|
Name |
Accession |
Description |
Interval |
E-value |
| Isoaspartyl-dipeptidase |
cd01308 |
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of ... |
2-390 |
0e+00 |
|
Isoaspartyl dipeptidase hydrolyzes the beta-L-isoaspartyl linkages in dipeptides, as part of the degradative pathway to eliminate proteins with beta-L-isoaspartyl peptide bonds, bonds whereby the beta-group of an aspartate forms the peptide link with the amino group of the following amino acid. Formation of this bond is a spontaneous nonenzymatic reaction in nature and can profoundly effect the function of the protein. Isoaspartyl dipeptidase is an octameric enzyme that contains a binuclear zinc center in the active site of each subunit and shows a strong preference of hydrolyzing Asp-Leu dipeptides.
Pssm-ID: 238633 [Multi-domain] Cd Length: 387 Bit Score: 522.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 2 MKLIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPTELEVEVIDGTGLLLLPGFIDSHVHVLGGGGEGGFANRTPEAT 81
Cdd:cd01308 1 FTLIKNAEVYAPEYLGKKDILIAGGKILAIEDQLNLPGYENVTVVDLHGKILVPGFIDQHVHIIGGGGEGGPSTRTPEVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 82 LSGLTRYGITTVVGCLGTDGIGRDIKSLVAKIKGLREQGISAYAYTGSYQVPVRTLTGGIIDDIMMIEEIIGTGEIAISD 161
Cdd:cd01308 81 LSDLTTAGVTTVVGCLGTDGISRSMEDLLAKARALEEEGITCFVYTGSYEVPTRTITGSIRKDLLLIDKVIGVGEIAISD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 162 HRSSQPTADEFKRLCADTRVGGILSGKAGIINIHLGDSPRCMDLINQVIAETEIPATQFLPTHVNRNAALFEEAVEYAKL 241
Cdd:cd01308 161 HRSSQPTVEELARIAAEARVGGLLGGKAGIVHIHLGDGKRALSPIFELIEETEIPITQFLPTHINRTAPLFEQGVEFAKM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 242 GGAVDFTGNEDIDYWETicDEVRVSKGIKRLLDEGVSSDLFTISSDGQGSLPMFSADGVFQGMGMGQSSCLLKEVRECVE 321
Cdd:cd01308 241 GGTIDLTSSIDPQFRKE--GEVRPSEALKRLLEQGVPLERITFSSDGNGSLPKFDENGNLVGLGVGSVDTLLREVREAVK 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2668721358 322 KEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMTKDLEIDTVIAMGQVMVKKGEPIVKGAFE 390
Cdd:cd01308 319 CGDIPLEVALRVITSNVARILKLRKKGEIQPGFDADLVILDKDLDINSVIAKGQIMVRNGKLLVKGTFE 387
|
|
| isoAsp_dipep |
TIGR01975 |
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically ... |
3-390 |
4.95e-157 |
|
isoaspartyl dipeptidase IadA; The L-isoaspartyl derivative of Asp arises non-enzymatically over time as a form of protein damage. In this isomerization, the connectivity of the polypeptide changes to pass through the beta-carboxyl of the side chain. Much but not all of this damage can be repaired by protein-L-isoaspartate (D-aspartate) O-methyltransferase. This model describes the isoaspartyl dipeptidase IadA, apparently one of two such enzymes in E. coli, an enzyme that degrades isoaspartyl dipeptides and may unblock degradation of proteins that cannot be repaired. This model also describes closely related proteins from other species (e.g. Clostridium perfringens, Thermoanaerobacter tengcongensis) that we assume to be equivalent in function. This family shows homology to dihydroorotases. [Protein fate, Degradation of proteins, peptides, and glycopeptides]
Pssm-ID: 131030 Cd Length: 389 Bit Score: 447.31 E-value: 4.95e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 3 KLIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPTEL-EVEVIDGT-GLLLLPGFIDSHVHVLGGGGEGGFANRTPEA 80
Cdd:TIGR01975 2 TLLKGAEVYAPEYIGKKDILIANDKIIAIADEIPSTKDFvPNCVVVGLeGMIAVPGFIDQHVHIIGGGGEGGPTTRTPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 81 TLSGLTRYGITTVVGCLGTDGIGRDIKSLVAKIKGLREQGISAYAYTGSYQVPVRTLTGGIIDDIMMIEEIIGTGEIAIS 160
Cdd:TIGR01975 82 TLSDITKGGVTTVVGLLGTDGITRHMESLLAKARALEEEGISCYMLTGAYHVPSRTITGSVESDLLLIDKVIGVGEIAIS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 161 DHRSSQPTADEFKRLCADTRVGGILSGKAGIINIHLGDSPRCMDLINQVIAETEIPATQFLPTHVNRNAALFEEAVEYAK 240
Cdd:TIGR01975 162 DHRSAQPTVEHLTNMAAEARVGGLLGGKPGIVNFHVGDSKRALQPIYELVENTDVPITQFLPTHINRNVPLFEAGLEFAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 241 LGGAVDFTGNEDIDYWETicDEVRVSKGIKRLLDEGVSSDLFTISSDGQGSLPMFSADGVFQGMGMGQSSCLLKEVRECV 320
Cdd:TIGR01975 242 KGGTIDLTSSIDPQFRKE--GEVAPAEGIKKALEAGVPLEKVTFSSDGNGSQPFFDENGELTGLGVGSFETLFEEVREAV 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 321 EKEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMTKDLEIDTVIAMGQVMVKKGEPIVKGAFE 390
Cdd:TIGR01975 320 KDGDVPLEKALRVITSNVAGVLNLTGKGEISPGNDADLVVLDPDLRIHSVIARGKLMVKDGKACVKGTFE 389
|
|
| HutI |
COG1228 |
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport ... |
4-387 |
2.33e-20 |
|
Imidazolonepropionase or related amidohydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440841 [Multi-domain] Cd Length: 386 Bit Score: 91.56 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEYLGV---KDVFLAGGKICKIADNIELPTELEVEVIDGTGLLLLPGFIDSHVH-VLGGGGEGGFANRTPE 79
Cdd:COG1228 11 LITNATLVDGTGGGVienGTVLVEDGKIAAVGPAADLAVPAGAEVIDATGKTVLPGLIDAHTHlGLGGGRAVEFEAGGGI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 80 ATLSGLT-----------RYGITTVVGCLGTD-GIGRDIKS-LVAKIKGLReqgisAYAyTGSYQVPVRTLTGGIIDDIM 146
Cdd:COG1228 91 TPTVDLVnpadkrlrralAAGVTTVRDLPGGPlGLRDAIIAgESKLLPGPR-----VLA-AGPALSLTGGAHARGPEEAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 147 -MIEEIIGTGEIAI---SDHRSSQPTADEFKRLC-------------ADTRVGGILSGKAGIINI-HLGD-SPRCMDLin 207
Cdd:COG1228 165 aALRELLAEGADYIkvfAEGGAPDFSLEELRAILeaahalglpvaahAHQADDIRLAVEAGVDSIeHGTYlDDEVADL-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 208 qvIAETEipATQFLPThvnrnAALFEEAVEYAKLGGAVDFTGNEDIDYweticdevrvsKGIKRLLDEGVssdLFTISSD 287
Cdd:COG1228 243 --LAEAG--TVVLVPT-----LSLFLALLEGAAAPVAAKARKVREAAL-----------ANARRLHDAGV---PVALGTD 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 288 GqgslpmfsadgvfqGMGMGQSSCLLKEVRECVeKEGIPLEIAIKAITSNPAKVLCLPQK-GRIEEGMDADLCLMTKDL- 365
Cdd:COG1228 300 A--------------GVGVPPGRSLHRELALAV-EAGLTPEEALRAATINAAKALGLDDDvGSLEPGKLADLVLLDGDPl 364
|
410 420
....*....|....*....|...
gi 2668721358 366 -EIDTVIAMGQVMvKKGEPIVKG 387
Cdd:COG1228 365 eDIAYLEDVRAVM-KDGRVVDRS 386
|
|
| AllB |
COG0044 |
Dihydroorotase or related cyclic amidohydrolase [Nucleotide transport and metabolism]; ... |
4-371 |
9.11e-20 |
|
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: 90.54 E-value: 9.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPTEleVEVIDGTGLLLLPGFIDSHVHVlggggeggfanRTPEAT-- 81
Cdd:COG0044 1 LIKNGRVVDPGGLERADVLIEDGRIAAIGPDLAAPEA--AEVIDATGLLVLPGLIDLHVHL-----------REPGLEhk 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 82 ---LSGlTRY----GITTVVGCLGTDGIGRDIKSLVAKIKGLREQGISAYAYTGsyqvpvrTLTGGIIDDIMMIEEIIGT 154
Cdd:COG0044 68 ediETG-TRAaaagGVTTVVDMPNTNPVTDTPEALEFKLARAEEKALVDVGPHG-------ALTKGLGENLAELGALAEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 155 GEIAI-----SDHRSSQPTADEFKRLCADTRVGGilsgkaGIINIHlgdsprCMD--LINQ-VIAETEIPATQFLPTH-- 224
Cdd:COG0044 140 GAVAFkvfmgSDDGNPVLDDGLLRRALEYAAEFG------ALVAVH------AEDpdLIRGgVMNEGKTSPRLGLKGRpa 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 225 ------VNRNAALFE-----------------EAVEYAKLGGaVDFTG----------NEDIDYWETICdevRVS----- 266
Cdd:COG0044 208 eaeeeaVARDIALAEetgarlhivhvstaeavELIREAKARG-LPVTAevcphhltltDEDLERYGTNF---KVNpplrt 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 267 -KGIKRLLdEGVSSDLF-TISSD------GQGSLPMFSADGvfqGMGMGQS--SCLLKEVrecVEKEGIPLEIAIKAITS 336
Cdd:COG0044 284 eEDREALW-EGLADGTIdVIATDhaphtlEEKELPFAEAPN---GIPGLETalPLLLTEL---VHKGRLSLERLVELLST 356
|
410 420 430
....*....|....*....|....*....|....*
gi 2668721358 337 NPAKVLCLPQKGRIEEGMDADLCLMtkDLEIDTVI 371
Cdd:COG0044 357 NPARIFGLPRKGRIAVGADADLVLF--DPDAEWTV 389
|
|
| NagA |
cd00854 |
N-acetylglucosamine-6-phosphate deacetylase, NagA, catalyzes the hydrolysis of the N-acetyl ... |
3-374 |
1.17e-18 |
|
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: 86.48 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 3 KLIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPTEleVEVIDGTGLLLLPGFIDSHVHvlgGGGEGGFANRTPEA-- 80
Cdd:cd00854 1 LIIKNARILTPGGLEDGAVLVEDGKIVAIGPEDELEEA--DEIIDLKGQYLVPGFIDIHIH---GGGGADFMDGTAEAlk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 81 TLS-GLTRYGITTVVGCLGTDGIGrDIKSLVAKIKGLREQGISA-----YAYtGSYQVPVRTltgGIIDDIMMIEeiigt 154
Cdd:cd00854 76 TIAeALAKHGTTSFLPTTVTAPPE-EIAKALAAIAEAIAEGQGAeilgiHLE-GPFISPEKK---GAHPPEYLRA----- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 155 geiaisdhrssqPTADEFKRLCADTRvggilsgkagiinihlgdsprcmDLINQVIAETEIP-ATQFLPTHVNRN----- 228
Cdd:cd00854 146 ------------PDPEELKKWLEAAG-----------------------GLIKLVTLAPELDgALELIRYLVERGiivsi 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 229 ---AALFEEAVEyAKLGGAVDFT--------------------GNEDIDYWETICDEVRVSKGIKRLLDEGVSSDLFTIS 285
Cdd:cd00854 191 ghsDATYEQAVA-AFEAGATHVThlfnamsplhhrepgvvgaaLSDDDVYAELIADGIHVHPAAVRLAYRAKGADKIVLV 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 286 SDGQGSLPMfsADGVF----QGMGMGQSSCLLKE-------------VRECVEKEGIPLEIAIKAITSNPAKVLCLP-QK 347
Cdd:cd00854 270 TDAMAAAGL--PDGEYelggQTVTVKDGVARLADgtlagstltmdqaVRNMVKWGGCPLEEAVRMASLNPAKLLGLDdRK 347
|
410 420
....*....|....*....|....*..
gi 2668721358 348 GRIEEGMDADLCLMTKDLEIDTVIAMG 374
Cdd:cd00854 348 GSLKPGKDADLVVLDDDLNVKATWING 374
|
|
| D-aminoacylase |
cd01297 |
D-aminoacylases (N-acyl-D-Amino acid amidohydrolases) catalyze the hydrolysis of ... |
20-360 |
7.97e-17 |
|
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: 81.57 E-value: 7.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 20 DVFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHvlggggEGGFANRTPEATLSglTRYGITTVVgcLGT 99
Cdd:cd01297 21 DVGIRDGRIAAIGPILSTSAR---EVIDAAGLVVAPGFIDVHTH------YDGQVFWDPDLRPS--SRQGVTTVV--LGN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 100 DGIG---------RDIKSLVAKIKGLREQGISAYAYTGSYqvpVRTLTGGiiddIMMIEEIIGTGEIAISDH----RSSQ 166
Cdd:cd01297 88 CGVSpapanpddlARLIMLMEGLVALGEGLPWGWATFAEY---LDALEAR----PPAVNVAALVGHAALRRAvmglDARE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 167 PTADEFKRLCADTRvGGILSGKAGI----INIH-LGDSPRCMDLINQVIAETEIPATQFLPTHVNRNAALFEEAVEYAKL 241
Cdd:cd01297 161 ATEEELAKMRELLR-EALEAGALGIstglAYAPrLYAGTAELVALARVAARYGGVYQTHVRYEGDSILEALDELLRLGRE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 242 GGA-VDFT-----GNEDIDYWETICDEvrvskgIKRLLDEG--VSSDLFTIssdGQGSL----PMFSADGVfqgMGMG-- 307
Cdd:cd01297 240 TGRpVHIShlksaGAPNWGKIDRLLAL------IEAARAEGlqVTADVYPY---GAGSEddvrRIMAHPVV---MGGSdg 307
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2668721358 308 --------QSSC-----LLKEVRecvEKEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCL 360
Cdd:cd01297 308 galgkphpRSYGdftrvLGHYVR---ERKLLSLEEAVRKMTGLPARVFGLADRGRIAPGYRADIVV 370
|
|
| PRK09237 |
PRK09237 |
amidohydrolase/deacetylase family metallohydrolase; |
4-362 |
1.56e-16 |
|
amidohydrolase/deacetylase family metallohydrolase;
Pssm-ID: 236423 [Multi-domain] Cd Length: 380 Bit Score: 80.28 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEYL--GVKDVFLAGGKICKIADNIELPTEleVEVIDGTGLLLLPGFIDSHVHVlggggeggFANRTP--- 78
Cdd:PRK09237 2 LLRGGRVIDPANGidGVIDIAIEDGKIAAVAGDIDGSQA--KKVIDLSGLYVSPGWIDLHVHV--------YPGSTPygd 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 79 EATLSGLtRYGITTVV--GCLGTDGIGrdikslvakikGLREQGISA-----YAYTGSYqvpvrtLTGGI-------IDD 144
Cdd:PRK09237 72 EPDEVGV-RSGVTTVVdaGSAGADNFD-----------DFRKLTIEAsktrvLAFLNIS------RIGLLaqdeladLED 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 145 iMMIEEIIGtgeiAISDHRssqptaDEFKRLCAdtRVGGILSGKAGIinihlgdspRCMDLINQVIAETEIPatqfLPTH 224
Cdd:PRK09237 134 -IDADAVAE----AVKRNP------DFIVGIKA--RMSSSVVGDNGI---------EPLELAKAIAAEANLP----LMVH 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 225 VNRNAALFEEAVEYAKLGGAVD--FTGNEDidyweTICDEV-RVSKGIKRLLDEGVSSDL-------------------- 281
Cdd:PRK09237 188 IGNPPPSLEEILELLRPGDILThcFNGKPN-----RILDEDgELRPSVLEALERGVRLDVghgtasfsfkvaeaaiaagi 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 282 --FTISSD-GQGSL---PMFSADGV---FQGMGMgqsscllkevrecvekegiPLEIAIKAITSNPAKVLCLPQKGRIEE 352
Cdd:PRK09237 263 lpDTISTDiYCRNRingPVYSLATVmskFLALGM-------------------PLEEVIAAVTKNAADALRLPELGRLQV 323
|
410
....*....|
gi 2668721358 353 GMDADLCLMT 362
Cdd:PRK09237 324 GSDADLTLFT 333
|
|
| NagA |
COG1820 |
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism]; |
4-375 |
7.86e-16 |
|
N-acetylglucosamine-6-phosphate deacetylase [Carbohydrate transport and metabolism];
Pssm-ID: 441425 [Multi-domain] Cd Length: 373 Bit Score: 78.22 E-value: 7.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEY-LGVKDVFLAGGKICKIADNIELptelEVEVIDGTGLLLLPGFIDSHVH----VLggggeggFANRTP 78
Cdd:COG1820 1 AITNARIFTGDGvLEDGALLIEDGRIAAIGPGAEP----DAEVIDLGGGYLAPGFIDLHVHggggVD-------FMDGTP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 79 EA--TLS-GLTRYGITTVVGCLGTDGIGrDIKSLVAKIKGLREQGISAyaytgsyqvpvrtltggiiddimmieEIIGtg 155
Cdd:COG1820 70 EAlrTIArAHARHGTTSFLPTTITAPPE-DLLRALAAIAEAIEQGGGA--------------------------GILG-- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 156 eiaI--------SDHRSSQ-------PTADEFKRLCADTRvggilsgkagiinihlgdsprcmDLINQV-IA-ETEiPAT 218
Cdd:COG1820 121 ---IhlegpflsPEKKGAHppeyirpPDPEELDRLLEAAG-----------------------GLIKLVtLApELP-GAL 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 219 QFLPTHVNRN--------AALFEEAVEYAKLG----------------------GAVdFTgNEDIdYWETICDEVRVS-- 266
Cdd:COG1820 174 EFIRYLVEAGvvvslghtDATYEQARAAFEAGathvthlfnamsplhhrepgvvGAA-LD-DDDV-YAELIADGIHVHpa 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 267 --------KGIKRL-----------LDEGvSSDLftissdgqGSLPMFSADGVF---QGMGMGQSSCLLKEVRECVEKEG 324
Cdd:COG1820 251 avrlalraKGPDRLilvtdamaaagLPDG-EYEL--------GGLEVTVKDGVArlaDGTLAGSTLTMDDAVRNLVEWTG 321
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2668721358 325 IPLEIAIKAITSNPAKVLCLP-QKGRIEEGMDADLCLMTKDLEIDTVIAMGQ 375
Cdd:COG1820 322 LPLEEAVRMASLNPARALGLDdRKGSIAPGKDADLVVLDDDLNVRATWVGGE 373
|
|
| pyrC |
PRK09357 |
dihydroorotase; Validated |
1-64 |
5.58e-14 |
|
dihydroorotase; Validated
Pssm-ID: 236479 [Multi-domain] Cd Length: 423 Bit Score: 72.92 E-value: 5.58e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2668721358 1 MMKLIKGVNLYTPEYLG-VKDVFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PRK09357 1 MMILIKNGRVIDPKGLDeVADVLIDDGKIAAIGENIEAEGA---EVIDATGLVVAPGLVDLHVHL 62
|
|
| COG3964 |
COG3964 |
Predicted amidohydrolase [General function prediction only]; |
4-362 |
9.38e-14 |
|
Predicted amidohydrolase [General function prediction only];
Pssm-ID: 443164 [Multi-domain] Cd Length: 376 Bit Score: 71.74 E-value: 9.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPE--YLGVKDVFLAGGKICKIADNIELPTEleVEVIDGTGLLLLPGFIDSHVHVlggggeggFANRTP--- 78
Cdd:COG3964 3 LIKGGRVIDPAngIDGVMDIAIKDGKIAAVAKDIDAAEA--KKVIDASGLYVTPGLIDLHTHV--------FPGGTDygv 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 79 EATLSGLtRYGITTVV--GCLGTDGIGrdikslvakikGLREQGISA-----YAY---------TGSYQVPVRTLTGGII 142
Cdd:COG3964 73 DPDGVGV-RSGVTTVVdaGSAGAANFD-----------GFRKYVIDPsktrvLAFlnisgiglvGGNELQDLDDIDPDAT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 143 ddIMMIEE----IIGTgEIAISDHRSSQPTADEFKRLCAdtrvggiLSGKAGI-INIHLGDSPRCMDLINQVIAETEIpa 217
Cdd:COG3964 141 --AAAAEAnpdfIVGI-KVRASKGVVGDNGIEPLKRAKE-------AAKEAGLpLMVHIGNPPPPLDEVLDLLRPGDI-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 218 tqflPTHVNRNaalfeeaveyaKLGGAVDFTGnedidyweticdevRVSKGIKRLLDEGVSSDL---------------- 281
Cdd:COG3964 209 ----LTHCFNG-----------KPNGILDEDG--------------KVRPSVREARKRGVLFDVghggasfsfkvaepai 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 282 ------FTISSD-GQGSL--PMFSadgvfqgMGMGQSSCLlkevreCVekeGIPLEIAIKAITSNPAKVLCLPQKGRIEE 352
Cdd:COG3964 260 aqgflpDTISTDlHTRNMngPVFD-------LATVMSKFL------AL---GMPLEEVIAAVTWNPARAIGLPELGTLSV 323
|
410
....*....|
gi 2668721358 353 GMDADLCLMT 362
Cdd:COG3964 324 GADADITIFD 333
|
|
| Amidohydro_1 |
pfam01979 |
Amidohydrolase family; This family of enzymes are a a large metal dependent hydrolase ... |
52-377 |
3.29e-12 |
|
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: 67.14 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 52 LLLPGFIDSHVHVLGGGGEGGFANRT--PEATLSGLT---RYGITTVVGCLGTD--GIGRDIKSLVAKIKGLREQGiSAY 124
Cdd:pfam01979 1 IVLPGLIDAHVHLEMGLLRGIPVPPEfaYEALRLGITtmlKSGTTTVLDMGATTstGIEALLEAAEELPLGLRFLG-PGC 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 125 AYTGSYQVPVRTLTGGIIDDIMMIEEIIGTG--EIAISDHRSSQPTADEFKRLCADTRVGGILsgkagiINIHLGDSPrc 202
Cdd:pfam01979 80 SLDTDGELEGRKALREKLKAGAEFIKGMADGvvFVGLAPHGAPTFSDDELKAALEEAKKYGLP------VAIHALETK-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 203 mDLINQVIAETEIPATQFLPTHVNRNAALFEEAVEYAKLGGAVDFTGNEDID---YWETICD----EVRVSKG---IKRL 272
Cdd:pfam01979 152 -GEVEDAIAAFGGGIEHGTHLEVAESGGLLDIIKLILAHGVHLSPTEANLLAehlKGAGVAHcpfsNSKLRSGriaLRKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 273 LDEGVssdLFTISSDGQgslpmfsadgvfqgmGMGQSSCLLKEVRECVE-----KEGIPLEIAIKAITSNPAKVLCLP-Q 346
Cdd:pfam01979 231 LEDGV---KVGLGTDGA---------------GSGNSLNMLEELRLALElqfdpEGGLSPLEALRMATINPAKALGLDdK 292
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2668721358 347 KGRIEEGMDADLCL-----------MTKDLEIDTVIAMGQVM 377
Cdd:pfam01979 293 VGSIEVGKDADLVVvdldplaaffgLKPDGNVKKVIVKGKIV 334
|
|
| PRK02382 |
PRK02382 |
dihydroorotase; Provisional |
4-361 |
4.55e-12 |
|
dihydroorotase; Provisional
Pssm-ID: 179417 [Multi-domain] Cd Length: 443 Bit Score: 66.98 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEYLGVKDVFLAGGKICKIADNIElPTELEvEVIDGTGLLLLPGFIDSHVHVlggggeggfanRTP----- 78
Cdd:PRK02382 5 LLKDGRVYYNNSLQPRDVRIDGGKITAVGKDLD-GSSSE-EVIDARGMLLLPGGIDVHVHF-----------REPgythk 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 79 EATLSGlTRY----GITTVVGCLGT-----DGIGRDIKSLVAKIKGLREQGISayaytgsyqvpvrtltGGIIDDIMMIE 149
Cdd:PRK02382 72 ETWYTG-SRSaaagGVTTVVDQPNTdpptvDGESFDEKAELAARKSIVDFGIN----------------GGVTGNWDPLE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 150 EI-------IG-------TGEIAISdhrssqptADEFKRLCADTRVGGILsgkagiINIHLGDSPRCMDLINQVIAETEI 215
Cdd:PRK02382 135 SLwergvfaLGeifmadsTGGMGID--------EELFEEALAEAARLGVL------ATVHAEDEDLFDELAKLLKGDADA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 216 PA-TQFLPTHVNRNAAlfEEAVEYAKLGG------------AVDFTGNEDI-------------DYWETICD------EV 263
Cdd:PRK02382 201 DAwSAYRPAAAEAAAV--ERALEVASETGarihiahistpeGVDAARREGItcevtphhlflsrRDWERLGTfgkmnpPL 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 264 RVSKGIKRLLDEGVSSDLFTISSD------GQGSLPMFSAD----GVFQGMGMgqsscLLKEVRecveKEGIPLEIAIKA 333
Cdd:PRK02382 279 RSEKRREALWERLNDGTIDVVASDhaphtrEEKDADIWDAPsgvpGVETMLPL-----LLAAVR----KNRLPLERVRDV 349
|
410 420
....*....|....*....|....*...
gi 2668721358 334 ITSNPAKVLCLPQKGRIEEGMDADLCLM 361
Cdd:PRK02382 350 TAANPARIFGLDGKGRIAEGYDADLVLV 377
|
|
| PRK06189 |
PRK06189 |
allantoinase; Provisional |
4-360 |
4.57e-12 |
|
allantoinase; Provisional
Pssm-ID: 235732 [Multi-domain] Cd Length: 451 Bit Score: 67.03 E-value: 4.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHVLGGGGEGGFANRTPEATLS 83
Cdd:PRK06189 6 IIRGGKVVTPEGVYRADIGIKNGKIAEIAPEISSPAR---EIIDADGLYVFPGMIDVHVHFNEPGRTHWEGFATGSAALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 84 --GLTRY------GITTVVgclgtdgigrDIKSLVAKIKGLREQGISAYAYTGSyqvpvrtLTGGIIDDImmiEEIIGTG 155
Cdd:PRK06189 83 agGCTTYfdmplnSIPPTV----------TREALDAKAELARQKSAVDFALWGG-------LVPGNLEHL---RELAEAG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 156 EIAISDHRSsQPTADEFkRLCAD-TRVGGILSGKA--GIINIHLGDSPRCMDLINQVIAETEIPATQFL---PTHVNRNA 229
Cdd:PRK06189 143 VIGFKAFMS-NSGTDEF-RSSDDlTLYEGMKEIAAlgKILALHAESDALTRHLTTQARQQGKTDVRDYLesrPVVAELEA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 230 AlfEEAVEYAKLGGA-----------------------VD-----------FTGN--EDIDYWETICDEVRVSKGIKRLL 273
Cdd:PRK06189 221 V--QRALLYAQETGCplhfvhissgkavaliaeakkrgVDvsvetcphyllFTEEdfERIGAVAKCAPPLRSRSQKEELW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 274 DEGVSSDLFTISSDGQGSLP-------MFSADGvfqGMGMGQSScLLKEVRECVEKEGIPLEIAIKAITSNPAKVLCLPQ 346
Cdd:PRK06189 299 RGLLAGEIDMISSDHSPCPPelkegddFFLVWG---GISGGQST-LLVMLTEGYIERGIPLETIARLLATNPAKRFGLPQ 374
|
410
....*....|....
gi 2668721358 347 KGRIEEGMDADLCL 360
Cdd:PRK06189 375 KGRLEVGADADFVL 388
|
|
| D-hydantoinase |
TIGR02033 |
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily ... |
3-372 |
5.29e-11 |
|
D-hydantoinase; This model represents the D-hydantoinase (dihydropyrimidinase) which primarily converts 5,6-dihydrouracil to 3-ureidopropanoate but also acts on dihydrothymine and hydantoin. The enzyme is a metalloenzyme.
Pssm-ID: 273937 [Multi-domain] Cd Length: 454 Bit Score: 63.94 E-value: 5.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 3 KLIKG---VNLYTPEYLgvkDVFLAGGKICKIADNIELPteLEVEVIDGTGLLLLPGFIDSHVHVLGGGGEGGFANRTPE 79
Cdd:TIGR02033 1 LLIKGgtvVNADDVFQA---DVLIEGGKIVAVGDNLIPP--DAVEVIDATGKYVLPGGIDVHTHLEMPFGGTTTADDFFT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 80 ATLSGLTRyGITTVVGcLGTDGIGRDIKSLVAKIKGLREqGISAYAYTgsYQVPVRTLTGGIIDDI--MMIEEIIGTGEI 157
Cdd:TIGR02033 76 GTKAAAAG-GTTTIID-FVVPEKGSSLTEALETWHEKAE-GKSVIDYG--FHMDITHWNDSVLEEHipEVKEEGINSFKV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 158 AISDHRSSQPTADE----FKR-------LCADTRVGGILS---------GKAGIINIHLGDSPRC-MDLINQVIAETEIP 216
Cdd:TIGR02033 151 FMAYKNLLMVDDEElfeiLKRlkelgalLQVHAENGDIIAelqarmlaqGITGPEYHALSRPPELeAEAVARAITLAALA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 217 ATQFLPTHVNRNAALfeEAVEYAKLGGAVDFT-------GNEDIDYWETICD-----------EVRVSKGIKRLLDEG-- 276
Cdd:TIGR02033 231 DAPLYVVHVSTKDAA--DEIAQARKKGQPVFGetcpqylVLDDTHYDKPGFEgakyvcspplrEPEDQDALWSALSSGal 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 277 --VSSDLFTISSDGQGSLPM--FSAdgVFQGM-GMGQSSCLLKEvrECVEKEGIPLEIAIKAITSNPAKVLCL-PQKGRI 350
Cdd:TIGR02033 309 qtVGSDHCTFNFAQKKAIGKddFTK--IPNGGpGVEERMSLLFD--EGVAKGRITLEKFVEVTSTNPAKIFNLyPRKGTI 384
|
410 420
....*....|....*....|..
gi 2668721358 351 EEGMDADLCLMtkDLEIDTVIA 372
Cdd:TIGR02033 385 AVGSDADIVIW--DPNRTTVIS 404
|
|
| D-HYD |
cd01314 |
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases ... |
3-94 |
2.97e-10 |
|
D-hydantoinases (D-HYD) also called dihydropyrimidases (DHPase) and related proteins; DHPases are a family of enzymes that catalyze the reversible hydrolytic ring opening of the amide bond in five- or six-membered cyclic diamides, like dihydropyrimidine or hydantoin. The hydrolysis of dihydropyrimidines is the second step of reductive catabolism of pyrimidines in human. The hydrolysis of 5-substituted hydantoins in microorganisms leads to enantiomerically pure N-carbamyl amino acids, which are used for the production of antibiotics, peptide hormones, pyrethroids, and pesticides. HYDs are classified depending on their stereoselectivity. This family also includes collapsin response regulators (CRMPs), cytosolic proteins involved in neuronal differentiation and axonal guidance which have strong homology to DHPases, but lack most of the active site residues.
Pssm-ID: 238639 [Multi-domain] Cd Length: 447 Bit Score: 61.46 E-value: 2.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 3 KLIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPteLEVEVIDGTGLLLLPGFIDSHVHV----LGGGGEGGFANRTp 78
Cdd:cd01314 1 LIIKNGTIVTADGSFKADILIEDGKIVAIGPNLEAP--GGVEVIDATGKYVLPGGIDPHTHLelpfMGTVTADDFESGT- 77
|
90
....*....|....*.
gi 2668721358 79 EATLSGltryGITTVV 94
Cdd:cd01314 78 RAAAAG----GTTTII 89
|
|
| Met_dep_hydrolase_B |
cd01307 |
Metallo-dependent hydrolases, subgroup B is part of the superfamily of metallo-dependent ... |
20-372 |
7.61e-10 |
|
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: 59.65 E-value: 7.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 20 DVFLAGGKICKIADNIelPTELEVEVIDGTGLLLLPGFIDSHVHVLggggeggfanrtPEATLSGL------TRYGITTV 93
Cdd:cd01307 1 DVAIENGKIAAVGAAL--AAPAATQIVDAGGCYVSPGWIDLHVHVY------------QGGTRYGDrpdmigVKSGVTTV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 94 V--GCLGTDgigrdikslvaKIKGLREQGISA-----YAYTGSYQVpvrtltggiiddimmieeiigtGEIAIsdHRSSQ 166
Cdd:cd01307 67 VdaGSAGAD-----------NIDGFRYTVIERsatrvYAFLNISRV----------------------GLVAQ--DELPD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 167 PTADEFKRLCA------DTRVGgiLSGKAGIINIhlGDSP-RCMDLINQVIAETEIPatqfLPTHVNRNAALFEEAVEYA 239
Cdd:cd01307 112 PDNIDEDAVVAaareypDVIVG--LKARASKSVV--GEWGiKPLELAKKIAKEADLP----LMVHIGSPPPILDEVVPLL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 240 KLGGAVD--FTG--NEDIDYWETICDEVR--VSKGI----------------KRLLDEGVSSDlfTISSDGQGSlpmFSA 297
Cdd:cd01307 184 RRGDVLThcFNGkpNGIVDEEGEVLPLVRraRERGVifdvghgtasfsfrvaRAAIAAGLLPD--TISSDIHGR---NRT 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 298 DG-VFQGMgmgqsscllkevrECVEKE---GIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMT--------KDL 365
Cdd:cd01307 259 NGpVYALA-------------TTLSKLlalGMPLEEVIEAVTANPARMLGLAEIGTLAVGYDADLTVFDlkdgrvelVDS 325
|
....*..
gi 2668721358 366 EIDTVIA 372
Cdd:cd01307 326 EGDTLIA 332
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
57-340 |
8.68e-10 |
|
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: 59.27 E-value: 8.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 57 FIDSHVHVLGGGGEGGFANR------------TPEATLSGLT---RYGITTVVGCLGTDGIGRDIKSLVAKIKGLREQ-G 120
Cdd:cd01292 1 FIDTHVHLDGSALRGTRLNLelkeaeelspedLYEDTLRALEallAGGVTTVVDMGSTPPPTTTKAAIEAVAEAARASaG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 121 ISAYAYTGSYQVPVRTLTGGIIDDIMMIEEIIGTGEIAI---SDHRSSQPTADEFKRLCADTRVGGIlsgkagIINIHLG 197
Cdd:cd01292 81 IRVVLGLGIPGVPAAVDEDAEALLLELLRRGLELGAVGLklaGPYTATGLSDESLRRVLEEARKLGL------PVVIHAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 198 DSPRCMDLINQVIAETEIPATqFLPTHVNRNAALFEEAVEYAKLGGAVDFTGNEDIDYWETicdevrVSKGIKRLLDEGV 277
Cdd:cd01292 155 ELPDPTRALEDLVALLRLGGR-VVIGHVSHLDPELLELLKEAGVSLEVCPLSNYLLGRDGE------GAEALRRLLELGI 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2668721358 278 ssdLFTISSDGQgslPMFSADGVFQGMGMGQSSCLLkevrecvekeGIPLEIAIKAITSNPAK 340
Cdd:cd01292 228 ---RVTLGTDGP---PHPLGTDLLALLRLLLKVLRL----------GLSLEEALRLATINPAR 274
|
|
| Cyclic_amidohydrolases |
cd01302 |
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and ... |
51-392 |
2.57e-09 |
|
Cyclic amidohydrolases, including hydantoinase, dihydropyrimidinase, allantoinase, and dihydroorotase, are involved in the metabolism of pyrimidines and purines, sharing the property of hydrolyzing the cyclic amide bond of each substrate to the corresponding N-carbamyl amino acids. Allantoinases catalyze the degradation of purines, while dihydropyrimidinases and hydantoinases, a microbial counterpart of dihydropyrimidinase, are involved in pyrimidine degradation. Dihydroorotase participates in the de novo synthesis of pyrimidines.
Pssm-ID: 238627 [Multi-domain] Cd Length: 337 Bit Score: 58.17 E-value: 2.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 51 LLLLPGFIDSHVHV---LGGGGEGGFANRTpEATLSGltryGITTVVGCLGTDGIGRDIKSLVAKIKGLREQGISAYAYT 127
Cdd:cd01302 1 LLVLPGFIDIHVHLrdpGGTTYKEDFESGS-RAAAAG----GVTTVIDMPNTGPPPIDLPAIELKIKLAEESSYVDFSFH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 128 G--SYQVPVRTLTGGIIDDI-----MMIEEiiGTGEIAISD---HRSSQPTADEFKRLCADTRVGGILSGKAGI-INI-H 195
Cdd:cd01302 76 AgiGPGDVTDELKKLFDAGInslkvFMNYY--FGELFDVDDgtlMRTFLEIASRGGPVMVHAERAAQLAEEAGAnVHIaH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 196 LGdSPRCMDLINQ-------VIAETEipatqflPTHvnrnaaLFEEAVEYAKLGGAVDFT----GNEDIDY-WETICDEV 263
Cdd:cd01302 154 VS-SGEALELIKFaknkgvkVTCEVC-------PHH------LFLDESMLRLNGAWGKVNpplrSKEDREAlWEGVKNGK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 264 rvskgIKRLLDEGVSSDLFTISSDGQGSLPMFSADGVfQGMgmgqSSCLLKEVRecveKEGIPLEIAIKAITSNPAKVLC 343
Cdd:cd01302 220 -----IDTIASDHAPHSKEEKESGKDIWKAPPGFPGL-ETR----LPILLTEGV----KRGLSLETLVEILSENPARIFG 285
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2668721358 344 LPQKGRIEEGMDADLCLMtkDLEIDTVIAMGQVMVKKGepivKGAFEGQ 392
Cdd:cd01302 286 LYPKGTIAVGYDADLVIV--DPKKEWKVTAEEIESKAD----WTPFEGM 328
|
|
| SsnA |
COG0402 |
Cytosine/adenosine deaminase or related metal-dependent hydrolase [Nucleotide transport and ... |
4-379 |
2.73e-09 |
|
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: 58.30 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYT--PEYLGVKDVFLA--GGKICKIADNIELPTELE-VEVIDGTGLLLLPGFIDSHVHV-------------- 64
Cdd:COG0402 3 LIRGAWVLTmdPAGGVLEDGAVLveDGRIAAVGPGAELPARYPaAEVIDAGGKLVLPGLVNTHTHLpqtllrgladdlpl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 65 ---LGGGGEGGFANRTPE----ATLSGLT---RYGITTV-----VGCLGTDGIgrdikslvakIKGLREQGISAYAYTGS 129
Cdd:COG0402 83 ldwLEEYIWPLEARLDPEdvyaGALLALAemlRSGTTTVadfyyVHPESADAL----------AEAAAEAGIRAVLGRGL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 130 YQVPVRTLTGGIIDDIM-----MIEEIIGTG----EIAISDH--RSSqpTADEFKRLCAdtrvggiLSGKAGI-INIHLG 197
Cdd:COG0402 153 MDRGFPDGLREDADEGLadserLIERWHGAAdgriRVALAPHapYTV--SPELLRAAAA-------LARELGLpLHTHLA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 198 DSPrcmDLINQVIAETEIPATQFLpthvNRNAALFEEAVeyakLGGAVDFTGNEdidyWETICD-----------EVRVS 266
Cdd:COG0402 224 ETR---DEVEWVLELYGKRPVEYL----DELGLLGPRTL----LAHCVHLTDEE----IALLAEtgasvahcptsNLKLG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 267 KGI---KRLLDEGVSsdlFTISSDGQGSLPMFSadgvfqgmgmgqsscLLKEVR--ECVEK------EGIPLEIAIKAIT 335
Cdd:COG0402 289 SGIapvPRLLAAGVR---VGLGTDGAASNNSLD---------------MFEEMRlaALLQRlrggdpTALSAREALEMAT 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2668721358 336 SNPAKVLCLPQK-GRIEEGMDADLCLMtkDLE----------------------IDTVIAMGQVMVK 379
Cdd:COG0402 351 LGGARALGLDDEiGSLEPGKRADLVVL--DLDaphlaplhdplsalvyaadgrdVRTVWVAGRVVVR 415
|
|
| pyrC_multi |
TIGR00857 |
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of ... |
20-366 |
6.76e-09 |
|
dihydroorotase, multifunctional complex type; In contrast to the homodimeric type of dihydroorotase found in E. coli, this class tends to appear in a large, multifunctional complex with aspartate transcarbamoylase. Homologous domains appear in multifunctional proteins of higher eukaryotes. In some species, including Pseudomonas putida and P. aeruginosa, this protein is inactive but is required as a non-catalytic subunit of aspartate transcarbamoylase (ATCase). In these species, a second, active dihydroorotase is also present. The seed for this model does not include any example of the dihydroorotase domain of eukaryotic multidomain pyrimidine synthesis proteins. All proteins described by this model should represent active and inactive dihydroorotase per se and functionally equivalent domains of multifunctional proteins from higher eukaryotes, but exclude related proteins such as allantoinase. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273302 [Multi-domain] Cd Length: 411 Bit Score: 57.07 E-value: 6.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 20 DVFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHVlggggeGGFANRTPEATLSGL---TRYGITTVVGC 96
Cdd:TIGR00857 7 DILVEGGRIKKIGKLRIPPDA---EVIDAKGLLVLPGFIDLHVHL------RDPGEEYKEDIESGSkaaAHGGFTTVADM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 97 LGTDGIGRDIKSLVAKIKGLREQGISAYAYTGSyqVPVRtLTGGIIDDIMMIEEIIGTGEIAISD----------HRSSQ 166
Cdd:TIGR00857 78 PNTKPPIDTPETLEWKLQRLKKVSLVDVHLYGG--VTQG-NQGKELTEAYELKEAGAVGRMFTDDgsevqdilsmRRALE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 167 PTADEFKRLCA-----DTRVGG-ILSGKAGIINIHLGDSPRCMDL-INQVIAETEIPATQFLPTHVNRNAALfeEAVEYA 239
Cdd:TIGR00857 155 YAAIAGVPIALhaedpDLIYGGvMHEGPSAAQLGLPARPPEAEEVaVARLLELAKHAGCPVHICHISTKESL--ELIVKA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 240 K---LGGAVDFT------GNEDIDYWETIcdeVRV-----SKGIKRLLDEGVSSDLF-TISSDGQGSL----PMFSADGV 300
Cdd:TIGR00857 233 KsqgIKITAEVTphhlllSEEDVARLDGN---GKVnpplrEKEDRLALIEGLKDGIIdIIATDHAPHTleekTKEFAAAP 309
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2668721358 301 FQGMGMGQS-SCLLKEVRecveKEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMtkDLE 366
Cdd:TIGR00857 310 PGIPGLETAlPLLLQLLV----KGLISLKDLIRMLSINPARIFGLPDKGTLEEGNPADITVF--DLK 370
|
|
| PRK08323 |
PRK08323 |
phenylhydantoinase; Validated |
1-63 |
3.75e-08 |
|
phenylhydantoinase; Validated
Pssm-ID: 236240 [Multi-domain] Cd Length: 459 Bit Score: 54.79 E-value: 3.75e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2668721358 1 MMKLIKGVNLYTPEYLGVKDVFLAGGKICKIADNIElpteleVEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK08323 1 MSTLIKNGTVVTADDTYKADVLIEDGKIAAIGANLG------DEVIDATGKYVMPGGIDPHTH 57
|
|
| ATZ_TRZ_like |
cd01298 |
TRZ/ATZ family contains enzymes from the atrazine degradation pathway and related hydrolases. ... |
4-383 |
1.15e-07 |
|
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: 53.36 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEYLGV---KDVFLAGGKICKIADNIELPTELEVEVIDGTGLLLLPGFIDSHVHV---------------- 64
Cdd:cd01298 2 LIRNGTIVTTDPRRVledGDVLVEDGRIVAVGPALPLPAYPADEVIDAKGKVVMPGLVNTHTHLamtllrgladdlplme 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 65 -LGGGGEGGFANRTPE----ATLSGLT---RYGITTVV--GCLGTDGIgrdikslvakIKGLREQGISAYAYTGSYQVP- 133
Cdd:cd01298 82 wLKDLIWPLERLLTEEdvylGALLALAemiRSGTTTFAdmYFFYPDAV----------AEAAEELGIRAVLGRGIMDLGt 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 134 --VRTLTGGIIDDIMMIEEIIGTGE----IAISDHrsSQPTA-DEFKRLCADtrvggiLSGKAGI-INIHLgdsprcmdl 205
Cdd:cd01298 152 edVEETEEALAEAERLIREWHGAADgrirVALAPH--APYTCsDELLREVAE------LAREYGVpLHIHL--------- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 206 inqviAETEIPATQFLPTHVNRNAALFEEaVEYAK----LGGAVDFTgNEDIDYW-ET-------ICDEVRVSKGI---K 270
Cdd:cd01298 215 -----AETEDEVEESLEKYGKRPVEYLEE-LGLLGpdvvLAHCVWLT-DEEIELLaETgtgvahnPASNMKLASGIapvP 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 271 RLLDEGVSsdlFTISSDGQGS---LPMFSAdgvfqgmgMGQSScLLKEVRECVEKeGIPLEIAIKAITSNPAKVLCLPQK 347
Cdd:cd01298 288 EMLEAGVN---VGLGTDGAASnnnLDMFEE--------MRLAA-LLQKLAHGDPT-ALPAEEALEMATIGGAKALGLDEI 354
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2668721358 348 GRIEEGMDADLCLMTKDL--------------------EIDTVIAMGQVMVKKGEP 383
Cdd:cd01298 355 GSLEVGKKADLILIDLDGphllpvhdpishlvysanggDVDTVIVNGRVVMEDGEL 410
|
|
| COG3653 |
COG3653 |
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and ... |
4-103 |
1.63e-07 |
|
N-acyl-D-aspartate/D-glutamate deacylase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442870 [Multi-domain] Cd Length: 528 Bit Score: 53.25 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLY----TPEYLGvkDVFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHVlgggGEGGFANRtpe 79
Cdd:COG3653 5 LIRGGTVVdgtgAPPFRA--DVAIKGGRIVAVGDLAAAEAA---RVIDATGLVVAPGFIDIHTHY----DLQLLWDP--- 72
|
90 100
....*....|....*....|....
gi 2668721358 80 aTLSGLTRYGITTVVgcLGTDGIG 103
Cdd:COG3653 73 -RLEPSLRQGVTTVV--MGNCGVS 93
|
|
| Bact_CD |
cd01293 |
Bacterial cytosine deaminase and related metal-dependent hydrolases. Cytosine deaminases (CDs) ... |
4-63 |
1.81e-07 |
|
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: 52.63 E-value: 1.81e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEyLGVKDVFLAGGKICKIADNIELPTEleVEVIDGTGLLLLPGFIDSHVH 63
Cdd:cd01293 1 LLRNARLADGG-TALVDIAIEDGRIAAIGPALAVPPD--AEEVDAKGRLVLPAFVDPHIH 57
|
|
| PRK09236 |
PRK09236 |
dihydroorotase; Reviewed |
1-63 |
2.10e-07 |
|
dihydroorotase; Reviewed
Pssm-ID: 181716 Cd Length: 444 Bit Score: 52.57 E-value: 2.10e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2668721358 1 MMK-LIKGVNLYTPEYLGVKDVFLAGGKICKIADNIE-LPTElevEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK09236 1 MKRiLIKNARIVNEGKIFEGDVLIENGRIAKIASSISaKSAD---TVIDAAGRYLLPGMIDDQVH 62
|
|
| PRK09060 |
PRK09060 |
dihydroorotase; Validated |
4-63 |
3.91e-07 |
|
dihydroorotase; Validated
Pssm-ID: 181632 [Multi-domain] Cd Length: 444 Bit Score: 51.84 E-value: 3.91e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 4 LIKGVNLYTPEYLGVKDVFLAGGKICKIADnieLPTELEVEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK09060 8 ILKGGTVVNPDGEGRADIGIRDGRIAAIGD---LSGASAGEVIDCRGLHVLPGVIDSQVH 64
|
|
| L-HYD_ALN |
cd01315 |
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the ... |
2-371 |
6.80e-07 |
|
L-Hydantoinases (L-HYDs) and Allantoinase (ALN); L-Hydantoinases are a member of the dihydropyrimidinase family, which catalyzes the reversible hydrolytic ring opening of dihydropyrimidines and hydantoins (five-membered cyclic diamides used in biotechnology). But L-HYDs differ by having an L-enantio specificity and by lacking activity on possible natural substrates such as dihydropyrimidines. Allantoinase catalyzes the hydrolytic cleavage of the five-member ring of allantoin (5-ureidohydantoin) to form allantoic acid.
Pssm-ID: 238640 [Multi-domain] Cd Length: 447 Bit Score: 51.14 E-value: 6.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 2 MKLIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPTEleVEVIDGTGLLLLPGFIDSHVHVLGGGGEG--GFANRTpE 79
Cdd:cd01315 1 DLVIKNGRVVTPDGVREADIAVKGGKIAAIGPDIANTEA--EEVIDAGGLVVMPGLIDTHVHINEPGRTEweGFETGT-K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 80 ATLSGltryGITTVV----GCL--GTDGIGRDIKSLVAKIKglreqgisAYAYTGSYqvpvrtltGGIIDD-IMMIEEII 152
Cdd:cd01315 78 AAAAG----GITTIIdmplNSIppTTTVENLEAKLEAAQGK--------LHVDVGFW--------GGLVPGnLDQLRPLD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 153 GTGEIA----ISDhrssqPTADEFKRLCADTRVGG--ILSGKAGIINIHLGDSPRCMDLINQVIAE-------------- 212
Cdd:cd01315 138 EAGVVGfkcfLCP-----SGVDEFPAVDDEQLEEAmkELAKTGSVLAVHAENPEITEALQEQAKAKgkrdyrdylasrpv 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 213 -TEIPATQFLPT------------HVNRNAALfeEAVEYAKLGGA----------VDFTGN--EDIDYWETICDEVRVSK 267
Cdd:cd01315 213 fTEVEAIQRILLlaketgcrlhivHLSSAEAV--PLIREARAEGVdvtvetcphyLTFTAEdvPDGGTEFKCAPPIRDAA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 268 GIKRLLDEGVSSDLFTISSDGQGSLP---------MFSADGVFQGMGmgqsSCLLKEVRECVEKEGIPLEIAIKAITSNP 338
Cdd:cd01315 291 NQEQLWEALENGDIDMVVSDHSPCTPelkllgkgdFFKAWGGISGLQ----LGLPVMLTEAVNKRGLSLEDIARLMCENP 366
|
410 420 430
....*....|....*....|....*....|....
gi 2668721358 339 AKVLCL-PQKGRIEEGMDADLCLMtkDLEIDTVI 371
Cdd:cd01315 367 AKLFGLsHQKGRIAVGYDADFVVW--DPEEEFTV 398
|
|
| PRK08044 |
PRK08044 |
allantoinase AllB; |
252-364 |
1.05e-06 |
|
allantoinase AllB;
Pssm-ID: 169193 [Multi-domain] Cd Length: 449 Bit Score: 50.62 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 252 DIDYWETICDEVRVSKGIKRLLD-EGVSSDLFT-----ISSDGQGSLPMFSADGVFQGMG--MGQSSCLLKEVRECVEKE 323
Cdd:PRK08044 274 DTDQFEEIGTLAKCSPPIRDLENqKGMWEKLFNgeidcLVSDHSPCPPEMKAGNIMEAWGgiAGLQNCMDVMFDEAVQKR 353
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2668721358 324 GIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMTKD 364
Cdd:PRK08044 354 GMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPN 394
|
|
| PRK07575 |
PRK07575 |
dihydroorotase; Provisional |
1-63 |
1.15e-06 |
|
dihydroorotase; Provisional
Pssm-ID: 236055 [Multi-domain] Cd Length: 438 Bit Score: 50.44 E-value: 1.15e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2668721358 1 MMK-LIKGVNLYTPE---YLGvkDVFLAGGKICKIADniELPTELEVEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK07575 2 MMSlLIRNARILLPSgelLLG--DVLVEDGKIVAIAP--EISATAVDTVIDAEGLTLLPGVIDPQVH 64
|
|
| Met_dep_hydrolase_A |
cd01299 |
Metallo-dependent hydrolases, subgroup A is part of the superfamily of metallo-dependent ... |
43-364 |
1.38e-06 |
|
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: 49.60 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 43 VEVIDGTGLLLLPGFIDSHVHVLGGGGEGGFANRTPEA--------TLSGLTRYGITTVVGCLGTD-GIGRDikslvAKI 113
Cdd:cd01299 1 AQVIDLGGKTLMPGLIDAHTHLGSDPGDLPLDLALPVEyrtiratrQARAALRAGFTTVRDAGGADyGLLRD-----AID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 114 KGLRE--------QGISAyayTGSY-------QVPVRTLTGGIIDDI--------MMIEE------IIGTGE-IAISDH- 162
Cdd:cd01299 76 AGLIPgprvfasgRALSQ---TGGHgdprglsGLFPAGGLAAVVDGVeevraavrEQLRRgadqikIMATGGvLSPGDPp 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 163 RSSQPTADEFKRLCADTRVGGIL-------------SGKAGIINI-H-LGDSPRCMDLI--NQVIAETEIPATQFLPTHV 225
Cdd:cd01299 153 PDTQFSEEELRAIVDEAHKAGLYvaahaygaeairrAIRAGVDTIeHgFLIDDETIELMkeKGIFLVPTLATYEALAAEG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 226 NRnAALFEEAVEYAKLGGAvdftgnedidyweticdevRVSKGIKRLLDEGV----SSDLFTissdgqgslpmfsaDGVF 301
Cdd:cd01299 233 AA-PGLPADSAEKVALVLE-------------------AGRDALRRAHKAGVkiafGTDAGF--------------PVPP 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2668721358 302 QGMgmgqsscLLKEVRECVEKEGIPLEiAIKAITSNPAKVLCLPQK-GRIEEGMDADLCLMTKD 364
Cdd:cd01299 279 HGW-------NARELELLVKAGGTPAE-ALRAATANAAELLGLSDElGVIEAGKLADLLVVDGD 334
|
|
| PhnM |
cd01306 |
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is ... |
312-374 |
2.32e-06 |
|
PhnM is believed to be a subunit of the membrane associated C-P lyase complex. C-P lyase is thought to catalyze the direct cleavage of inactivated C-P bonds to yield inorganic phosphate and the corresponding hydrocarbons. It is responsible for cleavage of alkylphosphonates, which are utilized as sole phosphorus sources by many bacteria.
Pssm-ID: 238631 Cd Length: 325 Bit Score: 48.82 E-value: 2.32e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2668721358 312 LLKEVRECVEKEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMTKDL---EIDTVIAMG 374
Cdd:cd01306 260 LLHAAFRLADLGGWSLPEAVALVSANPARAVGLTDRGSIAPGKRADLILVDDMDgvpVVRTVWRGG 325
|
|
| PRK05985 |
PRK05985 |
cytosine deaminase; Provisional |
20-63 |
2.36e-06 |
|
cytosine deaminase; Provisional
Pssm-ID: 180337 [Multi-domain] Cd Length: 391 Bit Score: 49.16 E-value: 2.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2668721358 20 DVFLAGGKICKIADNieLPTELEVEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK05985 18 DILIRDGRIAAIGPA--LAAPPGAEVEDGGGALALPGLVDGHIH 59
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
316-386 |
2.44e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 49.33 E-value: 2.44e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2668721358 316 VRECVEkEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMT--KDLEIDTVIAMGQVMVKKGEPIVK 386
Cdd:COG1001 276 VRRAIE-LGLDPVTAIQMATLNAAEHFGLKDLGAIAPGRRADIVLLDdlEDFKVEKVYADGKLVAEDGKLLVD 347
|
|
| AdeC |
COG1001 |
Adenine deaminase [Nucleotide transport and metabolism]; |
4-64 |
3.24e-06 |
|
Adenine deaminase [Nucleotide transport and metabolism];
Pssm-ID: 440625 [Multi-domain] Cd Length: 559 Bit Score: 48.94 E-value: 3.24e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2668721358 4 LIKG---VNLYTPEYLgVKDVFLAGGKICKIADNIELPTEleveVIDGTGLLLLPGFIDSHVHV 64
Cdd:COG1001 8 VIKNgrlVNVFTGEIL-EGDIAIAGGRIAGVGDYIGEATE----VIDAAGRYLVPGFIDGHVHI 66
|
|
| PRK08204 |
PRK08204 |
hypothetical protein; Provisional |
20-126 |
4.36e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 181288 [Multi-domain] Cd Length: 449 Bit Score: 48.46 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 20 DVFLAGGKICKIADNIELPtelEVEVIDGTGLLLLPGFIDSHVHV-------------LGGGGEGGFAN----RTPE--- 79
Cdd:PRK08204 25 DILIEGDRIAAVAPSIEAP---DAEVVDARGMIVMPGLVDTHRHTwqsvlrgigadwtLQTYFREIHGNlgpmFRPEdvy 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2668721358 80 -ATLSGLTRY---GITTVVG-CLgtdgIGRDIKSLVAKIKGLREQGISA-YAY 126
Cdd:PRK08204 102 iANLLGALEAldaGVTTLLDwSH----INNSPEHADAAIRGLAEAGIRAvFAH 150
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
20-83 |
5.50e-06 |
|
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: 48.07 E-value: 5.50e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2668721358 20 DVFLAGGKICKIADNIELPTELE--VEVIDGTGLLLLPGFIDSHVHVLGGGGEGGFANRTPEATLS 83
Cdd:cd01300 1 AVAVRDGRIVAVGSDAEAKALKGpaTEVIDLKGKTVLPGFIDSHSHLLLGGLSLLWLDLSGVTSKE 66
|
|
| Amidohydro_3 |
pfam07969 |
Amidohydrolase family; |
79-385 |
6.19e-06 |
|
Amidohydrolase family;
Pssm-ID: 400360 [Multi-domain] Cd Length: 464 Bit Score: 47.91 E-value: 6.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 79 EATLSGLTRYGITTVVGCLGTDGIGRDIKSLVA-----KIKGLREQGISAYAYTGSYQVPVRTLtgGIIDDIMMIEEIIG 153
Cdd:pfam07969 154 AAALAALPGFGITSVDGGGGNVHSLDDYEPLREltaaeKLKELLDAPERLGLPHSIYELRIGAM--KLFADGVLGSRTAA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 154 TGEIAISDHRSSQPTAD--EFKRLCAdtrvggiLSGKAGI-INIHLGDSPRCMDLINQVIAETEIPATQFLPT--HVNRN 228
Cdd:pfam07969 232 LTEPYFDAPGTGWPDFEdeALAELVA-------AARERGLdVAIHAIGDATIDTALDAFEAVAEKLGNQGRVRieHAQGV 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 229 AALFEEAVE-YAKLGGAVDFT-----GNEDIDYWETICDEVRVSKGIKRLLDEGVSsdlFTISSDGQGSlPMFSADGVfQ 302
Cdd:pfam07969 305 VPYTYSQIErVAALGGAAGVQpvfdpLWGDWLQDRLGAERARGLTPVKELLNAGVK---VALGSDAPVG-PFDPWPRI-G 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 303 GMGMGQSSCLLKEVREcveKEGIPLEIAIKAITSNPAKVLCLPQ-KGRIEEGMDADLCLMTKD-LEID-TVIAMGQV--M 377
Cdd:pfam07969 380 AAVMRQTAGGGEVLGP---DEELSLEEALALYTSGPAKALGLEDrKGTLGVGKDADLVVLDDDpLTVDpPAIADIRVrlT 456
|
....*...
gi 2668721358 378 VKKGEPIV 385
Cdd:pfam07969 457 VVDGRVVY 464
|
|
| PhnM |
COG3454 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport ... |
320-358 |
7.06e-06 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase PhnM [Inorganic ion transport and metabolism];
Pssm-ID: 442677 Cd Length: 383 Bit Score: 47.83 E-value: 7.06e-06
10 20 30
....*....|....*....|....*....|....*....
gi 2668721358 320 VEKEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADL 358
Cdd:COG3454 319 AEDGGLDLPEAVALVTSNPARALGLDDRGEIAPGKRADL 357
|
|
| AdeC |
cd01295 |
Adenine deaminase (AdeC) directly deaminates adenine to form hypoxanthine. This reaction is ... |
316-391 |
7.16e-06 |
|
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: 47.60 E-value: 7.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 316 VRECVEkEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLMtKDLE---IDTVIAMGQVMV---KKGEPIVKGAF 389
Cdd:cd01295 227 VRRAIE-AGIPPEDAIQMATINPAECYGLHDLGAIAPGRIADIVIL-DDLEnfnITTVLAKGIAVVerhGKTGNIGVGFV 304
|
..
gi 2668721358 390 EG 391
Cdd:cd01295 305 KG 306
|
|
| Met_dep_hydrolase_C |
cd01309 |
Metallo-dependent hydrolases, subgroup C is part of the superfamily of metallo-dependent ... |
322-373 |
7.21e-06 |
|
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: 47.69 E-value: 7.21e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2668721358 322 KEGIPLEIAIKAITSNPAKVLCLPQK-GRIEEGMDADLCLMTKD-LEIDTVIAM 373
Cdd:cd01309 297 KYGLSYEEALKAITINPAKILGIEDRvGSLEPGKDADLVVWNGDpLEPTSKPEQ 350
|
|
| DHOase_IIa |
cd01317 |
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of ... |
42-360 |
8.22e-06 |
|
Dihydroorotase (DHOase), subgroup IIa; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This subgroup also contains proteins that lack the active site, like unc-33, a C.elegans protein involved in axon growth.
Pssm-ID: 238642 [Multi-domain] Cd Length: 374 Bit Score: 47.62 E-value: 8.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 42 EVEVIDGTGLLLLPGFIDSHVHVlggggeggfanRTP----EATLSGLTRY----GITTVVGCLGTDGIgRDIKSLVAKI 113
Cdd:cd01317 1 DAEVIDAEGKILAPGLVDLHVHL-----------REPgfeyKETLESGAKAaaagGFTTVVCMPNTNPV-IDNPAVVELL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 114 KGL-REQGISAYAYTGSYQVP--VRTLTGgiiddimmIEEIIGTGEIAISDHRSSQPTADEFKRLC-------------- 176
Cdd:cd01317 69 KNRaKDVGIVRVLPIGALTKGlkGEELTE--------IGELLEAGAVGFSDDGKPIQDAELLRRALeyaamldlpiivhp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 177 --ADTRVGGI-----LSGKAGIINIHlgdsprcmdlinqVIAETEIPATQFL-------PTHVNR-NAALFEEAVEYAKL 241
Cdd:cd01317 141 edPSLAGGGVmnegkVASRLGLPGIP-------------PEAETIMVARDLElaeatgaRVHFQHlSTARSLELIRKAKA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 242 GGAVDFTG---------NEDIDYWET----------ICDEVRVSKGIKRLLDEGVSSD--LFTISSDGQG-SLPMFSADG 299
Cdd:cd01317 208 KGLPVTAEvtphhllldDEALESYDTnakvnpplrsEEDREALIEALKDGTIDAIASDhaPHTDEEKDLPfAEAPPGIIG 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2668721358 300 VFQGMgmgqsSCLLKEVrecVEKEGIPLEIAIKAITSNPAKVLCLPQkGRIEEGMDADLCL 360
Cdd:cd01317 288 LETAL-----PLLWTLL---VKGGLLTLPDLIRALSTNPAKILGLPP-GRLEVGAPADLVL 339
|
|
| PLN02942 |
PLN02942 |
dihydropyrimidinase |
4-64 |
1.97e-05 |
|
dihydropyrimidinase
Pssm-ID: 178530 Cd Length: 486 Bit Score: 46.37 E-value: 1.97e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2668721358 4 LIKGVNLYTPEYLGVKDVFLAGGKICKIADNIELPTEleVEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PLN02942 8 LIKGGTVVNAHHQELADVYVEDGIIVAVAPNLKVPDD--VRVIDATGKFVMPGGIDPHTHL 66
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
4-65 |
2.52e-05 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 46.33 E-value: 2.52e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2668721358 4 LIKGVNLYT-------PEYLGVKDvflagGKICKIADNIELPTEL--EVEVIDGTGLLLLPGFIDSHVHVL 65
Cdd:COG1574 11 LLTNGRIYTmdpaqpvAEAVAVRD-----GRIVAVGSDAEVRALAgpATEVIDLGGKTVLPGFIDAHVHLL 76
|
|
| PRK08393 |
PRK08393 |
N-ethylammeline chlorohydrolase; Provisional |
1-64 |
5.58e-05 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 181411 [Multi-domain] Cd Length: 424 Bit Score: 44.79 E-value: 5.58e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2668721358 1 MMKLIK-GVNLYTPEYLGVK-DVFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PRK08393 1 MSILIKnGYVIYGENLKVIRaDVLIEGNKIVEVKRNINKPAD---TVIDASGSVVSPGFINAHTHS 63
|
|
| DHOase_IIb |
cd01318 |
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of ... |
320-358 |
5.79e-05 |
|
Dihydroorotase (DHOase), subgroup IIb; DHOases catalyze the reversible interconversion of carbamoyl aspartate to dihydroorotate, a key reaction in pyrimidine biosynthesis. This group contains the archeal members of the DHOase family.
Pssm-ID: 238643 [Multi-domain] Cd Length: 361 Bit Score: 44.63 E-value: 5.79e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2668721358 320 VEKEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADL 358
Cdd:cd01318 282 VNKGILSLSRVVRLTSHNPARIFGIKNKGRIAEGYDADL 320
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
320-358 |
8.11e-05 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 44.40 E-value: 8.11e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2668721358 320 VEKEGIPLEIAIKAITSNPAKVLCLPQKGRIEEGMDADL 358
Cdd:PRK15446 319 ADDGGLDLPQAVALVTANPARAAGLDDRGEIAPGKRADL 357
|
|
| PLN02795 |
PLN02795 |
allantoinase |
12-358 |
9.64e-05 |
|
allantoinase
Pssm-ID: 178392 [Multi-domain] Cd Length: 505 Bit Score: 44.38 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 12 TPEYLGVKDVFLAGGKICKIADNIELP-TELEVEVIDGTGLLLLPGFIDSHVHV--LGGGGEGGFANRTPEATLSgltry 88
Cdd:PLN02795 55 TPAGVIPGAVEVEGGRIVSVTKEEEAPkSQKKPHVLDYGNAVVMPGLIDVHVHLnePGRTEWEGFPTGTKAAAAG----- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 89 GITTVVGC-LGTDGIGRDIKSLVAKIK------------------------------------GLRE----QGISAYAYT 127
Cdd:PLN02795 130 GITTLVDMpLNSFPSTTSVETLELKIEaakgklyvdvgfwgglvpenahnasvleelldagalGLKSfmcpSGINDFPMT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 128 ------------GSYQVPVrtLTGGIIDDIMMIEEIIGTGEIAISDHRSSQPTADE---FKRLC---ADTRVGGILSGkA 189
Cdd:PLN02795 210 tathikaalpvlAKYGRPL--LVHAEVVSPVESDSRLDADPRSYSTYLKSRPPSWEqeaIRQLLevaKDTRPGGVAEG-A 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 190 GIINIHLGDSPRCMDLINQ-------VIAET----------EIP--ATQFL---PTHVNRNAALFEEAVeyakLGGAVDF 247
Cdd:PLN02795 287 HVHIVHLSDAESSLELIKEakakgdsVTVETcphylafsaeEIPdgDTRYKcapPIRDAANRELLWKAL----LDGDIDM 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 248 TGNediDYWETICDEvrvskgikRLLDEGVSSDLFTISSDGQGSLPMFSADGVFQGMGMGQSSCLLKEvrecvekegipl 327
Cdd:PLN02795 363 LSS---DHSPSPPDL--------KLLEEGNFLRAWGGISSLQFVLPATWTAGRAYGLTLEQLARWWSE------------ 419
|
410 420 430
....*....|....*....|....*....|.
gi 2668721358 328 eiaikaitsNPAKVLCLPQKGRIEEGMDADL 358
Cdd:PLN02795 420 ---------RPAKLAGLDSKGAIAPGKDADI 441
|
|
| PRK07572 |
PRK07572 |
cytosine deaminase; Validated |
1-87 |
1.17e-04 |
|
cytosine deaminase; Validated
Pssm-ID: 181039 Cd Length: 426 Bit Score: 43.85 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 1 MMKLI-KGVNLytPEYLGVKDVFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHVlggggeggfanrtpE 79
Cdd:PRK07572 1 MFDLIvRNANL--PDGRTGIDIGIAGGRIAAVEPGLQAEAA---EEIDAAGRLVSPPFVDPHFHM--------------D 61
|
....*....
gi 2668721358 80 ATLS-GLTR 87
Cdd:PRK07572 62 ATLSyGLPR 70
|
|
| PRK13404 |
PRK13404 |
dihydropyrimidinase; Provisional |
20-64 |
2.05e-04 |
|
dihydropyrimidinase; Provisional
Pssm-ID: 184033 [Multi-domain] Cd Length: 477 Bit Score: 43.15 E-value: 2.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2668721358 20 DVFLAGGKICKIADNieLPTEleVEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PRK13404 23 DIGIRGGRIAALGEG--LGPG--AREIDATGRLVLPGGVDSHCHI 63
|
|
| PRK09228 |
PRK09228 |
guanine deaminase; Provisional |
1-63 |
2.11e-04 |
|
guanine deaminase; Provisional
Pssm-ID: 236419 [Multi-domain] Cd Length: 433 Bit Score: 43.26 E-value: 2.11e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2668721358 1 MMKLIKGVNLYT---PEYLGVKD---------VFLAGGKICKIADNIELPTEL--EVEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK09228 2 TTKAYRGRLLHFtadPAEVDDEDalryiedglLLVEDGRIVAAGPYAELRAQLpaDAEVTDYRGKLILPGFIDTHIH 78
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
1-64 |
2.58e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 42.87 E-value: 2.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2668721358 1 MMKLIKGVNLYTP------EylgVKDVFLAGGKIckiadnIELPTELEV-EVIDGTGLLLLPGFIDSHVHV 64
Cdd:COG1229 1 MELIIKNGRVYDPangidgE---VMDIAIKDGKI------VEEPSDPKDaKVIDASGKVVMAGGVDIHTHI 62
|
|
| PRK06846 |
PRK06846 |
putative deaminase; Validated |
17-64 |
4.17e-04 |
|
putative deaminase; Validated
Pssm-ID: 235873 [Multi-domain] Cd Length: 410 Bit Score: 42.31 E-value: 4.17e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2668721358 17 GVKDVFLAGGKICKIADNiELPTELEVEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PRK06846 30 ALCTLEIQDGKIVAIRPN-KQVPDATLPTYDANGLLMLPAFREMHIHL 76
|
|
| PRK12394 |
PRK12394 |
metallo-dependent hydrolase; |
2-64 |
4.25e-04 |
|
metallo-dependent hydrolase;
Pssm-ID: 183497 [Multi-domain] Cd Length: 379 Bit Score: 42.05 E-value: 4.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2668721358 2 MK---LIKGVNLYTPEY--LGVKDVFLAGGKIckiADNIELPTELEVEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PRK12394 1 MKndiLITNGHIIDPARniNEINNLRIINDII---VDADKYPVASETRIIHADGCIVTPGLIDYHAHV 65
|
|
| PRK09061 |
PRK09061 |
D-glutamate deacylase; Validated |
17-63 |
5.83e-04 |
|
D-glutamate deacylase; Validated
Pssm-ID: 236369 [Multi-domain] Cd Length: 509 Bit Score: 41.99 E-value: 5.83e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 2668721358 17 GVKDVFLAGGKICKIADNielPTELEvEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK09061 37 AVRDVGIKGGKIAAVGTA---AIEGD-RTIDATGLVVAPGFIDLHAH 79
|
|
| PRK07369 |
PRK07369 |
dihydroorotase; Provisional |
18-63 |
5.99e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 236002 [Multi-domain] Cd Length: 418 Bit Score: 41.51 E-value: 5.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2668721358 18 VKDVFLAGGKICKIADNIElPTELEVEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK07369 21 IADVLIEDGKIQAIEPHID-PIPPDTQIIDASGLILGPGLVDLYSH 65
|
|
| PRK09230 |
PRK09230 |
cytosine deaminase; Provisional |
2-63 |
6.66e-04 |
|
cytosine deaminase; Provisional
Pssm-ID: 181713 Cd Length: 426 Bit Score: 41.61 E-value: 6.66e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2668721358 2 MKLIKGVNLYTPEylGVKDVFLAGGKICKIADNIELPTELEvEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK09230 5 LMTIKNARLPGKE--GLWQITIEDGKISAIEPQSEASLEAG-EVLDAEGGLAIPPFIEPHIH 63
|
|
| YtcJ |
COG1574 |
Predicted amidohydrolase YtcJ [General function prediction only]; |
323-368 |
6.80e-04 |
|
Predicted amidohydrolase YtcJ [General function prediction only];
Pssm-ID: 441182 [Multi-domain] Cd Length: 535 Bit Score: 41.71 E-value: 6.80e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 2668721358 323 EGIPLEIAIKAITSNPAKVLCLPQ-KGRIEEGMDADLCLMTKD-LEID 368
Cdd:COG1574 465 ERLTVEEALRAYTIGAAYAAFEEDeKGSLEPGKLADFVVLDRDpLTVP 512
|
|
| FwdA |
COG1229 |
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion]; |
328-386 |
7.03e-04 |
|
Formylmethanofuran dehydrogenase subunit A [Energy production and conversion];
Pssm-ID: 440842 Cd Length: 554 Bit Score: 41.72 E-value: 7.03e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2668721358 328 EIAIkaIT-SNPAKVLCLPQKGRIEEGMDADLCLMT---KDLEIDTVIAM----------GQVMVKKGEpIVK 386
Cdd:COG1229 433 EIAI--MTrAGPAKALGLADRGHLGVGADADIAIYDinpDDKDYEDIEKMfskpayvikdGEVVVKDGE-IVA 502
|
|
| ureC |
PRK13207 |
urease subunit alpha; Reviewed |
17-95 |
7.36e-04 |
|
urease subunit alpha; Reviewed
Pssm-ID: 237305 [Multi-domain] Cd Length: 568 Bit Score: 41.70 E-value: 7.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 17 GVKDvflagGKICKI--------ADNIELPTELEVEVIDGTGLLLLPGFIDSHVHVLggggeggfANRTPEATLSGltry 88
Cdd:PRK13207 88 GIKD-----GRIVAIgkagnpdiQDGVDIIIGPGTEVIAGEGLIVTAGGIDTHIHFI--------CPQQIEEALAS---- 150
|
....*..
gi 2668721358 89 GITTVVG 95
Cdd:PRK13207 151 GVTTMIG 157
|
|
| PRK07627 |
PRK07627 |
dihydroorotase; Provisional |
323-360 |
8.00e-04 |
|
dihydroorotase; Provisional
Pssm-ID: 181059 [Multi-domain] Cd Length: 425 Bit Score: 41.20 E-value: 8.00e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2668721358 323 EGIPLEIAIKAITSNPAKVLCLPqKGRIEEGMDADLCL 360
Cdd:PRK07627 343 AKVPLARALARITSAPARVLGLP-AGRLAEGAPADLCV 379
|
|
| PRK07228 |
PRK07228 |
5'-deoxyadenosine deaminase; |
20-63 |
1.01e-03 |
|
5'-deoxyadenosine deaminase;
Pssm-ID: 180895 [Multi-domain] Cd Length: 445 Bit Score: 41.14 E-value: 1.01e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2668721358 20 DVFLAGGKICKIADNIELptELEVEVIDGTGLLLLPGFIDSHVH 63
Cdd:PRK07228 23 DVLIEDDRIAAVGDRLDL--EDYDDHIDATGKVVIPGLIQGHIH 64
|
|
| YtcJ_like |
cd01300 |
YtcJ_like metal dependent amidohydrolases. YtcJ is a Bacillus subtilis ORF of unknown function. ... |
269-360 |
1.17e-03 |
|
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: 40.76 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 269 IKRLLDEGV----SSDLFTISSDgqgslPMFSAdgvfQGMGMGQSScllKEVRECVEKEGIPLEIAIKAITSNPAKVLCL 344
Cdd:cd01300 395 FRSLLDAGVpvalGSDAPVAPPD-----PLLGI----WAAVTRKTP---GGGVLGNPEERLSLEEALRAYTIGAAYAIGE 462
|
90
....*....|....*..
gi 2668721358 345 PQ-KGRIEEGMDADLCL 360
Cdd:cd01300 463 EDeKGSLEPGKLADFVV 479
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
328-386 |
1.42e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 40.86 E-value: 1.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2668721358 328 EIAIkaIT-SNPAKVLCLPQKGRIEEGMDADLCLMTKD-LEIDT---------------VIAMGQVMVKKGEpIVK 386
Cdd:cd01304 431 EIAI--MTrAGPAKLLGLSDKGHLGVGADADIAIYDDDpDQVDPsdyekvekafsraayVLKDGEIVVKDGE-VVA 503
|
|
| Imidazolone-5PH |
cd01296 |
Imidazolonepropionase/imidazolone-5-propionate hydrolase (Imidazolone-5PH) catalyzes the third ... |
25-86 |
2.13e-03 |
|
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: 39.93 E-value: 2.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2668721358 25 GGKICKI--ADNIELPTELEVEVIDGTGLLLLPGFIDSHVHVLggggeggFA-NRTPE--ATLSGLT 86
Cdd:cd01296 5 DGRIAAVgpAASLPAPGPAAAEEIDAGGRAVTPGLVDCHTHLV-------FAgDRVDEfaARLAGAS 64
|
|
| PRK07583 |
PRK07583 |
cytosine deaminase; |
326-384 |
3.33e-03 |
|
cytosine deaminase;
Pssm-ID: 236062 Cd Length: 438 Bit Score: 39.20 E-value: 3.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2668721358 326 PLEIAIKAITSNPAKVLCLPQKGRIEEGMDADLCLmTKDLEIDTVIAMGQ---VMVKKGEPI 384
Cdd:PRK07583 361 PYDDWPAAVTTTPADIMGLPDLGRIAVGAPADLVL-FKARSFSELLSRPQsdrIVLRAGKPI 421
|
|
| PRK06038 |
PRK06038 |
N-ethylammeline chlorohydrolase; Provisional |
4-64 |
7.66e-03 |
|
N-ethylammeline chlorohydrolase; Provisional
Pssm-ID: 180363 [Multi-domain] Cd Length: 430 Bit Score: 38.19 E-value: 7.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2668721358 4 LIKGVNLYTPEYLGVKD--VFLAGGKICKIADNIELPTElevEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PRK06038 5 IIKNAYVLTMDAGDLKKgsVVIEDGTITEVSESTPGDAD---TVIDAKGSVVMPGLVNTHTHA 64
|
|
| nagA |
PRK11170 |
N-acetylglucosamine-6-phosphate deacetylase; Provisional |
307-375 |
7.68e-03 |
|
N-acetylglucosamine-6-phosphate deacetylase; Provisional
Pssm-ID: 183010 Cd Length: 382 Bit Score: 38.03 E-value: 7.68e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2668721358 307 GQSSCLLKEVRECVEKEGIPLEIAIKAITSNPAKVLCLPQK-GRIEEGMDADLCLMTKDLEIDTVIAMGQ 375
Cdd:PRK11170 308 GSALTMIEAVRNLVEHVGIALDEALRMATLYPARAIGVDKRlGSIEAGKVANLTAFTRDFKITKTIVNGN 377
|
|
| PRK06380 |
PRK06380 |
metal-dependent hydrolase; Provisional |
20-64 |
9.13e-03 |
|
metal-dependent hydrolase; Provisional
Pssm-ID: 180548 [Multi-domain] Cd Length: 418 Bit Score: 37.94 E-value: 9.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 2668721358 20 DVFLAGGKICKIADnIELPTElevEVIDGTGLLLLPGFIDSHVHV 64
Cdd:PRK06380 23 NVYIEGNKIVYVGD-VNEEAD---YIIDATGKVVMPGLINTHAHV 63
|
|
| FMDH_A |
cd01304 |
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive ... |
5-64 |
9.13e-03 |
|
Formylmethanofuran dehydrogenase (FMDH) subunit A; Methanogenic bacteria and archea derive the energy for autotrophic growth from methanogenesis, the reduction of CO2 with molecular hydrogen as the electron donor. FMDH catalyzes the first step in methanogenesis, the formyl-methanofuran synthesis. In this step, CO2 is bound to methanofuran and subsequently reduced to the formyl state with electrons derived from hydrogen.
Pssm-ID: 238629 [Multi-domain] Cd Length: 541 Bit Score: 38.16 E-value: 9.13e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2668721358 5 IKGVNLYTPEYlGVK----DVFLAGGKICKiadniELPTELEVEVIDGTGLLLLPGFIDSHVHV 64
Cdd:cd01304 1 IKNGTVYDPLN-GINgekmDIFIRDGKIVE-----SSSGAKPAKVIDASGKVVMAGGVDMHSHI 58
|
|
| PRK15446 |
PRK15446 |
phosphonate metabolism protein PhnM; Provisional |
1-61 |
9.27e-03 |
|
phosphonate metabolism protein PhnM; Provisional
Pssm-ID: 237967 [Multi-domain] Cd Length: 383 Bit Score: 37.85 E-value: 9.27e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2668721358 1 MMKLIKGVNLYTPEYLGVKDVFLAGGKICKIADNielpTELEVEVIDGTGLLLLPGFIDSH 61
Cdd:PRK15446 2 MEMILSNARLVLPDEVVDGSLLIEDGRIAAIDPG----ASALPGAIDAEGDYLLPGLVDLH 58
|
|
| |
