|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-404 |
1.03e-161 |
|
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: 459.03 E-value: 1.03e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 35 LIVREGHICDIVPETQLPVSG---DNIHDMQGRLVTPGLIDCHTHLVFAGNRAAEWEQRLNGASYQHISAQGGGINATVS 111
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGpaaAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 112 ATRACAEETLYQLARERMMRLASEGVTLLEIKSGYGLELATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYRDDPDg 191
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGREE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 192 YITLVCETMIPQLWKKGLFDAVDLFCESVGFNVAQSERVLQTAKALGIPVKGHVEQLSLLGGAQLVSRYQGLSADHIEYL 271
Cdd:cd01296 160 YIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 272 DEAGVAAMRDGGTVGVLLPGAFYFLRETQhPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMACVQFGLTPEEAWAG 351
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLRETY-PPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 447172232 352 VTRHAARALGRQATHGQLRAGYRADFVVWDAEQPVEIVYEPGRNPLYQRVYRG 404
Cdd:cd01296 319 ATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
30-406 |
3.18e-160 |
|
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273512 [Multi-domain] Cd Length: 377 Bit Score: 455.72 E-value: 3.18e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 30 VDNQALIVREGHICDIVPETQLP-VSGDNIHDMQGRLVTPGLIDCHTHLVFAGNRAAEWEQRLNGASYQHISAQGGGINA 108
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPgEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 109 TVSATRACAEETLYQLARERMMRLASEGVTLLEIKSGYGLELATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYRDD 188
Cdd:TIGR01224 81 TVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 189 PDGYITLVCETMIPQLWKKGLFDAVDLFCESVGFNVAQSERVLQTAKALGIPVKGHVEQLSLLGGAQLVSRYQGLSADHI 268
Cdd:TIGR01224 161 PDDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 269 EYLDEAGVAAMRDGGTVGVLLPGAFYFLREtQHPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMACVQFGLTPEEA 348
Cdd:TIGR01224 241 EHASDAGIKALAEAGTVAVLLPGTTFYLRE-TYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 447172232 349 WAGVTRHAARALGRQATHGQLRAGYRADFVVWDAEQPVEIVYEPGRNPLYQRVYRGKI 406
Cdd:TIGR01224 320 LHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGNI 377
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
6-406 |
2.20e-85 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 265.29 E-value: 2.20e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 6 PGDTVWRNIRLATMDPQrqapyGLVDNQALIVREGHICDIVPETQLPV-SGDNIHDMQGRLVTPGLIDCHTHLVFAGNRA 84
Cdd:COG1228 7 AGTLLITNATLVDGTGG-----GVIENGTVLVEDGKIAAVGPAADLAVpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 85 AEWEQrlngasyqhisaqGGGINATVsatracaeeTLYQLARERMMRLASEGVTLLEIKSGYGLEL-----ATEEKLLRV 159
Cdd:COG1228 82 VEFEA-------------GGGITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLPG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 160 AAKLAAENAIDISptlLAAHA-TPAEyrddpdgyitlvCETMIPQLWKKGlFDAVDLFCE--SVGFNVAQSERVLQTAKA 236
Cdd:COG1228 140 PRVLAAGPALSLT---GGAHArGPEE------------ARAALRELLAEG-ADYIKVFAEggAPDFSLEELRAILEAAHA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 237 LGIPVKGHVEQLSllgGAQLVSRYQGLSADHIEYLDEAGVAAMRDGGTVgVLLPGAFYFL-----------------RET 299
Cdd:COG1228 204 LGLPVAAHAHQAD---DIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvREA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 300 QHPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMAcVQFGLTPEEAWAGVTRHAARALGRQATHGQLRAGYRADFVV 379
Cdd:COG1228 280 ALANARRLHDAGVPVALGTDAGVGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVL 358
|
410 420
....*....|....*....|....*..
gi 447172232 380 WDAEQPVEIVYepgRNPLYQRVYRGKI 406
Cdd:COG1228 359 LDGDPLEDIAY---LEDVRAVMKDGRV 382
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
8-404 |
4.82e-25 |
|
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and metabolism, General function prediction only]; Cytosine/adenosine deaminase or related metal-dependent hydrolase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440171 [Multi-domain] Cd Length: 416 Bit Score: 105.68 E-value: 4.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 8 DTVWRNIRLATMDPQRqapyGLVDNQALIVREGHICDIVPETQLPVS--GDNIHDMQGRLVTPGLIDCHTHLVFAGNRAA 85
Cdd:COG0402 1 DLLIRGAWVLTMDPAG----GVLEDGAVLVEDGRIAAVGPGAELPARypAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 86 -------EWEQRLNGASYQHISAQGgginATVSATRACAEetlyqlarermmrLASEGVT-LLEIksgYGLELATEEKLL 157
Cdd:COG0402 77 addlpllDWLEEYIWPLEARLDPED----VYAGALLALAE-------------MLRSGTTtVADF---YYVHPESADALA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 158 RVAAKL---AAenaidISPTLLAAHAtPAEYRDDPDGYITLvCETMIPQlWKKGLFDAVDL-----FCESVgfNVAQSER 229
Cdd:COG0402 137 EAAAEAgirAV-----LGRGLMDRGF-PDGLREDADEGLAD-SERLIER-WHGAADGRIRValaphAPYTV--SPELLRA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 230 VLQTAKALGIPVKGHV-EQLSLLggAQLVSRYqGLSAdhIEYLDEAGV------------------AAMRDGGTVGVLLP 290
Cdd:COG0402 207 AAALARELGLPLHTHLaETRDEV--EWVLELY-GKRP--VEYLDELGLlgprtllahcvhltdeeiALLAETGASVAHCP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 291 GAFYFLRETqHPPVELLRRYQVPVAVASD---FNPGTSPFCSLHLAMNMACVQFG----LTPEEAWAGVTRHAARALGRQ 363
Cdd:COG0402 282 TSNLKLGSG-IAPVPRLLAAGVRVGLGTDgaaSNNSLDMFEEMRLAALLQRLRGGdptaLSAREALEMATLGGARALGLD 360
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 447172232 364 ATHGQLRAGYRADFVVWDAEQPveiVYEPGRNPLYQRVYRG 404
Cdd:COG0402 361 DEIGSLEPGKRADLVVLDLDAP---HLAPLHDPLSALVYAA 398
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-406 |
8.37e-21 |
|
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) catalyze the deamination of cytosine, producing uracil and ammonia. They play an important role in pyrimidine salvage. CDs are present in prokaryotes and fungi, but not mammalian cells. The bacterial enzymes, but not the fungal enzymes, are related to the adenosine deaminases (ADA). The bacterial enzymes are iron dependent and hexameric.
Pssm-ID: 238618 [Multi-domain] Cd Length: 398 Bit Score: 93.47 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 12 RNIRLATMDPqrqapyGLVDnqaLIVREGHICDIVPetQLPVSGDNIH-DMQGRLVTPGLIDCHTHL--VFAGNRaaewe 88
Cdd:cd01293 3 RNARLADGGT------ALVD---IAIEDGRIAAIGP--ALAVPPDAEEvDAKGRLVLPAFVDPHIHLdkTFTGGR----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 89 qrlngASYQHISAQGGGINATVSATRACAEETLYQLARERMMRLASEGVT-------------------LLEIKSGY--- 146
Cdd:cd01293 67 -----WPNNSGGTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTairthvdvdpaaglkaleaLLELREEWadl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 147 -----------GLELATE-EKLLRVAAKLAAEN--AIDisptllaahatPAEYRDDPDGYITLVCEtmipqLWKKglFDA 212
Cdd:cd01293 142 idlqivafpqhGLLSTPGgEELMREALKMGADVvgGIP-----------PAEIDEDGEESLDTLFE-----LAQE--HGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 213 -VDLFC-ESVGFNVAQSERVLQTAKALGIPVK---GHVEQLSLLGGAQLvsryqglsADHIEYLDEAGVAAMRDGGTVGV 287
Cdd:cd01293 204 dIDLHLdETDDPGSRTLEELAEEAERRGMQGRvtcSHATALGSLPEAEV--------SRLADLLAEAGISVVSLPPINLY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 288 LLPGAFYFLRETQHPPVELLRRYQVPVAVASD-----FNP-GT-SPFCSLHLAMNMAcvqfGLTPEE----AWAGVTRHA 356
Cdd:cd01293 276 LQGREDTTPKRRGVTPVKELRAAGVNVALGSDnvrdpWYPfGSgDMLEVANLAAHIA----QLGTPEdlalALDLITGNA 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 447172232 357 ARALGrqATHGQLRAGYRADFVVWDAEQPVEIVYEpgRNPLYQRVYRGKI 406
Cdd:cd01293 352 ARALG--LEDYGIKVGCPADLVLLDAEDVAEAVAR--QPPRRVVIRKGRV 397
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
70-359 |
4.68e-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: 71.98 E-value: 4.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 70 LIDCHTHLVFAGNRAAEWEQRLNGASYQhisaqggginatvsatracAEETLYQLARERMMRLASEGVTLLEIKSGYGLE 149
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEEL-------------------SPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 150 LATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYRDDPDgyitLVCETMIPQlwKKGLFDAVDLF--CESVGFNVAQS 227
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEA----LLLELLRRG--LELGAVGLKLAgpYTATGLSDESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 228 ERVLQTAKALGIPVKGHVEQLSLLGGA--QLVSRY---QGLSADHIEYLDEAGVAAMRDGG-TVGVLLPGAFYFLRETQH 301
Cdd:cd01292 136 RRVLEEARKLGLPVVIHAGELPDPTRAleDLVALLrlgGRVVIGHVSHLDPELLELLKEAGvSLEVCPLSNYLLGRDGEG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 302 -PPVELLRRYQVPVAVASDFNPGTSPFCSLH-LAMNMACVQFGLTPEEAWAGVTRHAARA 359
Cdd:cd01292 216 aEALRRLLELGIRVTLGTDGPPHPLGTDLLAlLRLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-394 |
1.57e-11 |
|
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: 65.03 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 39 EGHICDIVPETQLPVSGDNIhDMQGRLVTPGLIDCHTHL-------VFAGNRAAEweqrLNGASYQHISAqGGGINATvs 111
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVI-DAKGKHVTPGLIDAHSHLgldeeggVRETSDANE----ETDPVTPHVRA-IDGINPD-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 112 atracaeETLYQLARermmrlaSEGVTLLEI-------KSGYGLELAT-----EEKLLR--VAAKLA-AENA------ID 170
Cdd:cd01309 73 -------DEAFKRAR-------AGGVTTVQVlpgsanlIGGQGVVIKTdggtiEDMFIKapAGLKMAlGENPkrvyggKG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 171 ISPTllAAHATPAEYRD---DPDGYItlvcETMIPQLWKKGLFDAVDLFCESVGfNVAQSErvlqtakalgIPVKGHVEQ 247
Cdd:cd01309 139 KEPA--TRMGVAALLRDafiKAQEYG----RKYDLGKNAKKDPPERDLKLEALL-PVLKGE----------IPVRIHAHR 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 248 LSllggaqlvsryQGLSAdhIEYLDEAGVAAMRDGGTVGVLLP----------------GAFYFLRETQHP---PVELLR 308
Cdd:cd01309 202 AD-----------DILTA--IRIAKEFGIKITIEHGAEGYKLAdelakhgipviygptlTLPKKVEEVNDAidtNAYLLK 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 309 RYQVPVAVASDFNPGTSPFCSLHLAMnmaCVQFGLTPEEAWAGVTRHAARALGRQATHGQLRAGYRADFVVWDAEqP--- 385
Cdd:cd01309 269 KGGVAFAISSDHPVLNIRNLNLEAAK---AVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGD-Plep 344
|
410
....*....|..
gi 447172232 386 ---VEIVYEPGR 394
Cdd:cd01309 345 tskPEQVYIDGR 356
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
60-382 |
1.34e-10 |
|
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: 62.31 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 60 DMQGRLVTPGLIDCHTHLVFAGNRAAEWEQRLNgasyqhisaqggginatvsatracAEETLYQLARERMMRLAseGVTL 139
Cdd:cd01299 5 DLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPV------------------------EYRTIRATRQARAALRA--GFTT 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 140 LeiksgygLELATEEkllRVAAKLAAENAIDISPTLLAA---------HATPAEYRDD-PDGYITLVCETM------IPQ 203
Cdd:cd01299 59 V-------RDAGGAD---YGLLRDAIDAGLIPGPRVFASgralsqtggHGDPRGLSGLfPAGGLAAVVDGVeevraaVRE 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 204 LWKKGLfDAVDLFC-----------ESVGFNVAQSERVLQTAKALGIPVKGHVEqlsllgGAQLVSRYQGLSADHIE--- 269
Cdd:cd01299 129 QLRRGA-DQIKIMAtggvlspgdppPDTQFSEEELRAIVDEAHKAGLYVAAHAY------GAEAIRRAIRAGVDTIEhgf 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 270 YLDEAGVAAMRDGGTVGVLLPGAFYFLRETQHPP--------------------VELLRRYQVPVAVASDFNPGTSPFCS 329
Cdd:cd01299 202 LIDDETIELMKEKGIFLVPTLATYEALAAEGAAPglpadsaekvalvleagrdaLRRAHKAGVKIAFGTDAGFPVPPHGW 281
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 447172232 330 LHLAMNMAcVQFGLTPEEAWAGVTRHAARALGRQATHGQLRAGYRADFVVWDA 382
Cdd:cd01299 282 NARELELL-VKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDG 333
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
65-398 |
1.03e-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: 59.44 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 65 LVTPGLIDCHTHLVFAGNRAAeweqRLNGASYQHISAQG------GGInATVSATRACAEEtlyqlARERMMRLASEgvt 138
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGI----PVPPEFAYEALRLGittmlkSGT-TTVLDMGATTST-----GIEALLEAAEE--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 139 lleIKSGYGLELAteekllrvaaklaaenaiDISPTLLAAHATPAEYRDDPDGYITLVCETMipqlwKKGLFDAVDLFcE 218
Cdd:pfam01979 68 ---LPLGLRFLGP------------------GCSLDTDGELEGRKALREKLKAGAEFIKGMA-----DGVVFVGLAPH-G 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 219 SVGFNVAQSERVLQTAKALGIPVKGHVeqLSLLGGAQLVSRYQGLSADHIEYLDEAGVAAMRDGGTV----GVLLPGAFY 294
Cdd:pfam01979 121 APTFSDDELKAALEEAKKYGLPVAIHA--LETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLilahGVHLSPTEA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 295 -------------------FLRETQHPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMACVQF----GLTPEEAWAG 351
Cdd:pfam01979 199 nllaehlkgagvahcpfsnSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFdpegGLSPLEALRM 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 447172232 352 VTRHAARALGRQATHGQLRAGYRADFVVWDAEQPVEIVY-EPGRNPLY 398
Cdd:pfam01979 279 ATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGlKPDGNVKK 326
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
6-120 |
3.09e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 58.66 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 6 PGDTVWRNIRLATMDPQRQAPyglvdnQALIVREGHICDIVPETQLP---VSGDNIHDMQGRLVTPGLIDCHTHLVFAGN 82
Cdd:COG1574 7 AADLLLTNGRIYTMDPAQPVA------EAVAVRDGRIVAVGSDAEVRalaGPATEVIDLGGKTVLPGFIDAHVHLLGGGL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 447172232 83 RAAEWeqRLNGASyqhisaqggGINATVSATRACAEET 120
Cdd:COG1574 81 ALLGV--DLSGAR---------SLDELLARLRAAAAEL 107
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
12-385 |
1.42e-08 |
|
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. Atrazine, a chlorinated herbizide, can be catabolized by a variety of different bacteria. The first three steps of the atrazine dehalogenation pathway are catalyzed by atrazine chlorohydrolase (AtzA), hydroxyatrazine ethylaminohydrolase (AtzB), and N-isopropylammelide N-isopropylaminohydrolase (AtzC). All three enzymes belong to the superfamily of metal dependent hydrolases. AtzA and AtzB, beside other related enzymes are represented in this CD.
Pssm-ID: 238623 [Multi-domain] Cd Length: 411 Bit Score: 56.44 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 12 RNIRLATMDPQRqapygLVDNQALIVREGHICDIVPETQLPV-SGDNIHDMQGRLVTPGLIDCHTHL-------VFAGNR 83
Cdd:cd01298 4 RNGTIVTTDPRR-----VLEDGDVLVEDGRIVAVGPALPLPAyPADEVIDAKGKVVMPGLVNTHTHLamtllrgLADDLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 84 AAEW--------EQRLNGASyQHISAQGGGINATVSATRACAE------ETLYQLARERMMR-LASEGVtlleiksgygL 148
Cdd:cd01298 79 LMEWlkdliwplERLLTEED-VYLGALLALAEMIRSGTTTFADmyffypDAVAEAAEELGIRaVLGRGI----------M 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 149 ELATEEKLLRVAAKLAAENAIDisptllaahatpaEYRDDPDGYITLVcetMIPqlwkkglfdavdlfCESVGFNVAQSE 228
Cdd:cd01298 148 DLGTEDVEETEEALAEAERLIR-------------EWHGAADGRIRVA---LAP--------------HAPYTCSDELLR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 229 RVLQTAKALGIPVKGHV----------------------EQLSLLGG----AQLVsryqGLSADHIEYLDEAGVAA---- 278
Cdd:cd01298 198 EVAELAREYGVPLHIHLaetedeveeslekygkrpveylEELGLLGPdvvlAHCV----WLTDEEIELLAETGTGVahnp 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 279 ---MRDGgtVGVllpgafyflretqhPPVELLRRYQVPVAVASD---FNPGTSPFCSLHLAMNMACVQFG----LTPEEA 348
Cdd:cd01298 274 asnMKLA--SGI--------------APVPEMLEAGVNVGLGTDgaaSNNNLDMFEEMRLAALLQKLAHGdptaLPAEEA 337
|
410 420 430
....*....|....*....|....*....|....*..
gi 447172232 349 WAGVTRHAARALGRQAThGQLRAGYRADFVVWDAEQP 385
Cdd:cd01298 338 LEMATIGGAKALGLDEI-GSLEVGKKADLILIDLDGP 373
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
8-404 |
1.67e-08 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 56.09 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 8 DTVWRNIRLATMDPqrqapyglVDnqaLIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHL--VFAG---- 81
Cdd:PRK05985 3 DLLFRNVRPAGGAA--------VD---ILIRDGRIAAIGPALAAP-PGAEVEDGGGALALPGLVDGHIHLdkTFWGdpwy 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 82 --NRAAEWEQRL-NGASYQHISAQGGGINATVSATRACAEETL-----------YQLAR-ERMMRLASEGVTLLEI---- 142
Cdd:PRK05985 71 pnEPGPSLRERIaNERRRRAASGHPAAERALALARAAAAAGTTamrshvdvdpdAGLRHlEAVLAARETLRGLIDIqiva 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 143 --KSGYGLELATEEkLLRVAAKLAAEN--AIDisptllaahatPAEYRDDPDGYITLVCEtmIPQLWKKG----LFDAVD 214
Cdd:PRK05985 151 fpQSGVLSRPGTAE-LLDAALRAGADVvgGLD-----------PAGIDGDPEGQLDIVFG--LAERHGVGidihLHEPGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 215 LfcesvgfNVAQSERVLQTAKALGIPVKGHVEQLSLLGGAQLVSRyqglsADHIEYLDEAGVAAMRDGgtvgvllPGAFY 294
Cdd:PRK05985 217 L-------GAFQLERIAARTRALGMQGRVAVSHAFCLGDLPEREV-----DRLAERLAEAGVAIMTNA-------PGSVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 295 FlretqhPPVELLRRYQVPVAVASD-FNPGTSPFCS---LHLAMnMACVQFGL-TPEE---AWAGVTRHAARALGRQAtH 366
Cdd:PRK05985 278 V------PPVAALRAAGVTVFGGNDgIRDTWWPYGNgdmLERAM-LIGYRSGFrTDDElaaALDCVTHGGARALGLED-Y 349
|
410 420 430
....*....|....*....|....*....|....*...
gi 447172232 367 GqLRAGYRADFVVWDAEQPVEIVYEPgrnPLYQRVYRG 404
Cdd:PRK05985 350 G-LAVGARADFVLVDAETVAEAVVAV---PVRRLVVRG 383
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
26-390 |
2.70e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 55.11 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 26 PYGLVDNQALIVREGHICDIVPETQLpvsGDNIHDMQGRLVTPGLIDCHTHlvfagnraaeweqrlnGasyqhisaqGGG 105
Cdd:COG1820 10 GDGVLEDGALLIEDGRIAAIGPGAEP---DAEVIDLGGGYLAPGFIDLHVH----------------G---------GGG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 106 INATvsatrACAEETLYQLARErmmrLASEGVTLLeiksgygleLAT-----EEKLLRVAAKLAAENAIDISPTLLAAH- 179
Cdd:COG1820 62 VDFM-----DGTPEALRTIARA----HARHGTTSF---------LPTtitapPEDLLRALAAIAEAIEQGGGAGILGIHl 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 180 -----------ATPAEYRDDPD------------GYITLVceTMIPQLwkKGLFDAVDLFCE-----SVGFNVAQSERVl 231
Cdd:COG1820 124 egpflspekkgAHPPEYIRPPDpeeldrlleaagGLIKLV--TLAPEL--PGALEFIRYLVEagvvvSLGHTDATYEQA- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 232 QTAKALGIPVKGHveqlslLGGA--QLVSRYQGLsadhieyldeAGVAAMRDGGTVGVLLPGafyflretQH-PP--VEL 306
Cdd:COG1820 199 RAAFEAGATHVTH------LFNAmsPLHHREPGV----------VGAALDDDDVYAELIADG--------IHvHPaaVRL 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 307 LRRYQVP---VAV-----ASDFNPGTSPFCSL-------------------HLAMNmACVQF-----GLTPEEAWAGVTR 354
Cdd:COG1820 255 ALRAKGPdrlILVtdamaAAGLPDGEYELGGLevtvkdgvarladgtlagsTLTMD-DAVRNlvewtGLPLEEAVRMASL 333
|
410 420 430
....*....|....*....|....*....|....*.
gi 447172232 355 HAARALGRQATHGQLRAGYRADFVVWDAEQPVEIVY 390
Cdd:COG1820 334 NPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATW 369
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
267-379 |
2.74e-08 |
|
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. The Arabidopsis homolog LAF3 has been identified as a factor required for phytochrome A signalling.
Pssm-ID: 238625 [Multi-domain] Cd Length: 479 Bit Score: 55.39 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 267 HIEYLDEAGVAAMRDGGTVGVLLPG-AFYFL-----------RETQHPPVELLRRYQVPVAVASDFNPGT-SPFCSLHLA 333
Cdd:cd01300 346 HAQLVSPDDIPRFAKLGVIASVQPNhLYSDGdaaedrrlgeeRAKRSYPFRSLLDAGVPVALGSDAPVAPpDPLLGIWAA 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 447172232 334 MN--------MACVQFGLTPEEAWAGVTRHAARALGRQATHGQLRAGYRADFVV 379
Cdd:cd01300 426 VTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
267-382 |
2.82e-08 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 55.58 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 267 HIEYLDEAGVAAMRDGGTVGVLLP--------GAFyflretqhpPVELLRRYQVPVAVASDFNPGTSpFCSLHlAMNMAC 338
Cdd:PRK09228 270 HCIHLEDRERRRLAETGAAIAFCPtsnlflgsGLF---------DLKRADAAGVRVGLGTDVGGGTS-FSMLQ-TMNEAY 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 447172232 339 -VQ----FGLTPEEAWAGVTRHAARALGRQATHGQLRAGYRADFVVWDA 382
Cdd:PRK09228 339 kVQqlqgYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDP 387
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
300-383 |
6.92e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 54.46 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 300 QHPPVELLRRYQVPVAVASDFNPGtsPFCSLHL---------AMNMACVQFG--LTPEEAWAGVTRHAARALGRQATHGQ 368
Cdd:pfam07969 347 GLTPVKELLNAGVKVALGSDAPVG--PFDPWPRigaavmrqtAGGGEVLGPDeeLSLEEALALYTSGPAKALGLEDRKGT 424
|
90
....*....|....*
gi 447172232 369 LRAGYRADFVVWDAE 383
Cdd:pfam07969 425 LGVGKDADLVVLDDD 439
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
35-388 |
1.67e-07 |
|
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: 53.17 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 35 LIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHL----------VFAGNRAA------------------- 85
Cdd:COG0044 18 VLIEDGRIAAIGPDLAAP-EAAEVIDATGLLVLPGLIDLHVHLrepglehkedIETGTRAAaaggvttvvdmpntnpvtd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 86 ------EWEQRLNGASYQHISAQGGginatvsATRACAEETlyqlarERMMRLASEGVTLLEIKSGY--GLELATEEKLL 157
Cdd:COG0044 97 tpealeFKLARAEEKALVDVGPHGA-------LTKGLGENL------AELGALAEAGAVAFKVFMGSddGNPVLDDGLLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 158 RVAAKLAAENAidisptLLAAHAtpaeyrDDPDgyitLVCETMI------PQLWKKGlfdaVDLFCESVgfnvaQSERVL 231
Cdd:COG0044 164 RALEYAAEFGA------LVAVHA------EDPD----LIRGGVMnegktsPRLGLKG----RPAEAEEE-----AVARDI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 232 QTAKALGIPVkgHVEQLSLLGGAQLVSRY--QGL--SAD----HIeYLDEagvAAMRDGGTVGVLLPGafyfLRETQHpp 303
Cdd:COG0044 219 ALAEETGARL--HIVHVSTAEAVELIREAkaRGLpvTAEvcphHL-TLTD---EDLERYGTNFKVNPP----LRTEED-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 304 VELLRRYqvpVA------VASDFNP----------GTSPF------CSLHLAMNMACVQFGLTPEEAWAGVTRHAARALG 361
Cdd:COG0044 287 REALWEG---LAdgtidvIATDHAPhtleekelpfAEAPNgipgleTALPLLLTELVHKGRLSLERLVELLSTNPARIFG 363
|
410 420
....*....|....*....|....*..
gi 447172232 362 rQATHGQLRAGYRADFVVWDAEQPVEI 388
Cdd:COG0044 364 -LPRKGRIAVGADADLVLFDPDAEWTV 389
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
28-381 |
2.10e-07 |
|
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl group of N-acetyl-glucosamine-6-phosphate (GlcNAc-6-P) to glucosamine 6-phosphate and acetate. This is the first committed step in the biosynthetic pathway to amino-sugar-nucleotides, which is needed for cell wall peptidoglycan and teichoic acid biosynthesis. Deacetylation of N-acetylglucosamine is also important in lipopolysaccharide synthesis and cell wall recycling.
Pssm-ID: 238434 [Multi-domain] Cd Length: 374 Bit Score: 52.58 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 28 GLVDNQALIVREGHICDIVPEtQLPVSGDNIHDMQGRLVTPGLIDCHTHlvfagnraaeweqrlngasyqhisaqGGGIN 107
Cdd:cd00854 12 GGLEDGAVLVEDGKIVAIGPE-DELEEADEIIDLKGQYLVPGFIDIHIH--------------------------GGGGA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 108 ATVSATracaEETLYQLARermmRLASEGVTLLeiksgygleLAT-----EEKLLRVAAKLAAENAIDISPTLLAAH--- 179
Cdd:cd00854 65 DFMDGT----AEALKTIAE----ALAKHGTTSF---------LPTtvtapPEEIAKALAAIAEAIAEGQGAEILGIHleg 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 180 ---------ATPAEYRDDPD------------GYITLVceTMIPQLwkKGLFDAVDLFCE-----SVGFNVAQSERVlQT 233
Cdd:cd00854 128 pfispekkgAHPPEYLRAPDpeelkkwleaagGLIKLV--TLAPEL--DGALELIRYLVErgiivSIGHSDATYEQA-VA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 234 AKALGIpvkGHVEQLsllggaqlvsrYQGLSADHieyldeagvaaMRDGGTVGVLL--PGAFYflrET------QHPP-V 304
Cdd:cd00854 203 AFEAGA---THVTHL-----------FNAMSPLH-----------HREPGVVGAALsdDDVYA---ELiadgihVHPAaV 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 305 ELLRRYQVP---VAV-----ASDFNPGTSPFCSLH--------------LA-----MNmACVQF-----GLTPEEAWAGV 352
Cdd:cd00854 255 RLAYRAKGAdkiVLVtdamaAAGLPDGEYELGGQTvtvkdgvarladgtLAgstltMD-QAVRNmvkwgGCPLEEAVRMA 333
|
410 420
....*....|....*....|....*....
gi 447172232 353 TRHAARALGRQATHGQLRAGYRADFVVWD 381
Cdd:cd00854 334 SLNPAKLLGLDDRKGSLKPGKDADLVVLD 362
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
66-385 |
3.09e-06 |
|
Metallo-dependent hydrolases, subgroup D 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: 238637 [Multi-domain] Cd Length: 381 Bit Score: 48.98 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 66 VTPGLIDCHTHLVFAGNRAA-------EWEQRLNgASYQHISAQGG------GINATVSA-TRACAEETLYQLArerMMR 131
Cdd:cd01312 29 LLPGLINAHTHLEFSANVAQftygrfrAWLLSVI-NSRDELLKQPWeeairqGIRQMLESgTTSIGAISSDGSL---LPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 132 LASEGVTLLEIKSGYGLELATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYRDDPDGYITLvcetmiPQLWKK---- 207
Cdd:cd01312 105 LASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPYSVHPELAQDL------IDLAKKlnlp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 208 -------GLFDAVDLFCESVGFNVA-QSERVLQTAKALGIPvKGHVEQLSLLGGAqlvsryqgLSADHIEYLDEAGVAAM 279
Cdd:cd01312 179 lsthfleSKEEREWLEESKGWFKHFwESFLKLPKPKKLATA-IDFLDMLGGLGTR--------VSFVHCVYANLEEAEIL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 280 RDGGTVGVLLPGAFYFLrETQHPPVELLRRYQVPVAVASDfnpGTSPFCSLHLAMNM-----ACVQFGL--TPEEAWAGV 352
Cdd:cd01312 250 ASRGASIALCPRSNRLL-NGGKLDVSELKKAGIPVSLGTD---GLSSNISLSLLDELralldLHPEEDLleLASELLLMA 325
|
330 340 350
....*....|....*....|....*....|...
gi 447172232 353 TRHAARALGRQAthGQLRAGYRADFVVWDAEQP 385
Cdd:cd01312 326 TLGGARALGLNN--GEIEAGKRADFAVFELPGP 356
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
35-376 |
3.32e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 48.60 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 35 LIVREGHICD-----------------IVPETQLPVSG-DNIHDMQGRLVTPGLIDCHTHLVFAGNraaewEQRLNGasy 96
Cdd:PRK12394 5 ILITNGHIIDparnineinnlriindiIVDADKYPVASeTRIIHADGCIVTPGLIDYHAHVFYDGT-----EGGVRP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 97 qHISAQGGGINATVSATRA-CAEetlYQLARERMMRLASEGV-TLLEIKSGYGLELATEEKLlrvAAKLAAENAIdispt 174
Cdd:PRK12394 77 -DMYMPPNGVTTVVDAGSAgTAN---FDAFYRTVICASKVRIkAFLTVSPPGQTWSGYQENY---DPDNIDENKI----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 175 llaaHATPAEYRDDPDGYITLVCETMIPQLWKKGLfdavdlfcesvgfnvaqsERVLQTAKALGIPVKGHVEQlSLLGGA 254
Cdd:PRK12394 145 ----HALFRQYRNVLQGLKLRVQTEDIAEYGLKPL------------------TETLRIANDLRCPVAVHSTH-PVLPMK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 255 QLVSRYQglSAD---HIEY------LDEAG--VAAMRDGGTVGVLLP---GAFYFLRETQHPPVEllrRYQVPVAVASDF 320
Cdd:PRK12394 202 ELVSLLR--RGDiiaHAFHgkgstiLTEEGavLAEVRQARERGVIFDaanGRSHFDMNVARRAIA---NGFLPDIISSDL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 447172232 321 NPGT---SPFCSLHLAMNMAcVQFGLTPEEAWAGVTRHAARALGRQATHGQLRAGYRAD 376
Cdd:PRK12394 277 STITklaWPVYSLPWVLSKY-LALGMALEDVINACTHTPAVLMGMAAEIGTLAPGAFAD 334
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-77 |
4.36e-06 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 48.69 E-value: 4.36e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447172232 16 LATMDPQRQApyglVDNQALIVREGHICDIVPETQLPVSGDNIHDMQGRLVTPGLIDCHTHL 77
Cdd:PRK08203 11 IVTMDAARRE----IADGGLVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
29-77 |
1.24e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 47.29 E-value: 1.24e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447172232 29 LVDnqaLIVREGHICDIVPETQLPVSGDNIhDMQGRLVTPGLIDCHTHL 77
Cdd:PRK07583 40 LVD---IEIADGKIAAILPAGGAPDELPAV-DLKGRMVWPCFVDMHTHL 84
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
26-77 |
1.92e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 46.34 E-value: 1.92e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 447172232 26 PYGLVDNQALIVREGHICDIVPEtqLPVSGDNIHDMQGRLVTPGLIDCHTHL 77
Cdd:PRK09357 13 PKGLDEVADVLIDDGKIAAIGEN--IEAEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
8-388 |
6.70e-05 |
|
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: 44.97 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 8 DTVWRNIRLATMDPQRQApyglvdnqALIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHLVFAGNraAEW 87
Cdd:cd01315 1 DLVIKNGRVVTPDGVREA--------DIAVKGGKIAAIGPDIANT-EAEEVIDAGGLVVMPGLIDTHVHINEPGR--TEW 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 88 EQRLNGASyqhiSAQGGGI--------NATVSATRACAEETLYQLARERMM------------------RLASEGVTLLE 141
Cdd:cd01315 70 EGFETGTK----AAAAGGIttiidmplNSIPPTTTVENLEAKLEAAQGKLHvdvgfwgglvpgnldqlrPLDEAGVVGFK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 142 ---IKSGYG-LELATEEKLLRVAAKLAAENAIdisptlLAAHATPAEYRDDPDGyitlvcetmipQLWKKGLFDAVDlFC 217
Cdd:cd01315 146 cflCPSGVDeFPAVDDEQLEEAMKELAKTGSV------LAVHAENPEITEALQE-----------QAKAKGKRDYRD-YL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 218 ES--VGFNVAQSERVLQTAKALGIPVkgHVEQLSLLGGAQLVSRYQGLSAD-HIE----YLdeaGVAA--MRDGGTVGVL 288
Cdd:cd01315 208 ASrpVFTEVEAIQRILLLAKETGCRL--HIVHLSSAEAVPLIREARAEGVDvTVEtcphYL---TFTAedVPDGGTEFKC 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 289 LPGafyfLRETQHppVELLRRYQVP---VAVASDFNP------------------GTSpfcSLHLAMNM----ACVQFGL 343
Cdd:cd01315 283 APP----IRDAAN--QEQLWEALENgdiDMVVSDHSPctpelkllgkgdffkawgGIS---GLQLGLPVmlteAVNKRGL 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 447172232 344 TPEEAWAGVTRHAARALGRQATHGQLRAGYRADFVVWDAEQPVEI 388
Cdd:cd01315 354 SLEDIARLMCENPAKLFGLSHQKGRIAVGYDADFVVWDPEEEFTV 398
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
303-381 |
7.72e-05 |
|
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the conversion of guanine to xanthine and ammonia, the first step to utilize guanine as a nitrogen source. This reaction also removes the guanine base from the pool and therefore can play a role in the regulation of cellular GTP and the guanylate nucleotide pool.
Pssm-ID: 238628 [Multi-domain] Cd Length: 429 Bit Score: 44.58 E-value: 7.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 303 PVELLRRYQVPVAVASDFNPGTSP----------FCSLHLAMNMACVQFgLTPEEAWAGVTRHAARALGRQATHGQLRAG 372
Cdd:cd01303 302 DVRKLLDAGIKVGLGTDVGGGTSFsmldtlrqayKVSRLLGYELGGHAK-LSPAEAFYLATLGGAEALGLDDKIGNFEVG 380
|
....*....
gi 447172232 373 YRADFVVWD 381
Cdd:cd01303 381 KEFDAVVID 389
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
27-72 |
1.03e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 44.20 E-value: 1.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 447172232 27 YGLVDNQALIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLID 72
Cdd:PRK11170 13 HEVLDDHAVVIADGLIEAVCPVAELP-PGIEQRDLNGAILSPGFID 57
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
7-78 |
1.69e-04 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 43.45 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447172232 7 GDTVWRNIRLATMDPQRQAPYGlvdnqALIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHLV 78
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREIVDG-----DVLIEDDRIAAVGDRLDLE-DYDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
37-81 |
2.29e-04 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 42.85 E-value: 2.29e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 447172232 37 VREGHICDiVPETQLPVSGDNIHDMQGRLVTPGLIDCHTHlVFAG 81
Cdd:COG3964 24 IKDGKIAA-VAKDIDAAEAKKVIDASGLYVTPGLIDLHTH-VFPG 66
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
37-384 |
2.53e-04 |
|
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: 43.05 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 37 VREGHICDIVPEtqLPVSGDNIHDMQGRLVTPGLIDCHTH--------------------LVFAGN-----------RAA 85
Cdd:cd01297 24 IRDGRIAAIGPI--LSTSAREVIDAAGLVVAPGFIDVHTHydgqvfwdpdlrpssrqgvtTVVLGNcgvspapanpdDLA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 86 EWEQRLNG---------------ASY-QHISAQGGGINATVSATRAcaeetlyQLARERMMRLASEgvtlleiksgygle 149
Cdd:cd01297 102 RLIMLMEGlvalgeglpwgwatfAEYlDALEARPPAVNVAALVGHA-------ALRRAVMGLDARE-------------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 150 lATEEKLLRVAAKLA---AENAIDISPTLLAAH---ATPAEYrddpdgyiTLVCETMIpqlwKKG--LFDAVDLFCESVg 221
Cdd:cd01297 161 -ATEEELAKMRELLRealEAGALGISTGLAYAPrlyAGTAEL--------VALARVAA----RYGgvYQTHVRYEGDSI- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 222 fnVAQSERVLQTAKALGIPVkghveQLSLLG--GAQLVSRYQgLSADHIEyldeagvAAMRDGGTVGV-LLPGAFYFLRE 298
Cdd:cd01297 227 --LEALDELLRLGRETGRPV-----HISHLKsaGAPNWGKID-RLLALIE-------AARAEGLQVTAdVYPYGAGSEDD 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 299 TQhppvELLRRYQVPvaVASDFNPGTSPfcslHLAMnMACVQF----------GLTPEEAWAGVTRHAARALGrQATHGQ 368
Cdd:cd01297 292 VR----RIMAHPVVM--GGSDGGALGKP----HPRS-YGDFTRvlghyvrerkLLSLEEAVRKMTGLPARVFG-LADRGR 359
|
410
....*....|....*.
gi 447172232 369 LRAGYRADFVVWDAEQ 384
Cdd:cd01297 360 IAPGYRADIVVFDPDT 375
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
26-76 |
2.56e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.98 E-value: 2.56e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 447172232 26 PYGLV-DNQALIVREGHICDIVPETQLPV--SGDNIHDMQGRLVTPGLIDCHTH 76
Cdd:PRK09045 21 PAGVVlEDHAVAIRDGRIVAILPRAEARAryAAAETVELPDHVLIPGLINAHTH 74
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
9-87 |
6.52e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 41.53 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 9 TVWRNIRLATMDPQRqapyGLVDNQALIVREGHICDIVPEtqLPVSGDNIHDMQGRLVTPGLIDCHTHLVFAGNR--AAE 86
Cdd:PRK08204 4 TLIRGGTVLTMDPAI----GDLPRGDILIEGDRIAAVAPS--IEAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRgiGAD 77
|
.
gi 447172232 87 W 87
Cdd:PRK08204 78 W 78
|
|
| PLN02795 |
PLN02795 |
allantoinase |
26-110 |
9.77e-04 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 41.30 E-value: 9.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 26 PYGLVDNqALIVREGHICDIVPETQLPVSGDNIH--DMQGRLVTPGLIDCHTHLVFAGNraAEWEQRLNGASyqhiSAQG 103
Cdd:PLN02795 56 PAGVIPG-AVEVEGGRIVSVTKEEEAPKSQKKPHvlDYGNAVVMPGLIDVHVHLNEPGR--TEWEGFPTGTK----AAAA 128
|
....*..
gi 447172232 104 GGINATV 110
Cdd:PLN02795 129 GGITTLV 135
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
303-381 |
1.30e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.61 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 303 PVELLRRYQVPVAVASD---FNPGTSPFCSLHLAMNMACVQFG---LTPEEA--WAgvTRHAARALGRQAThGQLRAGYR 374
Cdd:PRK08203 305 PVRELRAAGVPVGLGVDgsaSNDGSNLIGEARQALLLQRLRYGpdaMTAREAleWA--TLGGARVLGRDDI-GSLAPGKL 381
|
....*..
gi 447172232 375 ADFVVWD 381
Cdd:PRK08203 382 ADLALFD 388
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
231-390 |
2.97e-03 |
|
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is part of one of the adenine salvage pathways, as well as the degradation pathway. It is important for adenine utilization as a purine, as well as a nitrogen source in bacteria and archea.
Pssm-ID: 238620 [Multi-domain] Cd Length: 422 Bit Score: 39.51 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 231 LQTAKALGIPVKGHVEQLSllgGAQL-VSRYQGLSADH----IEYLDE---AGVAAMRDGGTVG----VLLPgafyflre 298
Cdd:cd01295 127 IQAAKKAGKPVDGHAPGLS---GEELnAYMAAGISTDHeamtGEEALEklrLGMYVMLREGSIAknleALLP-------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 299 tqhppvELLRRYQVPVAVASDfnpGTSPFCSLHLAMNMACV----QFGLTPEEAWAGVTRHAARALGRQaTHGQLRAGYR 374
Cdd:cd01295 196 ------AITEKNFRRFMFCTD---DVHPDDLLSEGHLDYIVrraiEAGIPPEDAIQMATINPAECYGLH-DLGAIAPGRI 265
|
170
....*....|....*...
gi 447172232 375 ADFVVW-DAEQP-VEIVY 390
Cdd:cd01295 266 ADIVILdDLENFnITTVL 283
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
338-394 |
3.00e-03 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 39.70 E-value: 3.00e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 447172232 338 CVQFGLTPEEAWAGVTRHAARALGRqATHGQLRAGYRADFVVWD--AEQPVEIVYEPGR 394
Cdd:COG1001 279 AIELGLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADIVLLDdlEDFKVEKVYADGK 336
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
8-88 |
3.11e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 39.68 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 8 DTVWRNIRLATMDPQRQAPYGlvdnqaliVREGHICDIVPETQLPvsGDNIHDMQGRLVTPGLIDCHTHLVFAGNraAEW 87
Cdd:PRK06189 4 DLIIRGGKVVTPEGVYRADIG--------IKNGKIAEIAPEISSP--AREIIDADGLYVFPGMIDVHVHFNEPGR--THW 71
|
.
gi 447172232 88 E 88
Cdd:PRK06189 72 E 72
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
315-404 |
5.12e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 38.62 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 315 AVASDFNPGtspfcSLHLAMNMACVQFGLTPEEAWAGVTRHAARALG---RqathGQLRAGYRADFVVwdaeqpveiVYE 391
Cdd:PRK15446 301 ILSSDYYPA-----SLLDAAFRLADDGGLDLPQAVALVTANPARAAGlddR----GEIAPGKRADLVR---------VRR 362
|
90
....*....|...
gi 447172232 392 PGRNPLYQRVYRG 404
Cdd:PRK15446 363 AGGLPVVRAVWRG 375
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
8-77 |
6.58e-03 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 38.53 E-value: 6.58e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172232 8 DTVWRNIRLATMDPQRQAPYGlvdnqaliVREGHICDIvpETQLPvSGDNIHDMQGRLVTPGLIDCHTHL 77
Cdd:PRK13404 5 DLVIRGGTVVTATDTFQADIG--------IRGGRIAAL--GEGLG-PGAREIDATGRLVLPGGVDSHCHI 63
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
337-385 |
8.00e-03 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 38.29 E-value: 8.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447172232 337 ACVQFGLTPEEAWAGVTRHAARALGRQAthGQLRAGYRADFVVWDAEQP 385
Cdd:PRK09229 351 AAAAQPSVGRRLFDAALAGGAQALGRAI--GGLAVGARADLVVLDLDHP 397
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
342-389 |
8.89e-03 |
|
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: 38.08 E-value: 8.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447172232 342 GLTPEEAWAGVTRHAARALGRqATHGQLRAGYRADFVVWD-AEQPVEIV 389
Cdd:cd01307 276 GMPLEEVIEAVTANPARMLGL-AEIGTLAVGYDADLTVFDlKDGRVELV 323
|
|
| |
