdlntYRPVRRE-ELLTKCGWSPFEGWNLTgwPVTTIVGGqIVFDR 422
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
5-59 |
4.78e-03 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 38.67 E-value: 4.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488217097 5 LIKNGRLVDGSKIEVA---IEKGMIKAVAAEINQPAQ-EVVDLEGKYYLSAGwIDDHVH 59
Cdd:PLN02942 8 LIKGGTVVNAHHQELAdvyVEDGIIVAVAPNLKVPDDvRVIDATGKFVMPGG-IDPHTH 65
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
296-332 |
5.93e-03 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 38.52 E-value: 5.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488217097 296 SWEEIIEKVTAVPARNF-----HLKNKGQLAVNYDADLTIFE 332
Cdd:PRK09061 417 SLLEAIRKCTLMPAQILedsvpAMRRKGRLQAGADADIVVFD 458
|
|
| |
