|
Name |
Accession |
Description |
Interval |
E-value |
| EF_0837 |
TIGR03583 |
probable amidohydrolase EF_0837/AHA_3915; Members of this family of relatively uncommon ... |
3-368 |
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: 647.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 3 YDLLIKNGQTVDGMPVEIAIKEKKIAAVAATISGSAKETIHLEPGTYVSAGWIDDHVHCFEKMALYYDYPDEIGVKKGVT 82
Cdd:TIGR03583 1 YDLLIKNGRTVNGTPVDIAIEDGKIAAVGTTITGSAKQTIDLEGETYVSAGWIDDHTHCFPKSALYYDEPDEIGVKTGVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 83 TVIDAGTTGAENIHEFYDLAQQAKTNVFGLVNISKWGIVAQDELADLSKVQASLVKKAIQELPDFVVGIKARMSRTVIGD 162
Cdd:TIGR03583 81 TVVDAGSTGADDIDDFYRLAQQAKTNVFALLNISRIGLVAQDELADLSNLDASAVKQAVERYPDFIVGLKARMSKSVVGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 163 NGITPLELAKQIQQENQEIPLMVHIGSAPPHLDEILALMEKGDVLTHCFNGKENGILDqATDKIKDFAWQAYNKGVVFDI 242
Cdd:TIGR03583 161 NGIEPLEIAKQIQQENLELPLMVHIGSAPPELDEILALMEKGDVLTHCFNGKPNGILR-ETGEVKPSVLEAYNRGVILDV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 243 GHGTDSFNFHVAETALREGMKAASISTDIYIRNRENGPVYDLATTMEKLRVVGYDWPEIIEKVTKAPAENFHLTQKGTLE 322
Cdd:TIGR03583 240 GHGTASFSFHVAEKAKRAGIFPDTISTDIYIRNRINGPVYSLATVMSKFLALGYSLEEVIEKVTKNAAEILKLTQKGRLQ 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1185284473 323 IGKDADLTIFTIQAEEKTLTDSNGLTRVAKEQIRPIKTIIGGQIYD 368
Cdd:TIGR03583 320 EGYDADLTIFTVKAEPKKLTDSEGDSRIAEEQIKPLAVIIGGEYYE 365
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
5-369 |
0e+00 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 522.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 5 LLIKNGQTVD-----GMPVEIAIKEKKIAAVAATISGS-AKETIHLEpGTYVSAGWIDDHVHCFEKMALYYDYPDEIGVK 78
Cdd:PRK09237 1 LLLRGGRVIDpangiDGVIDIAIEDGKIAAVAGDIDGSqAKKVIDLS-GLYVSPGWIDLHVHVYPGSTPYGDEPDEVGVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 79 KGVTTVIDAGTTGAENIHEFYDLAQQA-KTNVFGLVNISKWGIVAQDELADLSKVQASLVKKAIQELPDFVVGIKARMSR 157
Cdd:PRK09237 80 SGVTTVVDAGSAGADNFDDFRKLTIEAsKTRVLAFLNISRIGLLAQDELADLEDIDADAVAEAVKRNPDFIVGIKARMSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 158 TVIGDNGITPLELAKQIQQENqEIPLMVHIGSAPPHLDEILALMEKGDVLTHCFNGKENGILDQaTDKIKDFAWQAYNKG 237
Cdd:PRK09237 160 SVVGDNGIEPLELAKAIAAEA-NLPLMVHIGNPPPSLEEILELLRPGDILTHCFNGKPNRILDE-DGELRPSVLEALERG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 238 VVFDIGHGTDSFNFHVAETALREGMKAASISTDIYIRNRENGPVYDLATTMEKLRVVGYDWPEIIEKVTKAPAENFHLTQ 317
Cdd:PRK09237 238 VRLDVGHGTASFSFKVAEAAIAAGILPDTISTDIYCRNRINGPVYSLATVMSKFLALGMPLEEVIAAVTKNAADALRLPE 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1185284473 318 KGTLEIGKDADLTIFTIQAEEKTLTDSNGLTRVAKEQIRPIKTIIGGQIYDN 369
Cdd:PRK09237 318 LGRLQVGSDADLTLFTLKDGPFTLTDSEGDSLIGERLLTPLATVRGGKVVLT 369
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-368 |
3.68e-177 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 497.00 E-value: 3.68e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 4 DLLIKNGQTVDGM-----PVEIAIKEKKIAAVAATI-SGSAKETIHLEpGTYVSAGWIDDHVHCFEKMALYYDYPDEIGV 77
Cdd:COG3964 1 DLLIKGGRVIDPAngidgVMDIAIKDGKIAAVAKDIdAAEAKKVIDAS-GLYVTPGLIDLHTHVFPGGTDYGVDPDGVGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 78 KKGVTTVIDAGTTGAENIHEFYD-LAQQAKTNVFGLVNISKWGIVAQDELADLSKVQASLVKKAIQELPDFVVGIKARMS 156
Cdd:COG3964 80 RSGVTTVVDAGSAGAANFDGFRKyVIDPSKTRVLAFLNISGIGLVGGNELQDLDDIDPDATAAAAEANPDFIVGIKVRAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 157 RTVIGDNGITPLELAKQIQQENQeIPLMVHIGSAPPHLDEILALMEKGDVLTHCFNGKENGILDqATDKIKDFAWQAYNK 236
Cdd:COG3964 160 KGVVGDNGIEPLKRAKEAAKEAG-LPLMVHIGNPPPPLDEVLDLLRPGDILTHCFNGKPNGILD-EDGKVRPSVREARKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 237 GVVFDIGHGTDSFNFHVAETALREGMKAASISTDIYIRNrENGPVYDLATTMEKLRVVGYDWPEIIEKVTKAPAENFHLT 316
Cdd:COG3964 238 GVLFDVGHGGASFSFKVAEPAIAQGFLPDTISTDLHTRN-MNGPVFDLATVMSKFLALGMPLEEVIAAVTWNPARAIGLP 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1185284473 317 QKGTLEIGKDADLTIFTIQAEEKTLTDSNGLTRVAKEQIRPIKTIIGGQIYD 368
Cdd:COG3964 317 ELGTLSVGADADITIFDLREGPFGFTDSEGETLEGDRLLEPEATVRGGKVVY 368
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
19-357 |
4.42e-164 |
|
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: 462.18 E-value: 4.42e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 19 EIAIKEKKIAAVAATISGSAKETIHLEPGTYVSAGWIDDHVHCFEKMALYYDYPDEIGVKKGVTTVIDAGTTGAENIHEF 98
Cdd:cd01307 1 DVAIENGKIAAVGAALAAPAATQIVDAGGCYVSPGWIDLHVHVYQGGTRYGDRPDMIGVKSGVTTVVDAGSAGADNIDGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 99 -YDLAQQAKTNVFGLVNISKWGIVAQDELADLSKVQASLVKKAIQELPDFVVGIKARMSRTVIGDNGITPLELAKQIQQE 177
Cdd:cd01307 81 rYTVIERSATRVYAFLNISRVGLVAQDELPDPDNIDEDAVVAAAREYPDVIVGLKARASKSVVGEWGIKPLELAKKIAKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 178 NQeIPLMVHIGSAPPHLDEILALMEKGDVLTHCFNGKENGILDqATDKIKDFAWQAYNKGVVFDIGHGTDSFNFHVAETA 257
Cdd:cd01307 161 AD-LPLMVHIGSPPPILDEVVPLLRRGDVLTHCFNGKPNGIVD-EEGEVLPLVRRARERGVIFDVGHGTASFSFRVARAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 258 LREGMKAASISTDIYIRNRENGPVYDLATTMEKLRVVGYDWPEIIEKVTKAPAENFHLTQKGTLEIGKDADLTIFTIQAE 337
Cdd:cd01307 239 IAAGLLPDTISSDIHGRNRTNGPVYALATTLSKLLALGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDLKDG 318
|
330 340
....*....|....*....|
gi 1185284473 338 EKTLTDSNGLTRVAKEQIRP 357
Cdd:cd01307 319 RVELVDSEGDTLIAERLLVP 338
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
1-366 |
1.16e-51 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 176.10 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 1 MDYDLLIKNGQTVD-----GMPVEIAIKEKKIAAVAATISGSAKETIHLEpGTYVSAGWIDDHVHCFEKMALYYDYPDEI 75
Cdd:PRK12394 1 MKNDILITNGHIIDparniNEINNLRIINDIIVDADKYPVASETRIIHAD-GCIVTPGLIDYHAHVFYDGTEGGVRPDMY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 76 GVKKGVTTVIDAGTTGAENIHEFY-DLAQQAKTNVFGLVNISKWG-IVAQ-DELADLSKVQASLVKKAIQELPDFVVGIK 152
Cdd:PRK12394 80 MPPNGVTTVVDAGSAGTANFDAFYrTVICASKVRIKAFLTVSPPGqTWSGyQENYDPDNIDENKIHALFRQYRNVLQGLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 153 ARMSRTVIGDNGITPLELAKQIQQEnQEIPLMVHIGSAPPHLDEILALMEKGDVLTHCFNGKENGILDQaTDKIKDFAWQ 232
Cdd:PRK12394 160 LRVQTEDIAEYGLKPLTETLRIAND-LRCPVAVHSTHPVLPMKELVSLLRRGDIIAHAFHGKGSTILTE-EGAVLAEVRQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 233 AYNKGVVFDIGHGTDSFNFHVAETALREGMKAASISTDIYIRNRENGPVYDLATTMEKLRVVGYDWPEIIEKVTKAPAEN 312
Cdd:PRK12394 238 ARERGVIFDAANGRSHFDMNVARRAIANGFLPDIISSDLSTITKLAWPVYSLPWVLSKYLALGMALEDVINACTHTPAVL 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1185284473 313 FHLTQK-GTLEIGKDADLTIFTIQAEEKTLTDSNGLTRVAKEQIRPIKTIIGGQI 366
Cdd:PRK12394 318 MGMAAEiGTLAPGAFADIAIFKLKNRHVEFADIHGETLTGTHVLVPQMTIKSGEI 372
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
6-369 |
2.98e-11 |
|
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: 64.34 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 6 LIKNGQTVDG---MPVEIAIKEKKIAAVAATISG-SAKETIHLEpGTYVSAGWIDDHVHC----------FE---KMAly 68
Cdd:COG0044 1 LIKNGRVVDPgglERADVLIEDGRIAAIGPDLAApEAAEVIDAT-GLLVLPGLIDLHVHLrepglehkedIEtgtRAA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 69 ydypdeigVKKGVTTVID-----AGTTGAENIHEFYDLAQQAktnvfGLVNISKWGIVAQD---ELADLskvqASLVKKA 140
Cdd:COG0044 78 --------AAGGVTTVVDmpntnPVTDTPEALEFKLARAEEK-----ALVDVGPHGALTKGlgeNLAEL----GALAEAG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 141 iqelpdfVVGIKARMSRTviGDNGITPLELAKQIQQENQEIPLMV------------------------HIGSAPPH--- 193
Cdd:COG0044 141 -------AVAFKVFMGSD--DGNPVLDDGLLRRALEYAAEFGALVavhaedpdlirggvmnegktsprlGLKGRPAEaee 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 194 --LDEILALMEKGDVLTHCF------------NGKENGI----------LDQATDKIKDFawqaynkgvvfdighGTdsf 249
Cdd:COG0044 212 eaVARDIALAEETGARLHIVhvstaeavelirEAKARGLpvtaevcphhLTLTDEDLERY---------------GT--- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 250 NFHVA---------EtALREGMKAASI---STD----------IYIRNRENG--------PV-YDLATTMEKLrvvgyDW 298
Cdd:COG0044 274 NFKVNpplrteedrE-ALWEGLADGTIdviATDhaphtleekeLPFAEAPNGipgletalPLlLTELVHKGRL-----SL 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1185284473 299 PEIIEKVTKAPAENFHLTQKGTLEIGKDADLTIFTIQAeEKTLTDSNGLTRVA------KE-QIRPIKTIIGGQI-YDN 369
Cdd:COG0044 348 ERLVELLSTNPARIFGLPRKGRIAVGADADLVLFDPDA-EWTVTAEDLHSKSKntpfegRElTGRVVATIVRGRVvYED 425
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-369 |
5.44e-11 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 63.44 E-value: 5.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 4 DLLIKNGQTVDGM------PVEIAIKEKKIAAVAATISGSAK---ETIHLEpGTYVSAGWIDDHVHcfekMALYYDYPDE 74
Cdd:COG1228 9 TLLITNATLVDGTgggvieNGTVLVEDGKIAAVGPAADLAVPagaEVIDAT-GKTVLPGLIDAHTH----LGLGGGRAVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 75 IGVKKGVTTVIDAGTTGAENIHEF-------------YDLAQQAKTNVFGLVNISKWGIVAQDELADLSK---------V 132
Cdd:COG1228 84 FEAGGGITPTVDLVNPADKRLRRAlaagvttvrdlpgGPLGLRDAIIAGESKLLPGPRVLAAGPALSLTGgahargpeeA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 133 QAsLVKKAIQELPDFvvgIKARMSRtviGDNGITPLELAKQIQQE-NQEIPLMVHIGSApphlDEILALMEKG-DVLTHC 210
Cdd:COG1228 164 RA-ALRELLAEGADY---IKVFAEG---GAPDFSLEELRAILEAAhALGLPVAAHAHQA----DDIRLAVEAGvDSIEHG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 211 fngkeNGILDQATDKIKD-------------FAWQAYNKGVVFDIGHGTDSFNFHVAETALREGMKAAsISTDIyirNRE 277
Cdd:COG1228 233 -----TYLDDEVADLLAEagtvvlvptlslfLALLEGAAAPVAAKARKVREAALANARRLHDAGVPVA-LGTDA---GVG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 278 NGPVYDLATTMEKLRVVGYDWPEIIEKVTKAPAENFHLTQK-GTLEIGKDADLTIFtiqaeektltDSNGLTRVAKEQiR 356
Cdd:COG1228 304 VPPGRSLHRELALAVEAGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLL----------DGDPLEDIAYLE-D 372
|
410
....*....|...
gi 1185284473 357 PIKTIIGGQIYDN 369
Cdd:COG1228 373 VRAVMKDGRVVDR 385
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
4-332 |
8.75e-11 |
|
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of N-acyl-D-amino acids to produce the corresponding D-amino acids, which are used as intermediates in the synthesis of pesticides, bioactive peptides, and antibiotics.
Pssm-ID: 238622 [Multi-domain] Cd Length: 415 Bit Score: 62.70 E-value: 8.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 4 DLLIKNGQTVDG---MPVE--IAIKEKKIAAVAATISGSAKETIHLEpGTYVSAGWIDDHVHcfekmalyYDYPDEI--- 75
Cdd:cd01297 1 DLVIRNGTVVDGtgaPPFTadVGIRDGRIAAIGPILSTSAREVIDAA-GLVVAPGFIDVHTH--------YDGQVFWdpd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 76 ---GVKKGVTTVIDaGTTGAENIHEFYDLAQQAKTNVFGLVNISK---WGIVAQDELADlskvqaslvkkAIQELPD--- 146
Cdd:cd01297 72 lrpSSRQGVTTVVL-GNCGVSPAPANPDDLARLIMLMEGLVALGEglpWGWATFAEYLD-----------ALEARPPavn 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 147 --FVVGIKArMSRTVIGDNGI--TPLELAK---QIQQENQEIPLMVHIGSAPPHL-----DEILALmekGDVLthcfnGK 214
Cdd:cd01297 140 vaALVGHAA-LRRAVMGLDAReaTEEELAKmreLLREALEAGALGISTGLAYAPRlyagtAELVAL---ARVA-----AR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 215 ENGILDQATDKIKDFAWQAY----------NKGVVFDIGHGTDSFNFHVAETALREgMKAA-----SISTDIYirNRENG 279
Cdd:cd01297 211 YGGVYQTHVRYEGDSILEALdellrlgretGRPVHISHLKSAGAPNWGKIDRLLAL-IEAAraeglQVTADVY--PYGAG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 280 PVYDLATTMEK----------------LRVVGY------DW---------PEIIEKVTKAPAENFHLTQKGTLEIGKDAD 328
Cdd:cd01297 288 SEDDVRRIMAHpvvmggsdggalgkphPRSYGDftrvlgHYvrerkllslEEAVRKMTGLPARVFGLADRGRIAPGYRAD 367
|
....
gi 1185284473 329 LTIF 332
Cdd:cd01297 368 IVVF 371
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
49-366 |
2.53e-09 |
|
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: 57.90 E-value: 2.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 49 YVSAGWIDDHVHCFEKMALYYDYPDE-------IGVKK----GVTTVIDAGTTGAENIHefyDLAQQAKTNVFGLVNISK 117
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEfayealrLGITTmlksGTTTVLDMGATTSTGIE---ALLEAAEELPLGLRFLGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 118 WGIVAQDELADLSKvqasLVKKAIQELPDFVVGIKARMSRTVIGDNG--ITPLELAKQIQQENQEIPLMVHIgsappHLD 195
Cdd:pfam01979 78 GCSLDTDGELEGRK----ALREKLKAGAEFIKGMADGVVFVGLAPHGapTFSDDELKAALEEAKKYGLPVAI-----HAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 196 EILALME-----KGDVLTHCF---NGKENGILDQATDKIKDFAWqAYNKGVVFDIGHGTDSFNFHV--AETALREGMKAA 265
Cdd:pfam01979 149 ETKGEVEdaiaaFGGGIEHGThleVAESGGLLDIIKLILAHGVH-LSPTEANLLAEHLKGAGVAHCpfSNSKLRSGRIAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 266 ----------SISTDIYIRNRENGPVYDLATTMEKLRVVGYDWP--EIIEKVTKAPAENFHLT-QKGTLEIGKDADLTIF 332
Cdd:pfam01979 228 rkaledgvkvGLGTDGAGSGNSLNMLEELRLALELQFDPEGGLSplEALRMATINPAKALGLDdKVGSIEVGKDADLVVV 307
|
330 340 350
....*....|....*....|....*....|....
gi 1185284473 333 tiqaEEKTLTDSNGLTRVAKeqirPIKTIIGGQI 366
Cdd:pfam01979 308 ----DLDPLAAFFGLKPDGN----VKKVIVKGKI 333
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-115 |
2.98e-09 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 58.57 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 4 DLLIKNGQTVD---G--MPVEIAIKEKKIAAVAATIsGSAKETIHLEpGTYVSAGWIDDHVHC---------FEKMALyy 69
Cdd:COG1001 6 DLVIKNGRLVNvftGeiLEGDIAIAGGRIAGVGDYI-GEATEVIDAA-GRYLVPGFIDGHVHIessmvtpaeFARAVL-- 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1185284473 70 dypdeigvKKGVTTVIdagttgaENIHEFydlaqqakTNVFGLVNI 115
Cdd:COG1001 82 --------PHGTTTVI-------ADPHEI--------ANVLGLEGV 104
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
1-60 |
9.55e-09 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 56.63 E-value: 9.55e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1185284473 1 MDYDLLIKNGQTV--DGM-PVEIAIKEKKIAAVAATISGSAKETIHLEpGTYVSAGWIDDHVH 60
Cdd:PRK06189 1 MMYDLIIRGGKVVtpEGVyRADIGIKNGKIAEIAPEISSPAREIIDAD-GLYVFPGMIDVHVH 62
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
4-196 |
1.71e-08 |
|
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: 55.76 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 4 DLLIKNGQTV--DGM-PVEIAIKEKKIAAVAATIS-GSAKETIHLEpGTYVSAGWIDDHVHCFEkmalyydyPD------ 73
Cdd:cd01315 1 DLVIKNGRVVtpDGVrEADIAVKGGKIAAIGPDIAnTEAEEVIDAG-GLVVMPGLIDTHVHINE--------PGrteweg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 74 -EIGVKK----GVTTVID------AGTTGAENIHEFYDLAQQaKTNV-FGLvniskWGIVAQDELADLskvqASLVKKAi 141
Cdd:cd01315 72 fETGTKAaaagGITTIIDmplnsiPPTTTVENLEAKLEAAQG-KLHVdVGF-----WGGLVPGNLDQL----RPLDEAG- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1185284473 142 qelpdfVVGIKARMSRTVIGD----NGITPLELAKQIQQENQeiPLMVHIGSAPPHLDE 196
Cdd:cd01315 141 ------VVGFKCFLCPSGVDEfpavDDEQLEEAMKELAKTGS--VLAVHAENPEITEAL 191
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
287-366 |
1.05e-05 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.14 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 287 TMEKLRVVG----YDWPEIIEKVTKAPAENFHLTQ-KGTLEIGKDADLTIFtiqaeektltDSNGLTRVAKE--QIRPIK 359
Cdd:pfam07969 386 TAGGGEVLGpdeeLSLEEALALYTSGPAKALGLEDrKGTLGVGKDADLVVL----------DDDPLTVDPPAiaDIRVRL 455
|
....*..
gi 1185284473 360 TIIGGQI 366
Cdd:pfam07969 456 TVVDGRV 462
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
1-60 |
2.76e-05 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 45.68 E-value: 2.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1185284473 1 MDYDLLIKNGQTV--DG-MPVEIAIKEKKIAAVAATISGSAKETI-----HLEPGTyvsagwIDDHVH 60
Cdd:PRK09060 3 QTFDLILKGGTVVnpDGeGRADIGIRDGRIAAIGDLSGASAGEVIdcrglHVLPGV------IDSQVH 64
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
5-86 |
3.15e-05 |
|
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: 45.67 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 5 LLIKNGQTV---DGMPVEIAIKEKKIAAVAATISGSA-KETIHLEpGTYVSAGWIDDHVHC-FEKMALY----YDYPDEI 75
Cdd:cd01314 1 LIIKNGTIVtadGSFKADILIEDGKIVAIGPNLEAPGgVEVIDAT-GKYVLPGGIDPHTHLeLPFMGTVtaddFESGTRA 79
|
90
....*....|.
gi 1185284473 76 GVKKGVTTVID 86
Cdd:cd01314 80 AAAGGTTTIID 90
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
4-60 |
3.42e-05 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 45.40 E-value: 3.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1185284473 4 DLLIKNGQTVDG-MPVEIAIKEKKIAAVAATISGSAKETIHLEpGTYVSAGWIDDHVH 60
Cdd:PRK07572 3 DLIVRNANLPDGrTGIDIGIAGGRIAAVEPGLQAEAAEEIDAA-GRLVSPPFVDPHFH 59
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-86 |
4.12e-05 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 45.41 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 4 DLLIKNGQTVDG---MPVEIAIKEKKIAAVAATISGSAKETIHLEPGTYVSAGWIDDHVHcFEKMALYYDYPDEIGVKK- 79
Cdd:PRK02382 3 DALLKDGRVYYNnslQPRDVRIDGGKITAVGKDLDGSSSEEVIDARGMLLLPGGIDVHVH-FREPGYTHKETWYTGSRSa 81
|
90
....*....|
gi 1185284473 80 ---GVTTVID 86
Cdd:PRK02382 82 aagGVTTVVD 91
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
296-366 |
1.07e-04 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 43.94 E-value: 1.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1185284473 296 YDWPEIIEKVTKAPAENFHLTQKGTLEIGKDADLTIFTIQAEEKTLTDSNGLTRVAKeqiRPIKTIIGGQI 366
Cdd:cd01304 427 YSLYEIAIMTRAGPAKLLGLSDKGHLGVGADADIAIYDDDPDQVDPSDYEKVEKAFS---RAAYVLKDGEI 494
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
3-100 |
1.67e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 43.53 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 3 YDLLIKNGQTVD---GMPV--EIAIKEKKIAAVaATISGSAKETIHLEpGTYVSAGWIDDHVHCFEKMALYYDYPDeigv 77
Cdd:PRK09061 19 YDLVIRNGRVVDpetGLDAvrDVGIKGGKIAAV-GTAAIEGDRTIDAT-GLVVAPGFIDLHAHGQSVAAYRMQAFD---- 92
|
90 100
....*....|....*....|...
gi 1185284473 78 kkGVTTVIDAgTTGAENIHEFYD 100
Cdd:PRK09061 93 --GVTTALEL-EAGVLPVARWYA 112
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
80-210 |
1.94e-04 |
|
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: 42.71 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 80 GVTTVIDAGTTGAENIHEFYDLAQQAKTNVFGLVNISKWGIVAQDELADLSKVQASLVKKAIQELPDFVVGIKARMSRTV 159
Cdd:cd01292 48 GVTTVVDMGSTPPPTTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLKLAGPYTA 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1185284473 160 IGdngiTPLELAKQIQQENQE--IPLMVHIGSAPPHLDEILAL-----MEKGDVLTHC 210
Cdd:cd01292 128 TG----LSDESLRRVLEEARKlgLPVVIHAGELPDPTRALEDLvallrLGGRVVIGHV 181
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
301-364 |
2.32e-04 |
|
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: 42.71 E-value: 2.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1185284473 301 IIEKVTKAPAENFHLTQKGTLEIGKDADLTIFTIqAEEKTLTDSNGLTRVA-------KEQIRPIKTIIGG 364
Cdd:cd01318 292 VVRLTSHNPARIFGIKNKGRIAEGYDADLTVVDL-KEERTIRAEEFHSKAGwtpfegfEVTGFPVMTIVRG 361
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
3-60 |
1.62e-03 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 40.16 E-value: 1.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1185284473 3 YDLLIKNGQTV---DGMPVEIAIKEKKIAAVAAtisGSAKETIHLEpGTYVSAGWIDDHVH 60
Cdd:PRK08323 1 MSTLIKNGTVVtadDTYKADVLIEDGKIAAIGA---NLGDEVIDAT-GKYVMPGGIDPHTH 57
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
297-337 |
1.73e-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: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1185284473 297 DWPEIIEKVTKAPAENFHLTQkGTLEIGKDADLTIFTIQAE 337
Cdd:cd01317 306 TLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVLFDPDAE 345
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
5-60 |
2.24e-03 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 39.85 E-value: 2.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1185284473 5 LLIKN------GQTVDGmpvEIAIKEKKIAAVAATISG-SAKETIHLEpGTYVSAGWIDDHVH 60
Cdd:PRK09236 4 ILIKNarivneGKIFEG---DVLIENGRIAKIASSISAkSADTVIDAA-GRYLLPGMIDDQVH 62
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
5-332 |
3.30e-03 |
|
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: 39.10 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 5 LLIKNGQTVDG---MPVEIAIKEKKIAAVAATIS-GSAKETIHLEpGTYVSAGWIDDHVH-------------CFEKMAL 67
Cdd:cd00854 1 LIIKNARILTPgglEDGAVLVEDGKIVAIGPEDElEEADEIIDLK-GQYLVPGFIDIHIHggggadfmdgtaeALKTIAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 68 YYdypdeigVKKGVT----TVIdagTTGAENIHEFYDLAQQAK-----TNVFGL------VNISKWGivAQDEladlskv 132
Cdd:cd00854 80 AL-------AKHGTTsflpTTV---TAPPEEIAKALAAIAEAIaegqgAEILGIhlegpfISPEKKG--AHPP------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 133 qASLVKKAIQELPDFVvgikarmsrtVIGDNGITPLELAKQIQQENQEIPLMVH------IGsappHLDEILALMEKG-- 204
Cdd:cd00854 141 -EYLRAPDPEELKKWL----------EAAGGLIKLVTLAPELDGALELIRYLVErgiivsIG----HSDATYEQAVAAfe 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 205 ---DVLTHCFNG------KENGILDQATDKIKDFAwqaynkGVVFDiGHgtdsfnfHVAETALREGMKAASIS-----TD 270
Cdd:cd00854 206 agaTHVTHLFNAmsplhhREPGVVGAALSDDDVYA------ELIAD-GI-------HVHPAAVRLAYRAKGADkivlvTD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 271 ------------------IYIRNR----ENGpvyDLA---TTMEK-----LRVVGYDWPEIIEKVTKAPAENFHLT-QKG 319
Cdd:cd00854 272 amaaaglpdgeyelggqtVTVKDGvarlADG---TLAgstLTMDQavrnmVKWGGCPLEEAVRMASLNPAKLLGLDdRKG 348
|
410
....*....|...
gi 1185284473 320 TLEIGKDADLTIF 332
Cdd:cd00854 349 SLKPGKDADLVVL 361
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
302-357 |
3.49e-03 |
|
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: 38.91 E-value: 3.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1185284473 302 IEKVTKAPAENFHLTQKGTLEIGKDADLTIFtiqaeektltDSNGLTRVAKEQIRP 357
Cdd:cd01302 273 VEILSENPARIFGLYPKGTIAVGYDADLVIV----------DPKKEWKVTAEEIES 318
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
312-366 |
7.76e-03 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 38.24 E-value: 7.76e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1185284473 312 NFHLTQKGTLEIGKDADLTIFtiqaeektltDSNgLTRVAKEQIRPIK---TIIGGQI 366
Cdd:COG1574 484 AFEEDEKGSLEPGKLADFVVL----------DRD-PLTVPPEEIKDIKvllTVVGGRV 530
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
284-337 |
8.10e-03 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 37.87 E-value: 8.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1185284473 284 LATTMEKLRVVGY-DWPEIIEKVTKAPAENFHLTQkGTLEIGKDADLTIFTIQAE 337
Cdd:PRK09357 331 LSLLYTTLVKTGLlDLEQLLEKMTINPARILGLPA-GPLAEGEPADLVIFDPEAE 384
|
|
| Urease_alpha |
cd00375 |
Urease alpha-subunit; Urease is a nickel-dependent metalloenzyme that catalyzes the hydrolysis ... |
4-93 |
9.26e-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: 38.08 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185284473 4 DLLIKNGQTVD--GM-PVEIAIKEKKIAAV-------------AATISGSAKETIHLEpGTYVSAGWIDDHVH--CFEKM 65
Cdd:cd00375 66 DLVITNALIIDytGIyKADIGIKDGRIVAIgkagnpdimdgvtPNMIVGPSTEVIAGE-GKIVTAGGIDTHVHfiCPQQI 144
|
90 100
....*....|....*....|....*...
gi 1185284473 66 alyydypdEIGVKKGVTTVIDAGTTGAE 93
Cdd:cd00375 145 --------EEALASGITTMIGGGTGPAA 164
|
|
| |
