|
Name |
Accession |
Description |
Interval |
E-value |
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
35-404 |
8.17e-160 |
|
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: 454.41 E-value: 8.17e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 35 LIVREGHICDIVPETQLPVSG---DNIHDMQGRLVTPGLIDCHTHLVFAGNRAAEWEQRLNGASYQHISAQGGGINATVS 111
Cdd:cd01296 1 IAIRDGRIAAVGPAASLPAPGpaaAEEIDAGGRAVTPGLVDCHTHLVFAGDRVDEFAARLAGASYEEILAAGGGILSTVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 112 ATRACAEETLYLLARERMMRLASEGVTLLEIKSGYGLELATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYRDDPDg 191
Cdd:cd01296 81 ATRAASEDELFASALRRLARMLRHGTTTVEVKSGYGLDLETELKMLRVIRRLKEEGPVDLVSTFLGAHAVPPEYKGREE- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 192 YITLVCETMIPQLWQKGLFDAVDLFCESVGFNVAQSERVLQTAKALGIPVKGHVEQLSLLGGAQLVSRYQGLSADHIEYL 271
Cdd:cd01296 160 YIDLVIEEVLPAVAEENLADFCDVFCEKGAFSLEQSRRILEAAKEAGLPVKIHADELSNIGGAELAAELGALSADHLEHT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 272 DEVGVAAMRDGGTVGVLLPGAFYFLRETqRPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMACVQFGLTPEEAWAG 351
Cdd:cd01296 240 SDEGIAALAEAGTVAVLLPGTAFSLRET-YPPARKLIDAGVPVALGTDFNPGSSPTSSMPLVMHLACRLMRMTPEEALTA 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 447172216 352 VTRHAARALGRQATHGQIRAGYRADFVVWDAEQPVEIVYEPGRNPLYQRVYRG 404
Cdd:cd01296 319 ATINAAAALGLGETVGSLEVGKQADLVILDAPSYEHLAYRFGVNLVEYVIKNG 371
|
|
| hutI |
TIGR01224 |
imidazolonepropionase; This enzyme catalyzes the third step in histidine degradation. [Energy ... |
30-406 |
1.81e-158 |
|
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: 451.10 E-value: 1.81e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 30 VDNQALIVREGHICDIVPETQLP-VSGDNIHDMQGRLVTPGLIDCHTHLVFAGNRAAEWEQRLNGASYQHISAQGGGINA 108
Cdd:TIGR01224 1 IEDAVILIHGGKIVWIGQLAALPgEEATEIIDCGGGLVTPGLVDPHTHLVFAGDRVNEFEMKLQGASYLEILAQGGGILS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 109 TVSATRACAEETLYLLARERMMRLASEGVTLLEIKSGYGLELATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYRDD 188
Cdd:TIGR01224 81 TVRATRAASEEELLKLALFRLKSMLRSGTTTAEVKSGYGLDLETELKMLRAAKALHEEQPVDVVTTFLGAHAVPPEFQGR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 189 PDGYITLVCETMIPQLWQKGLFDAVDLFCESVGFNVAQSERVLQTAKALGIPVKGHVEQLSLLGGAQLVSRYQGLSADHI 268
Cdd:TIGR01224 161 PDDYVDGICEELIPQVAEEGLASFADVFCEAGVFSVEQSRRILQAAQEAGLPVKLHAEELSNLGGAELAAKLGAVSADHL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 269 EYLDEVGVAAMRDGGTVGVLLPGAFYFLREtQRPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMACVQFGLTPEEA 348
Cdd:TIGR01224 241 EHASDAGIKALAEAGTVAVLLPGTTFYLRE-TYPPARQLIDYGVPVALATDLNPGSSPTLSMQLIMSLACRLMKMTPEEA 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 447172216 349 WAGVTRHAARALGRQATHGQIRAGYRADFVVWDAEQPVEIVYEPGRNPLYQRVYRGKI 406
Cdd:TIGR01224 320 LHAATVNAAYALGLGEERGTLEAGRDADLVILSAPSYAEIPYHYGVNHVHAVIKNGNI 377
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
6-406 |
8.48e-85 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 263.74 E-value: 8.48e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 6 PGDTVWRNIRLATMDPQqqalyGLVDNQALIVREGHICDIVPETQLPV-SGDNIHDMQGRLVTPGLIDCHTHLVFAGNRA 84
Cdd:COG1228 7 AGTLLITNATLVDGTGG-----GVIENGTVLVEDGKIAAVGPAADLAVpAGAEVIDATGKTVLPGLIDAHTHLGLGGGRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 85 AEWEQrlngasyqhisaqGGGINATVsatracaeeTLYLLARERMMRLASEGVTLLEIKSGYGLEL-----ATEEKLLRV 159
Cdd:COG1228 82 VEFEA-------------GGGITPTV---------DLVNPADKRLRRALAAGVTTVRDLPGGPLGLrdaiiAGESKLLPG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 160 AAKLAAENAIDISptlLAAHA-TPAEyrddpdgyitlvCETMIPQLWQKGlFDAVDLFCE--SVGFNVAQSERVLQTAKA 236
Cdd:COG1228 140 PRVLAAGPALSLT---GGAHArGPEE------------ARAALRELLAEG-ADYIKVFAEggAPDFSLEELRAILEAAHA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 237 LGIPVKGHVEQLSllgGAQLVSRYQGLSADHIEYLDEVGVAAMRDGGTVgVLLPGAFYFL-----------------RET 299
Cdd:COG1228 204 LGLPVAAHAHQAD---DIRLAVEAGVDSIEHGTYLDDEVADLLAEAGTV-VLVPTLSLFLallegaaapvaakarkvREA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 300 QRPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMAcVQFGLTPEEAWAGVTRHAARALGRQATHGQIRAGYRADFVV 379
Cdd:COG1228 280 ALANARRLHDAGVPVALGTDAGVGVPPGRSLHRELALA-VEAGLTPEEALRAATINAAKALGLDDDVGSLEPGKLADLVL 358
|
410 420
....*....|....*....|....*..
gi 447172216 380 WDAEQPVEIVYepgRNPLYQRVYRGKI 406
Cdd:COG1228 359 LDGDPLEDIAY---LEDVRAVMKDGRV 382
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
8-404 |
1.36e-24 |
|
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: 104.52 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 8 DTVWRNIRLATMDPQqqalYGLVDNQALIVREGHICDIVPETQLPVS--GDNIHDMQGRLVTPGLIDCHTHLVFAGNRAA 85
Cdd:COG0402 1 DLLIRGAWVLTMDPA----GGVLEDGAVLVEDGRIAAVGPGAELPARypAAEVIDAGGKLVLPGLVNTHTHLPQTLLRGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 86 -------EWEQRLNGASYQHISAQGgginATVSATRACAEetlyllarermmrLASEGVT-LLEIksgYGLELATEEKLL 157
Cdd:COG0402 77 addlpllDWLEEYIWPLEARLDPED----VYAGALLALAE-------------MLRSGTTtVADF---YYVHPESADALA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 158 RVAAKL---AAenaidISPTLLAAHAtPAEYRDDPDGYITLvCETMIPQlWQKGLFDAVDL-----FCESVgfNVAQSER 229
Cdd:COG0402 137 EAAAEAgirAV-----LGRGLMDRGF-PDGLREDADEGLAD-SERLIER-WHGAADGRIRValaphAPYTV--SPELLRA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 230 VLQTAKALGIPVKGHV-EQLSLLggAQLVSRYqGLSAdhIEYLDEVGV------------------AAMRDGGTVGVLLP 290
Cdd:COG0402 207 AAALARELGLPLHTHLaETRDEV--EWVLELY-GKRP--VEYLDELGLlgprtllahcvhltdeeiALLAETGASVAHCP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 291 GAFYFLRETqRPPVELLRRYQVPVAVASD---FNPGTSPFCSLHLAMNMACVQFG----LTPEEAWAGVTRHAARALGRQ 363
Cdd:COG0402 282 TSNLKLGSG-IAPVPRLLAAGVRVGLGTDgaaSNNSLDMFEEMRLAALLQRLRGGdptaLSAREALEMATLGGARALGLD 360
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 447172216 364 ATHGQIRAGYRADFVVWDAEQPveiVYEPGRNPLYQRVYRG 404
Cdd:COG0402 361 DEIGSLEPGKRADLVVLDLDAP---HLAPLHDPLSALVYAA 398
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
12-406 |
3.88e-18 |
|
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: 85.38 E-value: 3.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 12 RNIRLATMDPqqqalyGLVDnqaLIVREGHICDIVPetQLPVSGDNIH-DMQGRLVTPGLIDCHTHL--VFAGNRAaewe 88
Cdd:cd01293 3 RNARLADGGT------ALVD---IAIEDGRIAAIGP--ALAVPPDAEEvDAKGRLVLPAFVDPHIHLdkTFTGGRW---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 89 qrlngaSYQHISAQGGGINATVSATRACAEETLYLLARERMMRLASEGVT-------------------LLEIKSGY--- 146
Cdd:cd01293 68 ------PNNSGGTLLEAIIAWEERKLLLTAEDVKERAERALELAIAHGTTairthvdvdpaaglkaleaLLELREEWadl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 147 -----------GLELATE-EKLLRVAAKLAAEN--AIDisptllaahatPAEYRDDPDGYITLVCEtmipqLWQKglFDA 212
Cdd:cd01293 142 idlqivafpqhGLLSTPGgEELMREALKMGADVvgGIP-----------PAEIDEDGEESLDTLFE-----LAQE--HGL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 213 -VDLFC-ESVGFNVAQSERVLQTAKALGIPVK---GHVEQLSLLGGAQLvsryqglsADHIEYLDEVGVAAMRDGGTVGV 287
Cdd:cd01293 204 dIDLHLdETDDPGSRTLEELAEEAERRGMQGRvtcSHATALGSLPEAEV--------SRLADLLAEAGISVVSLPPINLY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 288 LLPGAFYFLRETQRPPVELLRRYQVPVAVASD-----FNP-GT-SPFCSLHLAMNMAcvqfGLTPEE----AWAGVTRHA 356
Cdd:cd01293 276 LQGREDTTPKRRGVTPVKELRAAGVNVALGSDnvrdpWYPfGSgDMLEVANLAAHIA----QLGTPEdlalALDLITGNA 351
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 447172216 357 ARALGrqATHGQIRAGYRADFVVWDAEQPVEIVYEpgRNPLYQRVYRGKI 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 |
2.38e-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: 72.75 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 70 LIDCHTHLVFAGNRAAEWEQRLNGASYQhisaqggginatvsatracAEETLYLLARERMMRLASEGVTLLEIKSGYGLE 149
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLELKEAEEL-------------------SPEDLYEDTLRALEALLAGGVTTVVDMGSTPPP 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 150 LATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYRDDPDGYITLvcetmIPQLWQKGlFDAVDLF--CESVGFNVAQS 227
Cdd:cd01292 62 TTTKAAIEAVAEAARASAGIRVVLGLGIPGVPAAVDEDAEALLLEL-----LRRGLELG-AVGLKLAgpYTATGLSDESL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 228 ERVLQTAKALGIPVKGHVEQLSLLGGA--QLVSRY---QGLSADHIEYLDEVGVAAMRDGGTVGVLLPGAFYFLR--ETQ 300
Cdd:cd01292 136 RRVLEEARKLGLPVVIHAGELPDPTRAleDLVALLrlgGRVVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGrdGEG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 301 RPPVELLRRYQVPVAVASDFNPGTSPFCSLH-LAMNMACVQFGLTPEEAWAGVTRHAARA 359
Cdd:cd01292 216 AEALRRLLELGIRVTLGTDGPPHPLGTDLLAlLRLLLKVLRLGLSLEEALRLATINPARA 275
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
60-382 |
2.62e-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: 61.16 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 60 DMQGRLVTPGLIDCHTHLVF-AGNRAAEWEQRLNGASYQHISAQGGGINATVSATRACAEETLYLLARE---------RM 129
Cdd:cd01299 5 DLGGKTLMPGLIDAHTHLGSdPGDLPLDLALPVEYRTIRATRQARAALRAGFTTVRDAGGADYGLLRDAidaglipgpRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 130 MR-----------LASEGVTLLEIKSGYGLELATEEKLLRVAAKLAAENA--IDISPTllAAHATPAeyrDDPDgyitlv 196
Cdd:cd01299 85 FAsgralsqtgghGDPRGLSGLFPAGGLAAVVDGVEEVRAAVREQLRRGAdqIKIMAT--GGVLSPG---DPPP------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 197 cetmipqlwqkglfdavdlfceSVGFNVAQSERVLQTAKALGIPVKGHVEqlsllgGAQLVSRYQGLSADHIE---YLDE 273
Cdd:cd01299 154 ----------------------DTQFSEEELRAIVDEAHKAGLYVAAHAY------GAEAIRRAIRAGVDTIEhgfLIDD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 274 VGVAAMRDGGTVGV---------LLPGAFYFL-----------RETQRPPVELLRRYQVPVAVASDFNPGTSPFCSLHLA 333
Cdd:cd01299 206 ETIELMKEKGIFLVptlatyealAAEGAAPGLpadsaekvalvLEAGRDALRRAHKAGVKIAFGTDAGFPVPPHGWNARE 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 447172216 334 MNMAcVQFGLTPEEAWAGVTRHAARALGRQATHGQIRAGYRADFVVWDA 382
Cdd:cd01299 286 LELL-VKAGGTPAEALRAATANAAELLGLSDELGVIEAGKLADLLVVDG 333
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
65-398 |
2.66e-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: 61.36 E-value: 2.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 65 LVTPGLIDCHTHLVFAGNRAAeweqRLNGASYQHISAQG------GGInATVSATRACAEEtlyllARERMMRLASEgvt 138
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGI----PVPPEFAYEALRLGittmlkSGT-TTVLDMGATTST-----GIEALLEAAEE--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 139 lleIKSGYGLELAteekllrvaaklaaenaiDISPTLLAAHATPAEYRDDPDGYITLVCETMipqlwQKGLFDAVDLFcE 218
Cdd:pfam01979 68 ---LPLGLRFLGP------------------GCSLDTDGELEGRKALREKLKAGAEFIKGMA-----DGVVFVGLAPH-G 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 219 SVGFNVAQSERVLQTAKALGIPVKGHVeqLSLLGGAQLVSRYQGLSADHIEYLDEVGVAAMRDGGTV----GVLLPGAFY 294
Cdd:pfam01979 121 APTFSDDELKAALEEAKKYGLPVAIHA--LETKGEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLilahGVHLSPTEA 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 295 -------------------FLRETQRPPVELLRRYQVPVAVASDFNPGTSPFCSLHLAMNMACVQF----GLTPEEAWAG 351
Cdd:pfam01979 199 nllaehlkgagvahcpfsnSKLRSGRIALRKALEDGVKVGLGTDGAGSGNSLNMLEELRLALELQFdpegGLSPLEALRM 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 447172216 352 VTRHAARALGRQATHGQIRAGYRADFVVWDAEQPVEIVY-EPGRNPLY 398
Cdd:pfam01979 279 ATINPAKALGLDDKVGSIEVGKDADLVVVDLDPLAAFFGlKPDGNVKK 326
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
39-394 |
2.86e-10 |
|
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: 61.17 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 39 EGHICDIVPETQLPVSGDNIhDMQGRLVTPGLIDCHTHL-------VFAGNRAAEweqrLNGASYQHISAqGGGINATVS 111
Cdd:cd01309 1 DGKIVAVGAEITTPADAEVI-DAKGKHVTPGLIDAHSHLgldeeggVRETSDANE----ETDPVTPHVRA-IDGINPDDE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 112 A-TRACAEETLYLL----------ARERMMRLASEGVTLLEIKSGYGLELATEEKLLRVaaklaaENAIDISPTllAAHA 180
Cdd:cd01309 75 AfKRARAGGVTTVQvlpgsanligGQGVVIKTDGGTIEDMFIKAPAGLKMALGENPKRV------YGGKGKEPA--TRMG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 181 TPAEYRD---DPDGYItlvcETMIPQLWQKGLFDAVDLFCESVGfNVAQSErvlqtakalgIPVKGHVEQLSllggaqlv 257
Cdd:cd01309 147 VAALLRDafiKAQEYG----RKYDLGKNAKKDPPERDLKLEALL-PVLKGE----------IPVRIHAHRAD-------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 258 sryQGLSAdhIEYLDEVGVAAMRDGGTVGVLLP------------GAFYFLRETQRP-------PVELLRRYQVPVAVAS 318
Cdd:cd01309 204 ---DILTA--IRIAKEFGIKITIEHGAEGYKLAdelakhgipviyGPTLTLPKKVEEvndaidtNAYLLKKGGVAFAISS 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 319 DFNPGTSPFCSLHLAMnmaCVQFGLTPEEAWAGVTRHAARALGRQATHGQIRAGYRADFVVWDAEqP------VEIVYEP 392
Cdd:cd01309 279 DHPVLNIRNLNLEAAK---AVKYGLSYEEALKAITINPAKILGIEDRVGSLEPGKDADLVVWNGD-PleptskPEQVYID 354
|
..
gi 447172216 393 GR 394
Cdd:cd01309 355 GR 356
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
6-120 |
4.88e-09 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 57.89 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 6 PGDTVWRNIRLATMDPQQ-QAlyglvdnQALIVREGHICDIVPETQLP---VSGDNIHDMQGRLVTPGLIDCHTHLVFAG 81
Cdd:COG1574 7 AADLLLTNGRIYTMDPAQpVA-------EAVAVRDGRIVAVGSDAEVRalaGPATEVIDLGGKTVLPGFIDAHVHLLGGG 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 447172216 82 NRAAEWeqRLNGASyqhisaqggGINATVSATRACAEET 120
Cdd:COG1574 80 LALLGV--DLSGAR---------SLDELLARLRAAAAEL 107
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
312-382 |
1.85e-08 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 56.35 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 312 VPVAVASDFnPGTS--PFCSLHLAMN---MACVQFG----LTPEEAWAGVTRHAARALGRQATHGQIRAGYRADFVVWDA 382
Cdd:COG1574 428 APLAFGSDA-PVEPldPLLGIYAAVTrrtPSGRGLGpeerLTVEEALRAYTIGAAYAAFEEDEKGSLEPGKLADFVVLDR 506
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
338-390 |
2.66e-08 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 55.11 E-value: 2.66e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 447172216 338 CVQF-GLTPEEAWAGVTRHAARALGRQATHGQIRAGYRADFVVWDAEQPVEIVY 390
Cdd:COG1820 316 LVEWtGLPLEEAVRMASLNPARALGLDDRKGSIAPGKDADLVVLDDDLNVRATW 369
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
302-383 |
6.39e-08 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 54.46 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 302 PPVELLRRYQVPVAVASDFNPGtsPFCSLHL---------AMNMACVQFG--LTPEEAWAGVTRHAARALGRQATHGQIR 370
Cdd:pfam07969 349 TPVKELLNAGVKVALGSDAPVG--PFDPWPRigaavmrqtAGGGEVLGPDeeLSLEEALALYTSGPAKALGLEDRKGTLG 426
|
90
....*....|...
gi 447172216 371 AGYRADFVVWDAE 383
Cdd:pfam07969 427 VGKDADLVVLDDD 439
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
12-385 |
7.27e-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: 54.13 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 12 RNIRLATMDPQqqalyGLVDNQALIVREGHICDIVPETQLPV-SGDNIHDMQGRLVTPGLIDCHTHL-------VFAGNR 83
Cdd:cd01298 4 RNGTIVTTDPR-----RVLEDGDVLVEDGRIVAVGPALPLPAyPADEVIDAKGKVVMPGLVNTHTHLamtllrgLADDLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 84 AAEW--------EQRLNGASyQHISAQGGGINATVSATRACAEetLYLLARERMMRLASEgvtlLEIKSGYGLELATEEK 155
Cdd:cd01298 79 LMEWlkdliwplERLLTEED-VYLGALLALAEMIRSGTTTFAD--MYFFYPDAVAEAAEE----LGIRAVLGRGIMDLGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 156 llrvAAKLAAENAIDISPTLLaahatpAEYRDDPDGYITLVcetMIPqlwqkglfdavdlfCESVGFNVAQSERVLQTAK 235
Cdd:cd01298 152 ----EDVEETEEALAEAERLI------REWHGAADGRIRVA---LAP--------------HAPYTCSDELLREVAELAR 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 236 ALGIPVKGHV-----EQlsllggAQLVSRYqGLSAdhIEYLDEVGVAAMRDGGTVGVLLPGA-FYFLRETQR-------- 301
Cdd:cd01298 205 EYGVPLHIHLaetedEV------EESLEKY-GKRP--VEYLEELGLLGPDVVLAHCVWLTDEeIELLAETGTgvahnpas 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 302 --------PPVELLRRYQVPVAVASD---FNPGTSPFCSLHLAMNMACVQFG----LTPEEAWAGVTRHAARALGRQATh 366
Cdd:cd01298 276 nmklasgiAPVPEMLEAGVNVGLGTDgaaSNNNLDMFEEMRLAALLQKLAHGdptaLPAEEALEMATIGGAKALGLDEI- 354
|
410
....*....|....*....
gi 447172216 367 GQIRAGYRADFVVWDAEQP 385
Cdd:cd01298 355 GSLEVGKKADLILIDLDGP 373
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
8-404 |
8.59e-08 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 53.78 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 8 DTVWRNIRLATMDPqqqalyglVDnqaLIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHL--VFAG---- 81
Cdd:PRK05985 3 DLLFRNVRPAGGAA--------VD---ILIRDGRIAAIGPALAAP-PGAEVEDGGGALALPGLVDGHIHLdkTFWGdpwy 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 82 --NRAAEWEQRL-NGASYQHISAQGGGINATVSATRACAEETLYL-----------LAR-ERMMRLASEGVTLLEI---- 142
Cdd:PRK05985 71 pnEPGPSLRERIaNERRRRAASGHPAAERALALARAAAAAGTTAMrshvdvdpdagLRHlEAVLAARETLRGLIDIqiva 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 143 --KSGYGLELATEEkLLRVAAKLAAEN--AIDisptllaahatPAEYRDDPDGYITLVCEtmIPQLWQKG----LFDAVD 214
Cdd:PRK05985 151 fpQSGVLSRPGTAE-LLDAALRAGADVvgGLD-----------PAGIDGDPEGQLDIVFG--LAERHGVGidihLHEPGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 215 LfcesvgfNVAQSERVLQTAKALGIPVKGHVEQLSLLGGAQLVSRyqglsADHIEYLDEVGVAAMRDGgtvgvllPGAFY 294
Cdd:PRK05985 217 L-------GAFQLERIAARTRALGMQGRVAVSHAFCLGDLPEREV-----DRLAERLAEAGVAIMTNA-------PGSVP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 295 FlretqrPPVELLRRYQVPVAVASD-FNPGTSPFCS---LHLAMnMACVQFGL-TPEE---AWAGVTRHAARALGRQAtH 366
Cdd:PRK05985 278 V------PPVAALRAAGVTVFGGNDgIRDTWWPYGNgdmLERAM-LIGYRSGFrTDDElaaALDCVTHGGARALGLED-Y 349
|
410 420 430
....*....|....*....|....*....|....*...
gi 447172216 367 GqIRAGYRADFVVWDAEQPVEIVYEPgrnPLYQRVYRG 404
Cdd:PRK05985 350 G-LAVGARADFVLVDAETVAEAVVAV---PVRRLVVRG 383
|
|
| Met_dep_hydrolase_D |
cd01312 |
Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent ... |
66-385 |
1.11e-07 |
|
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: 53.22 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 66 VTPGLIDCHTHLVFAGNRAA-------EWEQRLNgASYQHISAQGG------GINATVSA-TRACAEETLYLLArerMMR 131
Cdd:cd01312 29 LLPGLINAHTHLEFSANVAQftygrfrAWLLSVI-NSRDELLKQPWeeairqGIRQMLESgTTSIGAISSDGSL---LPA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 132 LASEGVTLLEIKSGYGLELATEEKLLRVAAKLAAENAIDISPTLLAAHATPAEYrddpdgyitlvceTMIPQLWQKGLFD 211
Cdd:cd01312 105 LASSGLRGVFFNEVIGSNPSAIDFKGETFLERFKRSKSFESQLFIPAISPHAPY-------------SVHPELAQDLIDL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 212 AVDL-----------------FCESVGFNVAQSERVLQTAK-ALGIPVKGHVEQLSLLGGAqlvsryqgLSADHIEYLDE 273
Cdd:cd01312 172 AKKLnlplsthfleskeerewLEESKGWFKHFWESFLKLPKpKKLATAIDFLDMLGGLGTR--------VSFVHCVYANL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 274 VGVAAMRDGGTVGVLLPGAFYFLrETQRPPVELLRRYQVPVAVASDfnpGTSPFCSLHLAMNM-----ACVQFGL--TPE 346
Cdd:cd01312 244 EEAEILASRGASIALCPRSNRLL-NGGKLDVSELKKAGIPVSLGTD---GLSSNISLSLLDELralldLHPEEDLleLAS 319
|
330 340 350
....*....|....*....|....*....|....*....
gi 447172216 347 EAWAGVTRHAARALGRQAthGQIRAGYRADFVVWDAEQP 385
Cdd:cd01312 320 ELLLMATLGGARALGLNN--GEIEAGKRADFAVFELPGP 356
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
28-381 |
1.54e-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: 52.97 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 28 GLVDNQALIVREGHICDIVPEtQLPVSGDNIHDMQGRLVTPGLIDCHTHlvfagnraaeweqrlngasyqhisaqGGGIN 107
Cdd:cd00854 12 GGLEDGAVLVEDGKIVAIGPE-DELEEADEIIDLKGQYLVPGFIDIHIH--------------------------GGGGA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 108 ATVSATracaEETLYLLARermmRLASEGVTLLeiksgygleLAT-----EEKLLRVAAKLAAENAIDISPTLLAAH--- 179
Cdd:cd00854 65 DFMDGT----AEALKTIAE----ALAKHGTTSF---------LPTtvtapPEEIAKALAAIAEAIAEGQGAEILGIHleg 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 180 ---------ATPAEYRDDPD------------GYITLVceTMIPQLwqKGLFDAVDLFCE-----SVGFNVAQSERVlQT 233
Cdd:cd00854 128 pfispekkgAHPPEYLRAPDpeelkkwleaagGLIKLV--TLAPEL--DGALELIRYLVErgiivSIGHSDATYEQA-VA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 234 AKALGIPVKGHveqlslLGGA--QLVSRYQGLsadhieyldeVGVAAMRDGGTVGV------LLPGAFYFLRETQRPPve 305
Cdd:cd00854 203 AFEAGATHVTH------LFNAmsPLHHREPGV----------VGAALSDDDVYAELiadgihVHPAAVRLAYRAKGAD-- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 306 llRRYQVPVAV-ASDFNPGTSPFCSLH--------------LA-----MNmACVQF-----GLTPEEAWAGVTRHAARAL 360
Cdd:cd00854 265 --KIVLVTDAMaAAGLPDGEYELGGQTvtvkdgvarladgtLAgstltMD-QAVRNmvkwgGCPLEEAVRMASLNPAKLL 341
|
410 420
....*....|....*....|.
gi 447172216 361 GRQATHGQIRAGYRADFVVWD 381
Cdd:cd00854 342 GLDDRKGSLKPGKDADLVVLD 362
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
267-379 |
2.99e-07 |
|
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: 52.31 E-value: 2.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 267 HIEYLDEVGVAAMRDGGTVGVLLPG-AFYFL-----------RETQRPPVELLRRYQVPVAVASDFNPGT-SPFCSLHLA 333
Cdd:cd01300 346 HAQLVSPDDIPRFAKLGVIASVQPNhLYSDGdaaedrrlgeeRAKRSYPFRSLLDAGVPVALGSDAPVAPpDPLLGIWAA 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 447172216 334 MN--------MACVQFGLTPEEAWAGVTRHAARALGRQATHGQIRAGYRADFVV 379
Cdd:cd01300 426 VTrktpgggvLGNPEERLSLEEALRAYTIGAAYAIGEEDEKGSLEPGKLADFVV 479
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
267-382 |
3.42e-07 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 52.12 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 267 HIEYLDEVGVAAMRDGGTVGVLLP--------GAFyflretqrpPVELLRRYQVPVAVASDFNPGTSpFCSLHlAMNMAC 338
Cdd:PRK09228 270 HCIHLEDRERRRLAETGAAIAFCPtsnlflgsGLF---------DLKRADAAGVRVGLGTDVGGGTS-FSMLQ-TMNEAY 338
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 447172216 339 -VQ----FGLTPEEAWAGVTRHAARALGRQATHGQIRAGYRADFVVWDA 382
Cdd:PRK09228 339 kVQqlqgYRLSPFQAFYLATLGGARALGLDDRIGNLAPGKEADFVVLDP 387
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
35-388 |
1.51e-06 |
|
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: 50.09 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 35 LIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHL----------VFAGNRAA------------------- 85
Cdd:COG0044 18 VLIEDGRIAAIGPDLAAP-EAAEVIDATGLLVLPGLIDLHVHLrepglehkedIETGTRAAaaggvttvvdmpntnpvtd 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 86 ------EWEQRLNGASYQHISAQGGginatvsATRACAEETlyllarERMMRLASEGVTLLEIKSGY--GLELATEEKLL 157
Cdd:COG0044 97 tpealeFKLARAEEKALVDVGPHGA-------LTKGLGENL------AELGALAEAGAVAFKVFMGSddGNPVLDDGLLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 158 RVAAKLAAENAidisptLLAAHAtpaeyrDDPDgyitLVCETMI------PQLWQKGlfdaVDLFCESVgfnvaQSERVL 231
Cdd:COG0044 164 RALEYAAEFGA------LVAVHA------EDPD----LIRGGVMnegktsPRLGLKG----RPAEAEEE-----AVARDI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 232 QTAKALGIPVkgHVEQLSLLGGAQLVSRY--QGL--SAD----HIeYLDEvgvAAMRDGGTVGVLLPGafyfLRETQRpp 303
Cdd:COG0044 219 ALAEETGARL--HIVHVSTAEAVELIREAkaRGLpvTAEvcphHL-TLTD---EDLERYGTNFKVNPP----LRTEED-- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 304 VELLRRYqvpVA------VASDFNP----------GTSPF------CSLHLAMNMACVQFGLTPEEAWAGVTRHAARALG 361
Cdd:COG0044 287 REALWEG---LAdgtidvIATDHAPhtleekelpfAEAPNgipgleTALPLLLTELVHKGRLSLERLVELLSTNPARIFG 363
|
410 420
....*....|....*....|....*..
gi 447172216 362 rQATHGQIRAGYRADFVVWDAEQPVEI 388
Cdd:COG0044 364 -LPRKGRIAVGADADLVLFDPDAEWTV 389
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
35-376 |
9.28e-06 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 47.45 E-value: 9.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 35 LIVREGHICD-----------------IVPETQLPVSG-DNIHDMQGRLVTPGLIDCHTHLVFAGNraaewEQRLNGasy 96
Cdd:PRK12394 5 ILITNGHIIDparnineinnlriindiIVDADKYPVASeTRIIHADGCIVTPGLIDYHAHVFYDGT-----EGGVRP--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 97 qHISAQGGGINATVSATRA-CAEETLYllaRERMMRLASEGV-TLLEIKSGYGLELATEEKLlrvAAKLAAENAIdispt 174
Cdd:PRK12394 77 -DMYMPPNGVTTVVDAGSAgTANFDAF---YRTVICASKVRIkAFLTVSPPGQTWSGYQENY---DPDNIDENKI----- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 175 llaaHATPAEYRDDPDGYITLVCETMIPQLWQKGLfdavdlfcesvgfnvaqsERVLQTAKALGIPVKGHVEQlSLLGGA 254
Cdd:PRK12394 145 ----HALFRQYRNVLQGLKLRVQTEDIAEYGLKPL------------------TETLRIANDLRCPVAVHSTH-PVLPMK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 255 QLVSRYQglSAD---HIEY------LDEVG--VAAMRDGGTVGVLLP---GAFYFLRETQRPPVEllrRYQVPVAVASDF 320
Cdd:PRK12394 202 ELVSLLR--RGDiiaHAFHgkgstiLTEEGavLAEVRQARERGVIFDaanGRSHFDMNVARRAIA---NGFLPDIISSDL 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 447172216 321 NPGT---SPFCSLHLAMNMAcVQFGLTPEEAWAGVTRHAARALGRQATHGQIRAGYRAD 376
Cdd:PRK12394 277 STITklaWPVYSLPWVLSKY-LALGMALEDVINACTHTPAVLMGMAAEIGTLAPGAFAD 334
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
16-77 |
1.02e-05 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 47.54 E-value: 1.02e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447172216 16 LATMDPQQQALyglvDNQALIVREGHICDIVPETQLPVSGDNIHDMQGRLVTPGLIDCHTHL 77
Cdd:PRK08203 11 IVTMDAARREI----ADGGLVVEGGRIVEVGPGGALPQPADEVFDARGHVVTPGLVNTHHHF 68
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
29-77 |
1.20e-05 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 47.29 E-value: 1.20e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447172216 29 LVDnqaLIVREGHICDIVPETQLPVSGDNIhDMQGRLVTPGLIDCHTHL 77
Cdd:PRK07583 40 LVD---IEIADGKIAAILPAGGAPDELPAV-DLKGRMVWPCFVDMHTHL 84
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
12-77 |
6.35e-05 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 44.80 E-value: 6.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447172216 12 RNIRLatMDPqqqalYGLVDNQALIVREGHICDIVPEtqLPVSGDNIHDMQGRLVTPGLIDCHTHL 77
Cdd:PRK09357 6 KNGRV--IDP-----KGLDEVADVLIDDGKIAAIGEN--IEAEGAEVIDATGLVVAPGLVDLHVHL 62
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
27-72 |
1.06e-04 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 44.20 E-value: 1.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 447172216 27 YGLVDNQALIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLID 72
Cdd:PRK11170 13 HEVLDDHAVVIADGLIEAVCPVAELP-PGIEQRDLNGAILSPGFID 57
|
|
| GDEase |
cd01303 |
Guanine deaminase (GDEase). Guanine deaminase is an aminohydrolase responsible for the ... |
303-381 |
1.51e-04 |
|
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: 43.81 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 303 PVELLRRYQVPVAVASDFNPGTSP----------FCSLHLAMNMACVQFgLTPEEAWAGVTRHAARALGRQATHGQIRAG 372
Cdd:cd01303 302 DVRKLLDAGIKVGLGTDVGGGTSFsmldtlrqayKVSRLLGYELGGHAK-LSPAEAFYLATLGGAEALGLDDKIGNFEVG 380
|
....*....
gi 447172216 373 YRADFVVWD 381
Cdd:cd01303 381 KEFDAVVID 389
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
37-384 |
1.82e-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: 43.44 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 37 VREGHICDIVPEtqLPVSGDNIHDMQGRLVTPGLIDCHTH--------------------LVFAGN-----------RAA 85
Cdd:cd01297 24 IRDGRIAAIGPI--LSTSAREVIDAAGLVVAPGFIDVHTHydgqvfwdpdlrpssrqgvtTVVLGNcgvspapanpdDLA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 86 EWEQRLNG---------------ASY-QHISAQGGGINATV----SATRacaeetlyllaRERMMRLASEgvtlleiksg 145
Cdd:cd01297 102 RLIMLMEGlvalgeglpwgwatfAEYlDALEARPPAVNVAAlvghAALR-----------RAVMGLDARE---------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 146 yglelATEEKLLRVAAKLA---AENAIDISPTLLAAH---ATPAEYrddpdgyiTLVCETMIPQlwqKGLFD-AVDLFCE 218
Cdd:cd01297 161 -----ATEEELAKMRELLRealEAGALGISTGLAYAPrlyAGTAEL--------VALARVAARY---GGVYQtHVRYEGD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 219 SVgfnVAQSERVLQTAKALGIPVkghveQLSLLG--GAQLVSRYQgLSADHIEyldevgvAAMRDGGTVGV-LLPGAFYF 295
Cdd:cd01297 225 SI---LEALDELLRLGRETGRPV-----HISHLKsaGAPNWGKID-RLLALIE-------AARAEGLQVTAdVYPYGAGS 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 296 LRETQRppveLLRRYQVPVAvaSDFNPGTSPfcslHLAMnMACVQF----------GLTPEEAWAGVTRHAARALGrQAT 365
Cdd:cd01297 289 EDDVRR----IMAHPVVMGG--SDGGALGKP----HPRS-YGDFTRvlghyvrerkLLSLEEAVRKMTGLPARVFG-LAD 356
|
410
....*....|....*....
gi 447172216 366 HGQIRAGYRADFVVWDAEQ 384
Cdd:cd01297 357 RGRIAPGYRADIVVFDPDT 375
|
|
| 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 447172216 37 VREGHICDiVPETQLPVSGDNIHDMQGRLVTPGLIDCHTHlVFAG 81
Cdd:COG3964 24 IKDGKIAA-VAKDIDAAEAKKVIDASGLYVTPGLIDLHTH-VFPG 66
|
|
| PRK09045 |
PRK09045 |
TRZ/ATZ family hydrolase; |
16-76 |
2.92e-04 |
|
TRZ/ATZ family hydrolase;
Pssm-ID: 236366 [Multi-domain] Cd Length: 443 Bit Score: 42.98 E-value: 2.92e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447172216 16 LATMDPQQQALyglvDNQALIVREGHICDIVPETQLPV--SGDNIHDMQGRLVTPGLIDCHTH 76
Cdd:PRK09045 16 IVPVEPAGVVL----EDHAVAIRDGRIVAILPRAEARAryAAAETVELPDHVLIPGLINAHTH 74
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
338-394 |
6.48e-04 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 42.01 E-value: 6.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 447172216 338 CVQFGLTPEEAWAGVTRHAARALGRqATHGQIRAGYRADFVVWD--AEQPVEIVYEPGR 394
Cdd:COG1001 279 AIELGLDPVTAIQMATLNAAEHFGL-KDLGAIAPGRRADIVLLDdlEDFKVEKVYADGK 336
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
231-390 |
6.76e-04 |
|
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: 41.44 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 231 LQTAKALGIPVKGHVEQLSllgGAQL-VSRYQGLSADHIEYLDEVGVAAMRDGGTVgvllpgafyFLRE-TQRPPVELLr 308
Cdd:cd01295 127 IQAAKKAGKPVDGHAPGLS---GEELnAYMAAGISTDHEAMTGEEALEKLRLGMYV---------MLREgSIAKNLEAL- 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 309 ryqvpVAVASDFNPGTSPFCS--LHLA-------MN----MAcVQFGLTPEEAWAGVTRHAARALGRQaTHGQIRAGYRA 375
Cdd:cd01295 194 -----LPAITEKNFRRFMFCTddVHPDdllseghLDyivrRA-IEAGIPPEDAIQMATINPAECYGLH-DLGAIAPGRIA 266
|
170
....*....|....*..
gi 447172216 376 DFVVW-DAEQP-VEIVY 390
Cdd:cd01295 267 DIVILdDLENFnITTVL 283
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
7-78 |
1.22e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 40.75 E-value: 1.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447172216 7 GDTVWRNIRLATMDPQQQALYGlvdnqALIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHLV 78
Cdd:PRK07228 1 MTILIKNAGIVTMNAKREIVDG-----DVLIEDDRIAAVGDRLDLE-DYDDHIDATGKVVIPGLIQGHIHLC 66
|
|
| PLN02795 |
PLN02795 |
allantoinase |
37-110 |
1.28e-03 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 40.91 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447172216 37 VREGHICDIVPETQLPVSGDNIH--DMQGRLVTPGLIDCHTHLVFAGNraAEWEQRLNGASyqhiSAQGGGINATV 110
Cdd:PLN02795 66 VEGGRIVSVTKEEEAPKSQKKPHvlDYGNAVVMPGLIDVHVHLNEPGR--TEWEGFPTGTK----AAAAGGITTLV 135
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
9-87 |
1.36e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 40.76 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 9 TVWRNIRLATMDPQqqalYGLVDNQALIVREGHICDIVPEtqLPVSGDNIHDMQGRLVTPGLIDCHTHLVFAGNR--AAE 86
Cdd:PRK08204 4 TLIRGGTVLTMDPA----IGDLPRGDILIEGDRIAAVAPS--IEAPDAEVVDARGMIVMPGLVDTHRHTWQSVLRgiGAD 77
|
.
gi 447172216 87 W 87
Cdd:PRK08204 78 W 78
|
|
| PRK08203 |
PRK08203 |
hydroxydechloroatrazine ethylaminohydrolase; Reviewed |
303-381 |
1.82e-03 |
|
hydroxydechloroatrazine ethylaminohydrolase; Reviewed
Pssm-ID: 236184 [Multi-domain] Cd Length: 451 Bit Score: 40.22 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 303 PVELLRRYQVPVAVASD---FNPGTSPFCSLHLAMNMACVQFG---LTPEEA--WAgvTRHAARALGRQAThGQIRAGYR 374
Cdd:PRK08203 305 PVRELRAAGVPVGLGVDgsaSNDGSNLIGEARQALLLQRLRYGpdaMTAREAleWA--TLGGARVLGRDDI-GSLAPGKL 381
|
....*..
gi 447172216 375 ADFVVWD 381
Cdd:PRK08203 382 ADLALFD 388
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
315-404 |
1.85e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 40.16 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447172216 315 AVASDFNPGtspfcSLHLAMNMACVQFGLTPEEAWAGVTRHAARALG---RqathGQIRAGYRADFVVwdaeqpveiVYE 391
Cdd:PRK15446 301 ILSSDYYPA-----SLLDAAFRLADDGGLDLPQAVALVTANPARAAGlddR----GEIAPGKRADLVR---------VRR 362
|
90
....*....|...
gi 447172216 392 PGRNPLYQRVYRG 404
Cdd:PRK15446 363 AGGLPVVRAVWRG 375
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
35-88 |
7.50e-03 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 38.53 E-value: 7.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 447172216 35 LIVREGHICDIVPETQLPvsGDNIHDMQGRLVTPGLIDCHTHLVFAGNraAEWE 88
Cdd:PRK06189 23 IGIKNGKIAEIAPEISSP--AREIIDADGLYVFPGMIDVHVHFNEPGR--THWE 72
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
10-81 |
8.01e-03 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 38.29 E-value: 8.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447172216 10 VWRNIRLatMDPQQQaLYGLVDnqaLIVREGHICDIVPETQLPvSGDNIHDMQGRLVTPGLIDCHTHlVFAG 81
Cdd:PRK09237 2 LLRGGRV--IDPANG-IDGVID---IAIEDGKIAAVAGDIDGS-QAKKVIDLSGLYVSPGWIDLHVH-VYPG 65
|
|
| PRK09229 |
PRK09229 |
N-formimino-L-glutamate deiminase; Validated |
337-385 |
9.36e-03 |
|
N-formimino-L-glutamate deiminase; Validated
Pssm-ID: 236420 [Multi-domain] Cd Length: 456 Bit Score: 37.91 E-value: 9.36e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 447172216 337 ACVQFGLTPEEAWAGVTRHAARALGRQAthGQIRAGYRADFVVWDAEQP 385
Cdd:PRK09229 351 AAAAQPSVGRRLFDAALAGGAQALGRAI--GGLAVGARADLVVLDLDHP 397
|
|
| |
