|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
4-358 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143500 [Multi-domain] Cd Length: 354 Bit Score: 595.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 4 ATAEINLTALAHNLSQVKRFAPNSKIMAVLKANAYGHGLVKIAQHLNSADAFAVARIDEALALRAGGLTKPIVLLEGFFN 83
Cdd:cd06827 2 ARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 84 KADLPILLANNFQTIVHDENQLAAIENATLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStINLMTHFSCA 163
Cdd:cd06827 82 ADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVAS-IVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 164 DDTHNTKTAQQISLFDTLVKGIDQAHCLSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCTGQEHNLKPVMRLTTKVIAV 243
Cdd:cd06827 161 DEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 244 RDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDIGENEhNVKVGDSVT 323
Cdd:cd06827 241 RELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLP-EAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 567929223 324 MWGPELPVEEIAHCADTIPYELLCNITPRVSYEYQ 358
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-357 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 512.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 1 MRLATAEINLTALAHNLSQVKRFAP-NSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPpKSKLMAVVKANAYGHGAVEVAKTLleAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 78 LEGFFNKADLPILLANNFQTIVHDENQLAAIENATLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStINLM 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 158 THFSCADDTHNTKTAQQISLFDTLVKGID-----QAHcLSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCTGQEHNLKP 232
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPgkgkpLRH-LANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 233 VMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDIGEN 312
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 567929223 313 EhNVKVGDSVTMWGPELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:PRK00053 319 P-QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-359 |
1.30e-169 |
|
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440550 [Multi-domain] Cd Length: 368 Bit Score: 476.91 E-value: 1.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 1 MRLATAEINLTALAHNLSQVKRFA-PNSKIMAVLKANAYGHGLVKIAQHLNS--ADAFAVARIDEALALRAGGLTKPIVL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALLEagADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 78 LEGFFnKADLPILLANNFQTIVHDENQLAAIENA--TLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStIN 155
Cdd:COG0787 81 LGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEV-EG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 156 LMTHFSCADDTHNTKTAQQISLFDTLVKGIDQAH------CLSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANcTGQEHN 229
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAGldpplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE-VAADLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 230 LKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDI 309
Cdd:COG0787 238 LKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 567929223 310 GENEhNVKVGDSVTMWGPE-LPVEEIAHCADTIPYELLCNITPRVSYEYQR 359
Cdd:COG0787 318 TDIP-DVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-357 |
1.13e-141 |
|
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is to generate D-alanine for cell wall formation. With D-alanine-D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route. It is a monomer with one pyridoxal phosphate per subunit. In E. coli, the ortholog is duplicated so that a second isozyme, DadX, is present. DadX, a paralog of the biosynthetic Alr, is induced by D- or L-alanine and is involved in catabolism. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129583 [Multi-domain] Cd Length: 367 Bit Score: 406.35 E-value: 1.13e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 2 RLATAEINLTALAHNLSQVKRF-APNSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLlqAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 79 EGFFNKaDLPILLANNFQTIVHDENQLAAIENATLDAP--ITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKSTINL 156
Cdd:TIGR00492 81 GGFFAE-DLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 157 MTHFSCADDTHNTKTAQQISLFDTLVKGIDQA-------HClSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCT-GQEH 228
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQnieppfrHI-ANSAAILNWPESHFDMVRPGIILYGLYPSADMSdGAPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 229 NLKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISID 308
Cdd:TIGR00492 239 GLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 567929223 309 IGENEhNVKVGDSVTMWGPELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:TIGR00492 319 LGPDL-QDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
4.82e-80 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 244.06 E-value: 4.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 8 INLTALAHNLSQVKRFA-PNSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLLEGFfNK 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 85 ADLPILLANNFQTIVHDENQLAAIENA--TLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStINLMTHFSC 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRL-EGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567929223 163 ADDTHNTKTAQQISLFDTLVKGIDQAH------CLSNSAGIIAWPAgHGDWIRPGLMLYGVSP 219
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAGlrppvvHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-357 |
1.61e-57 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 182.65 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 233 VMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKeGTPVMIAGQRYGIVGSVSMDMISIDIGEN 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 567929223 313 EhNVKVGDSVTMWGP-ELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:smart01005 80 P-DVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
4-358 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143500 [Multi-domain] Cd Length: 354 Bit Score: 595.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 4 ATAEINLTALAHNLSQVKRFAPNSKIMAVLKANAYGHGLVKIAQHLNSADAFAVARIDEALALRAGGLTKPIVLLEGFFN 83
Cdd:cd06827 2 ARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 84 KADLPILLANNFQTIVHDENQLAAIENATLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStINLMTHFSCA 163
Cdd:cd06827 82 ADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVAS-IVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 164 DDTHNTKTAQQISLFDTLVKGIDQAHCLSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCTGQEHNLKPVMRLTTKVIAV 243
Cdd:cd06827 161 DEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 244 RDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDIGENEhNVKVGDSVT 323
Cdd:cd06827 241 RELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLP-EAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 567929223 324 MWGPELPVEEIAHCADTIPYELLCNITPRVSYEYQ 358
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-357 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 512.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 1 MRLATAEINLTALAHNLSQVKRFAP-NSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPpKSKLMAVVKANAYGHGAVEVAKTLleAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 78 LEGFFNKADLPILLANNFQTIVHDENQLAAIENATLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStINLM 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 158 THFSCADDTHNTKTAQQISLFDTLVKGID-----QAHcLSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCTGQEHNLKP 232
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPgkgkpLRH-LANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 233 VMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDIGEN 312
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 567929223 313 EhNVKVGDSVTMWGPELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:PRK00053 319 P-QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-359 |
1.30e-169 |
|
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440550 [Multi-domain] Cd Length: 368 Bit Score: 476.91 E-value: 1.30e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 1 MRLATAEINLTALAHNLSQVKRFA-PNSKIMAVLKANAYGHGLVKIAQHLNS--ADAFAVARIDEALALRAGGLTKPIVL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALLEagADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 78 LEGFFnKADLPILLANNFQTIVHDENQLAAIENA--TLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStIN 155
Cdd:COG0787 81 LGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEV-EG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 156 LMTHFSCADDTHNTKTAQQISLFDTLVKGIDQAH------CLSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANcTGQEHN 229
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAGldpplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE-VAADLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 230 LKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDI 309
Cdd:COG0787 238 LKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 567929223 310 GENEhNVKVGDSVTMWGPE-LPVEEIAHCADTIPYELLCNITPRVSYEYQR 359
Cdd:COG0787 318 TDIP-DVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-357 |
1.00e-141 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 406.04 E-value: 1.00e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 1 MRLATAEINLTALAHNLSQVKRFAPNSKIMAVLKANAYGHGLVKIAQHLNSADAFAVARIDEALALRAGGLTKPIVLLEG 80
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 81 FFNKADLPILLANNFQTIVHDENQLAAIENATLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAkSTINLMTHF 160
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNV-GEMTLMSHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 161 SCADdtHNTKTAQQISLFDTLVKGIDQAHCLSNSAGIIAWPAGHGDWIRPGLMLYGVSPmancTGQEH-----NLKPVMR 235
Cdd:PRK03646 160 ARAD--HPDGISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASP----SGQWRdiantGLRPVMT 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 236 LTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDIGENEHn 315
Cdd:PRK03646 234 LSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQ- 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 567929223 316 VKVGDSVTMWGPELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:PRK03646 313 AGIGTPVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-357 |
1.13e-141 |
|
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is to generate D-alanine for cell wall formation. With D-alanine-D-alanine ligase, it makes up the D-alanine branch of the peptidoglycan biosynthetic route. It is a monomer with one pyridoxal phosphate per subunit. In E. coli, the ortholog is duplicated so that a second isozyme, DadX, is present. DadX, a paralog of the biosynthetic Alr, is induced by D- or L-alanine and is involved in catabolism. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 129583 [Multi-domain] Cd Length: 367 Bit Score: 406.35 E-value: 1.13e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 2 RLATAEINLTALAHNLSQVKRF-APNSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLlqAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 79 EGFFNKaDLPILLANNFQTIVHDENQLAAIENATLDAP--ITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKSTINL 156
Cdd:TIGR00492 81 GGFFAE-DLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 157 MTHFSCADDTHNTKTAQQISLFDTLVKGIDQA-------HClSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCT-GQEH 228
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQnieppfrHI-ANSAAILNWPESHFDMVRPGIILYGLYPSADMSdGAPF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 229 NLKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISID 308
Cdd:TIGR00492 239 GLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 567929223 309 IGENEhNVKVGDSVTMWGPELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:TIGR00492 319 LGPDL-QDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
4-353 |
2.53e-139 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.
Pssm-ID: 143481 [Multi-domain] Cd Length: 367 Bit Score: 400.33 E-value: 2.53e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 4 ATAEINLTALAHNLSQVKRFA-PNSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLLEG 80
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLgPGTKIMAVVKADAYGHGAVEVAKALeeAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 81 FFNkADLPILLANNFQTIVHDENQLAAIENA--TLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNakstINL-- 156
Cdd:cd00430 82 TPP-EEAEEAIEYDLTPTVSSLEQAEALSAAaaRLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPG----LELeg 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 157 -MTHFSCADDTHNTKTAQQISLFDTLVKGIDQA-------HClSNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCTGQEh 228
Cdd:cd00430 157 vFTHFATADEPDKAYTRRQLERFLEALAELEEAgippplkHL-ANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 229 NLKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISID 308
Cdd:cd00430 235 GLKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVD 314
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 567929223 309 IGENEhNVKVGDSVTMWGP----ELPVEEIAHCADTIPYELLCNITPRV 353
Cdd:cd00430 315 VTDIP-DVKVGDEVVLFGRqgdeEITAEELAELAGTINYEILCRISKRV 362
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
4-357 |
2.32e-88 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This subfamily is composed of Enterococcus gallinarum VanT and similar proteins. VanT is a membrane-bound serine racemase (EC 5.1.1.18) that is essential for vancomycin resistance in Enterococcus gallinarum. It converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. The C-terminal region of this protein contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, which is homologous to the fold type III PLP-dependent enzyme, bacterial alanine racemase (AR). AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. On the basis of this similarity, it has been suggested that dimer formation of VanT is required for its catalytic activity, and that it catalyzes the racemization of serine in a mechanistically similar manner to that of alanine by bacterial AR. Some biochemical evidence indicates that VanT also exhibits alanine racemase activity and plays a role in the racemization of L-alanine. VanT contains a unique N-terminal transmembrane domain, which may function as an L-serine transporter. VanT serine racemases are not related to eukaryotic serine racemases, which are fold type II PLP-dependent enzymes.
Pssm-ID: 143498 [Multi-domain] Cd Length: 368 Bit Score: 270.38 E-value: 2.32e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 4 ATAEINLTALAHNLSQVKRFAP-NSKIMAVLKANAYGHGLVKIAQHLNSA--DAFAVARIDEALALRAGGLTKPIVLLeG 80
Cdd:cd06825 2 AWLEIDLSALEHNVKEIKRLLPsTCKLMAVVKANAYGHGDVEVARVLEQIgiDFFAVATIDEGIRLREAGIKGEILIL-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 81 FFNKADLPILLANNF-QTIVHDENqlaAIENATLDAPITCWLKINTGMHRLGIAPEQFDAFySRLQRTPNAKSTiNLMTH 159
Cdd:cd06825 81 YTPPVRAKELKKYSLtQTLISEAY---AEELSKYAVNIKVHLKVDTGMHRLGESPEDIDSI-LAIYRLKNLKVS-GIFSH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 160 FSCADDThNTK----TAQQISLFDTLVKGIDQAH------CLSNSAGIIAWPAGHGDWIRPGLMLYGV-SPMANCTGQEH 228
Cdd:cd06825 156 LCVSDSL-DEDdiafTKHQIACFDQVLADLKARGievgkiHIQSSYGILNYPDLKYDYVRPGILLYGVlSDPNDPTKLGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 229 NLKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRH-AKEGTPVMIAGQRYGIVGSVSMDMISI 307
Cdd:cd06825 235 DLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSlSNQKAYVLINGKRAPIIGNICMDQLMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 567929223 308 DIGENEhNVKVGDSVTMWG----PELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:cd06825 315 DVTDIP-EVKEGDTATLIGqdgdEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
7-353 |
5.67e-84 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 271.06 E-value: 5.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 7 EINLTALAHNLSQVK-RFAPNSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLLegffN 83
Cdd:PRK11930 463 EINLNAIVHNLNYYRsKLKPETKIMCMVKAFAYGSGSYEIAKLLqeHRVDYLAVAYADEGVSLRKAGITLPIMVM----N 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 84 KA--DLPILLANNFQTIVHDENQLAAIENATLDAPITCW---LKINTGMHRLGIAPEQFDAFYSRLQRTPNAKSTiNLMT 158
Cdd:PRK11930 539 PEptSFDTIIDYKLEPEIYSFRLLDAFIKAAQKKGITGYpihIKIDTGMHRLGFEPEDIPELARRLKKQPALKVR-SVFS 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 159 HFSCADD-THNTKTAQQISLFDTLVKGIdQAHC-------LSNSAGIIAWPAGHGDWIRPGLMLYGVSPmancTGQEHN- 229
Cdd:PRK11930 618 HLAGSDDpDHDDFTRQQIELFDEGSEEL-QEALgykpirhILNSAGIERFPDYQYDMVRLGIGLYGVSA----SGAGQQa 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 230 LKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGT-PVMIAGQRYGIVGSVSMDMISID 308
Cdd:PRK11930 693 LRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNICMDMCMID 772
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 567929223 309 IGENehNVKVGDSVTMWGPELPVEEIAHCADTIPYELLCNITPRV 353
Cdd:PRK11930 773 VTDI--DAKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRV 815
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
4.82e-80 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 244.06 E-value: 4.82e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 8 INLTALAHNLSQVKRFA-PNSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLLEGFfNK 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 85 ADLPILLANNFQTIVHDENQLAAIENA--TLDAPITCWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKStINLMTHFSC 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRL-EGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 567929223 163 ADDTHNTKTAQQISLFDTLVKGIDQAH------CLSNSAGIIAWPAgHGDWIRPGLMLYGVSP 219
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAGlrppvvHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
4-347 |
1.71e-71 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 228.35 E-value: 1.71e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 4 ATAEINLTALAHNLSQVKRFAPN-SKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLLEG 80
Cdd:PRK13340 41 AWLEISPGAFRHNIKTLRSLLANkSKVCAVMKADAYGHGIELLMPSIikANVPCIGIASNEEARRVRELGFTGQLLRVRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 81 FfNKADLPILLANNFQTIVHDENQLAAIEN--ATLDAPITCWLKINT-GMHRLGIAPEQFDAFYSRLQ--RTPNAKsTIN 155
Cdd:PRK13340 121 A-SPAEIEQALRYDLEELIGDDEQAKLLAAiaKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWEALRiaTLPSLG-IVG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 156 LMTHFSCADDThntKTAQQISLFDTLVKGIDQAHCL---------SNSAGIIAWPAGHGDWIRPGLMLYGVSPMANCtgq 226
Cdd:PRK13340 199 IMTHFPNEDED---EVRWKLAQFKEQTAWLIGEAGLkrekitlhvANSYATLNVPEAHLDMVRPGGILYGDRHPANT--- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 227 ehNLKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMIS 306
Cdd:PRK13340 273 --EYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTLM 350
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 567929223 307 IDIGENEhNVKVGDSVTMWG----PELPVEEIAHCADTIPYELLC 347
Cdd:PRK13340 351 VDVTDIP-NVKPGDEVVLFGkqgnAEITVDEVEEASGTIFPELYT 394
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-357 |
1.61e-57 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 182.65 E-value: 1.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 233 VMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKeGTPVMIAGQRYGIVGSVSMDMISIDIGEN 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 567929223 313 EhNVKVGDSVTMWGP-ELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:smart01005 80 P-DVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
233-357 |
2.36e-55 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 177.17 E-value: 2.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 233 VMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDIGEN 312
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 567929223 313 EhNVKVGDSVTMWGP----ELPVEEIAHCADTIPYELLCNITPRVSYEY 357
Cdd:pfam00842 81 P-EVKVGDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
13-212 |
5.54e-34 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.
Pssm-ID: 143484 [Multi-domain] Cd Length: 211 Bit Score: 124.74 E-value: 5.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 13 LAHNLSQVKRFAP-NSKIMAVLKANAYGHgLVKIAQHLnsADAFAVARIDEALALRAGGL-TKPIVLLEGFFNKADLPIL 90
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKANANPE-VARTLAAL--GTGFDVASLGEALLLRAAGIpPEPILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 91 LANN-FQTIVHDENQLAAIENATLDA--PITCWLKINTG--MHRLGIAPEQFDAFYSRLQRTPNAKsTINLMTHFSCADD 165
Cdd:cd06808 78 AEQGvIVVTVDSLEELEKLEEAALKAgpPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLR-LVGLHTHFGSADE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 567929223 166 THNTkTAQQISLFDTLVKGID-------QAHcLSNSAGIIAW---PAGHGDWIRPGL 212
Cdd:cd06808 157 DYSP-FVEALSRFVAALDQLGelgidleQLS-IGGSFAILYLqelPLGTFIIVEPGR 211
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
7-353 |
7.43e-33 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is composed of bacterial alanine racemases (EC 5.1.1.1) with similarity to Yersinia pestis and Vibrio cholerae alanine racemase (AR) 2. ARs catalyze the interconversion between L- and D-alanine, an essential component of the peptidoglycan layer of bacterial cell walls. These proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143499 [Multi-domain] Cd Length: 365 Bit Score: 125.53 E-value: 7.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 7 EINLTALAHNLSQVK-RFAPNSKIMAVLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGGLTKPIVLLEGFfN 83
Cdd:cd06826 5 EISTGAFENNIKLLKkLLGGNTKLCAVMKADAYGHGIALVMPSIiaQNIPCVGITSNEEARVVREAGFTGKILRVRTA-T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 84 KADLPILLANNFQTIVHDENQLAAIEN--ATLDAPITCWLKINT-GMHRLGI----APEQFDAFysRLQRTPNAKsTINL 156
Cdd:cd06826 84 PSEIEDALAYNIEELIGSLDQAEQIDSlaKRHGKTLPVHLALNSgGMSRNGLelstAQGKEDAV--AIATLPNLK-IVGI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 157 MTHF---SCADDTHNTKTAQQISLFDTLVKGIDQAHCL---SNSAGIIAWPAGHGDWIRPGLMLYGVSPmancTGQEHnl 230
Cdd:cd06826 161 MTHFpveDEDDVRAKLARFNEDTAWLISNAKLKREKITlhaANSFATLNVPEAHLDMVRPGGILYGDTP----PSPEY-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 231 KPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPTQLAVVAMGYGDGYPRHAKEGTPVMIAGQRYGIVGSVSMDMISIDIG 310
Cdd:cd06826 235 KRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMVDVT 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 567929223 311 ENEhNVKVGDSVTMWG----PELPVEEIAHCADTIPYELLC---NITPRV 353
Cdd:cd06826 315 DIP-GVKAGDEVVLFGkqggAEITAAEIEEGSGTILAELYTlwgQTNPRV 363
|
|
| YhfX |
COG3457 |
Predicted amino acid racemase [Amino acid transport and metabolism]; |
7-325 |
9.64e-08 |
|
Predicted amino acid racemase [Amino acid transport and metabolism];
Pssm-ID: 442680 [Multi-domain] Cd Length: 356 Bit Score: 53.27 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 7 EINLTALAHNLSQVKRFAP--NSKIMAVLKANaygHGLVKIAQHLNSA--DAFAVARIDEALALRAGGLTKPIVLLEgff 82
Cdd:COG3457 7 VIDLDKIRENARRLVELAAkhGIELYGVTKQF---GGNPEIAKALLDGgiKGIVDSRIKNLKKLKRAGIPHPGHLLR--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 83 nkadLPIL-----LANNFQTI-VHDENQLAAIENATLDAPIT--CWLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKsTI 154
Cdd:COG3457 81 ----IPMLseveeVVRYADISlNSELETARALSEAAKKQGKVhkVILMVDLGDLREGGFPEELVDTVEEILKLPGIE-LA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 155 NLMTHFSCADDThnTKTAQQISLFDTLVKGIDQAHCLS-------NSAGI-----IAWPAG--HGdwiRPG-LMLYGVSP 219
Cdd:COG3457 156 GLGTNLPCFGGV--LPTEENLGTLLELAELLEAKFGIKlpivsggNSTSLpllaeGTLPKGinHL---RPGeALLLGTDP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 220 MANCTGqEHNLKPVMRLTTKVIAVRDVAAHERVGYGGRWQSDKPT-------QLAVVAMGYGDGYPRHAkegTPVMiagq 292
Cdd:COG3457 231 LNARPI-PGLEQDAFVLVAEIIELKEKPSVPIGEIGRDAFGNAPEfgdrgirKRAILAIGRQDVDPEGL---TPID---- 302
|
330 340 350
....*....|....*....|....*....|....*
gi 567929223 293 rYG--IVGSVSmDMISIDIGENEHNVKVGDSVTMW 325
Cdd:COG3457 303 -YGieILGASS-DHLILDVTDSKEDYKVGDTVVFC 335
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
7-325 |
6.48e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily is composed of uncharacterized bacterial proteins with similarity to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes.
Pssm-ID: 143490 [Multi-domain] Cd Length: 353 Bit Score: 44.46 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 7 EINLTALAHNLSQVK-RFAPNS-KIMAVLKANAyghGLVKIAQHLNSADA--FAVARIDEALALRAGGLTKPIVLL---- 78
Cdd:cd06815 5 EINLSKIRHNAKVLVeLCKSRGiEVTGVTKVVC---GDPEIAEALLEGGIthLADSRIENLKKLKDLGISGPKMLLripm 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 79 ----EGFFNKADLPIllaNNFQTIVHDENQLAAIENATLDapITcwLKINTGMHRLGIAPEQFDAFYSRLQRTPNAKsTI 154
Cdd:cd06815 82 lsevEDVVKYADISL---NSELETIKALSEEAKKQGKIHK--II--LMVDLGDLREGVLPEDLLDFVEEILKLPGIE-LV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 155 NLMTHFSC----ADDTHNtktaqqISLFDTLVKGIDQAHCLS-------NSAGIiawpaghgDWIRPGLM---------- 213
Cdd:cd06815 154 GIGTNLGCyggvLPTEEN------MGKLVELKEEIEKEFGIKlpiisggNSASL--------PLLLKGELpgginqlrig 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 214 ---LYGVSPMAN--CTGQEHNlkpVMRLTTKVIAVRD---VAAHERvGY--GGRWQS--DKPTQL-AVVAMGYGDGYPrh 280
Cdd:cd06815 220 eaiLLGRETTYNepIPGLYQD---AFTLEAEIIEIKEkpsVPIGEI-GLdaFGNKPEfeDRGIRKrAILAIGRQDVDP-- 293
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 567929223 281 akEGTPVMIAGQRygIVGSVSmDMISIDIGENEHNVKVGDSVTMW 325
Cdd:cd06815 294 --DGLTPVDNGIE--ILGASS-DHLILDITDSDRDYKVGDEIRFN 333
|
|
| PLPDE_III_ODC_DapDC_like |
cd06810 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate ... |
13-195 |
6.07e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Ornithine and Diaminopimelate Decarboxylases, and Related Enzymes; This family includes eukaryotic ornithine decarboxylase (ODC, EC 4.1.1.17), diaminopimelate decarboxylase (DapDC, EC 4.1.1.20), plant and prokaryotic biosynthetic arginine decarboxylase (ADC, EC 4.1.1.19), carboxynorspermidine decarboxylase (CANSDC), and ODC-like enzymes from diverse bacterial species. These proteins are fold type III PLP-dependent enzymes that catalyze essential steps in the biosynthesis of polyamine and lysine. ODC and ADC participate in alternative pathways of the biosynthesis of putrescine, which is the precursor of aliphatic polyamines in many organisms. ODC catalyzes the direct synthesis of putrescine from L-ornithine, while ADC converts L-arginine to agmatine, which is hydrolysed to putrescine by agmatinase in a pathway that exists only in plants and bacteria. DapDC converts meso-2,6-diaminoheptanedioate to L-lysine, which is the final step of lysine biosynthesis. CANSDC catalyzes the decarboxylation of carboxynorspermidine, which is the last step in the synthesis of norspermidine. The PLP-dependent decarboxylases in this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Prokaryotic ornithine, lysine and biodegradative arginine decarboxylases are fold type I PLP-dependent enzymes and are not included in this family.
Pssm-ID: 143485 [Multi-domain] Cd Length: 368 Bit Score: 41.52 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 13 LAHNLSQVKRFAPNSKIMAVLKANAYGHgLVKIAQHLnsADAFAVARIDE-ALALRAGGLTKPIVLLEGFFNKADLPILL 91
Cdd:cd06810 12 RAHYAALKEALPSGVKLFYAVKANPNPH-VLRTLAEA--GTGFDVASKGElALALAAGVPPERIIFTGPAKSVSEIEAAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 92 ANNFQTIVHD-ENQLAAIENATLDAPITC--WLKINTGM-------------HRLGIAPEQFDAFYSRLQRTPnaKSTIN 155
Cdd:cd06810 89 ASGVDHIVVDsLDELERLNELAKKLGPKAriLLRVNPDVsagthkistgglkSKFGLSLSEARAALERAKELD--LRLVG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 567929223 156 LMTHFSCaddthntktaqQISLFDTLVKGIDQAHCLSNSA 195
Cdd:cd06810 167 LHFHVGS-----------QILDLETIVQALSDARELIEEL 195
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
95-149 |
8.37e-04 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine aldolase (D-TA, EC 4.3.1.18) reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Its activity is present in several genera of bacteria but not in fungi. It requires PLP and a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ as cofactors for catalytic activity and thermal stability. Members of this subfamily show similarity to bacterial alanine racemase (AR), a fold type III PLP-dependent enzyme which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143495 [Multi-domain] Cd Length: 361 Bit Score: 40.74 E-value: 8.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 567929223 95 FQTIVHDENQLAAIENATLDA--PITCWLKINTGMHRLGIAPEQ-FDAFYSRLQRTPN 149
Cdd:cd06821 105 FSALVDDLEAAEALSAAAGSAglTLSVLLDVNTGMNRTGIAPGEdAEELYRAIATLPG 162
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
8-134 |
5.39e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; Low specificity D-threonine aldolase (Low specificity D-TA, EC 4.3.1.18), encoded by dtaAS gene from Arthrobacter sp. strain DK-38, is the prototype of this subfamily. Low specificity D-TAs are fold type III PLP-dependent enzymes that catalyze the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Members of this subfamily show similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143493 [Multi-domain] Cd Length: 358 Bit Score: 38.35 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567929223 8 INLTALAHNLSQVKRFAPNSKIMavLKANAYGHGLVKIAQHL--NSADAFAVARIDEALALRAGG-----LTKPIVLLeg 80
Cdd:cd06819 12 LDLDALERNIKRMAAFAKAHGVR--LRPHAKTHKCPAIARRQiaAGAVGVCCQKLSEAEVMAAAGirdilITNEVVGP-- 87
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 567929223 81 ffNKADLPILLANNFQTIV---HDEN--QLAAIENAtLDAPITCWLKINTGMHRLGIAP 134
Cdd:cd06819 88 --AKIARLAALARRAPLIVcvdHPDNvrALAAAAVE-AGVRLDVLVEIDVGQGRCGVPP 143
|
|
| |
