|
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: 573.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 4 ATAEINLTALAHNLAQVKGFAPNSKVMAVLKANAYGHGLVTIAQHLNNADAFAVARIDEGLALRAGGLTKPIVLLEGFFN 83
Cdd:cd06827 2 ARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 84 KADLPILLANNFQTIIHDEYQLAALEKAKLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAkNTVNLMTHFSCA 163
Cdd:cd06827 82 ADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNV-ASIVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 164 DDVDNAKTVQQITLFDNLVNGIDQAHCLSNSAGIIAWPSGHGDWVRPGLMLYGVSPMANSIGQQHKLKPVMRLTTRVIAV 243
Cdd:cd06827 161 DEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 244 RDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIGANEhNIKVGDRVT 323
Cdd:cd06827 241 RELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLP-EAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 639323649 324 MWGPELPVEEIALCADTIPYELLCNITPRVSYEYQ 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: 513.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 1 MRLATAEINLTALAHNLAQVKGFAP-NSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPpKSKLMAVVKANAYGHGAVEVAKTLleAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 78 LEGFFNKADLPILLANNFQTIIHDEYQLAALEKAKLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAkNTVNLM 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNV-RLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 158 THFSCADDVDNAKTVQQITLFDNLVNGID-----QAHcLSNSAGIIAWPSGHGDWVRPGLMLYGVSPMANSIGQQHKLKP 232
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPgkgkpLRH-LANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 233 VMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIGAN 312
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 639323649 313 EhNIKVGDRVTMWGPELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:PRK00053 319 P-QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-357 |
6.41e-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: 475.37 E-value: 6.41e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 1 MRLATAEINLTALAHNLAQVKGFA-PNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALleAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 78 LEGFFnKADLPILLANNFQTIIHDEYQLAALEKA--KLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKnTVN 155
Cdd:COG0787 81 LGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLE-VEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 156 LMTHFSCADDVDNAKTVQQITLFDNLVNGIDQAH------CLSNSAGIIAWPSGHGDWVRPGLMLYGVSPMANsIGQQHK 229
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAGldpplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE-VAADLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 230 LKPVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDI 309
Cdd:COG0787 238 LKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 639323649 310 GANEhNIKVGDRVTMWGPE-LPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:COG0787 318 TDIP-DVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVY 365
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-357 |
2.66e-136 |
|
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: 392.49 E-value: 2.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 2 RLATAEINLTALAHNLAQVKGF-APNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLlqAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 79 EGFFNKaDLPILLANNFQTIIHDEYQLAALEKAKLDAP--ITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKNTVNL 156
Cdd:TIGR00492 81 GGFFAE-DLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 157 MTHFSCADDVDNAKTVQQITLFDNLVNGIDQAHC------LSNSAGIIAWPSGHGDWVRPGLMLYGVSPMAN-SIGQQHK 229
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIeppfrhIANSAAILNWPESHFDMVRPGIILYGLYPSADmSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 230 LKPVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDI 309
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 639323649 310 GANEhNIKVGDRVTMWGPELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:TIGR00492 320 GPDL-QDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
1.91e-78 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 239.82 E-value: 1.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 8 INLTALAHNLAQVKGFA-PNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVLLEGFfNK 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 85 ADLPILLANNFQTIIHDEYQLAALEKA--KLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKNtVNLMTHFSC 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRL-EGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639323649 163 ADDVDNAKTVQQITLFDNLVNGIDQAH------CLSNSAGIIAWPsGHGDWVRPGLMLYGVSP 219
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAGlrppvvHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-357 |
3.76e-56 |
|
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: 179.19 E-value: 3.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 233 VMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKeGTPVIIGEQRYGIVGSVAMDMISVDIGAN 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 639323649 313 EhNIKVGDRVTMWGP-ELPVEEIALCADTIPYELLCNITPRVSYEY 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: 573.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 4 ATAEINLTALAHNLAQVKGFAPNSKVMAVLKANAYGHGLVTIAQHLNNADAFAVARIDEGLALRAGGLTKPIVLLEGFFN 83
Cdd:cd06827 2 ARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 84 KADLPILLANNFQTIIHDEYQLAALEKAKLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAkNTVNLMTHFSCA 163
Cdd:cd06827 82 ADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNV-ASIVLMTHFACA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 164 DDVDNAKTVQQITLFDNLVNGIDQAHCLSNSAGIIAWPSGHGDWVRPGLMLYGVSPMANSIGQQHKLKPVMRLTTRVIAV 243
Cdd:cd06827 161 DEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIAV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 244 RDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIGANEhNIKVGDRVT 323
Cdd:cd06827 241 RELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLP-EAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....*
gi 639323649 324 MWGPELPVEEIALCADTIPYELLCNITPRVSYEYQ 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: 513.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 1 MRLATAEINLTALAHNLAQVKGFAP-NSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPpKSKLMAVVKANAYGHGAVEVAKTLleAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 78 LEGFFNKADLPILLANNFQTIIHDEYQLAALEKAKLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAkNTVNLM 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNV-RLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 158 THFSCADDVDNAKTVQQITLFDNLVNGID-----QAHcLSNSAGIIAWPSGHGDWVRPGLMLYGVSPMANSIGQQHKLKP 232
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPgkgkpLRH-LANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 233 VMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIGAN 312
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 639323649 313 EhNIKVGDRVTMWGPELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:PRK00053 319 P-QDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-357 |
6.41e-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: 475.37 E-value: 6.41e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 1 MRLATAEINLTALAHNLAQVKGFA-PNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVL 77
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALleAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 78 LEGFFnKADLPILLANNFQTIIHDEYQLAALEKA--KLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKnTVN 155
Cdd:COG0787 81 LGGVP-PEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLE-VEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 156 LMTHFSCADDVDNAKTVQQITLFDNLVNGIDQAH------CLSNSAGIIAWPSGHGDWVRPGLMLYGVSPMANsIGQQHK 229
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAGldpplrHLANSAAILRYPEAHFDMVRPGIALYGLSPSPE-VAADLG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 230 LKPVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDI 309
Cdd:COG0787 238 LKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 639323649 310 GANEhNIKVGDRVTMWGPE-LPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:COG0787 318 TDIP-DVKVGDEVVLFGEQgITADELAEAAGTISYEILTRLGPRVPRVY 365
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
4-353 |
3.42e-141 |
|
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: 404.96 E-value: 3.42e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 4 ATAEINLTALAHNLAQVKGFA-PNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVLLEG 80
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLgPGTKIMAVVKADAYGHGAVEVAKALeeAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 81 FFNkADLPILLANNFQTIIHDEYQLAALEKA--KLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKNTvNLMT 158
Cdd:cd00430 82 TPP-EEAEEAIEYDLTPTVSSLEQAEALSAAaaRLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELE-GVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 159 HFSCADDVDNAKTVQQITLFDNLVNGIDQA-------HClSNSAGIIAWPSGHGDWVRPGLMLYGVSPmANSIGQQHKLK 231
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAELEEAgippplkHL-ANSAAILRFPEAHFDMVRPGIALYGLYP-SPEVKSPLGLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 232 PVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIGa 311
Cdd:cd00430 238 PVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVT- 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 639323649 312 NEHNIKVGDRVTMWGP----ELPVEEIALCADTIPYELLCNITPRV 353
Cdd:cd00430 317 DIPDVKVGDEVVLFGRqgdeEITAEELAELAGTINYEILCRISKRV 362
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-357 |
2.78e-138 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 397.18 E-value: 2.78e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 1 MRLATAEINLTALAHNLAQVKGFAPNSKVMAVLKANAYGHGLVTIAQHLNNADAFAVARIDEGLALRAGGLTKPIVLLEG 80
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 81 FFNKADLPILLANNFQTIIHDEYQLAALEKAKLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKNTVnLMTHF 160
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMT-LMSHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 161 SCADDVDNakTVQQITLFDNLVNGIDQAHCLSNSAGIIAWPSGHGDWVRPGLMLYGVSPM--ANSIGQQhKLKPVMRLTT 238
Cdd:PRK03646 160 ARADHPDG--ISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSgqWRDIANT-GLRPVMTLSS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 239 RVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIgANEHNIKV 318
Cdd:PRK03646 237 EIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDL-TPCPQAGI 315
|
330 340 350
....*....|....*....|....*....|....*....
gi 639323649 319 GDRVTMWGPELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:PRK03646 316 GTPVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-357 |
2.66e-136 |
|
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: 392.49 E-value: 2.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 2 RLATAEINLTALAHNLAQVKGF-APNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHiGPKSKIMAVVKANAYGHGLIEVAKTLlqAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 79 EGFFNKaDLPILLANNFQTIIHDEYQLAALEKAKLDAP--ITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKNTVNL 156
Cdd:TIGR00492 81 GGFFAE-DLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 157 MTHFSCADDVDNAKTVQQITLFDNLVNGIDQAHC------LSNSAGIIAWPSGHGDWVRPGLMLYGVSPMAN-SIGQQHK 229
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQQNIeppfrhIANSAAILNWPESHFDMVRPGIILYGLYPSADmSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 230 LKPVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDI 309
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 639323649 310 GANEhNIKVGDRVTMWGPELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:TIGR00492 320 GPDL-QDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
4-357 |
8.08e-94 |
|
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: 284.25 E-value: 8.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 4 ATAEINLTALAHNLAQVKGFAP-NSKVMAVLKANAYGHGLVTIAQHLNNA--DAFAVARIDEGLALRAGGLTKPIVLLeG 80
Cdd:cd06825 2 AWLEIDLSALEHNVKEIKRLLPsTCKLMAVVKANAYGHGDVEVARVLEQIgiDFFAVATIDEGIRLREAGIKGEILIL-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 81 FFNKADLPILLANNF-QTIIHDEYqlaALEKAKLDAPITCWLKVNTGMHRLGIAPEQFEAFySRLQKTPNAKNTvNLMTH 159
Cdd:cd06825 81 YTPPVRAKELKKYSLtQTLISEAY---AEELSKYAVNIKVHLKVDTGMHRLGESPEDIDSI-LAIYRLKNLKVS-GIFSH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 160 FSCADDVDNAK---TVQQITLFDNLVNGIDQAH------CLSNSAGIIAWPSGHGDWVRPGLMLYGV-SPMANSIGQQHK 229
Cdd:cd06825 156 LCVSDSLDEDDiafTKHQIACFDQVLADLKARGievgkiHIQSSYGILNYPDLKYDYVRPGILLYGVlSDPNDPTKLGLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 230 LKPVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRH-AKEGTPVIIGEQRYGIVGSVAMDMISVD 308
Cdd:cd06825 236 LRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSlSNQKAYVLINGKRAPIIGNICMDQLMVD 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 639323649 309 IGANEhNIKVGDRVTMWG----PELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:cd06825 316 VTDIP-EVKEGDTATLIGqdgdEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
7-353 |
3.92e-83 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 269.13 E-value: 3.92e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 7 EINLTALAHNLAQVKGF-APNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVLLegffN 83
Cdd:PRK11930 463 EINLNAIVHNLNYYRSKlKPETKIMCMVKAFAYGSGSYEIAKLLqeHRVDYLAVAYADEGVSLRKAGITLPIMVM----N 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 84 KAdlpillANNFQTIIhdEYQL----------AALEKAKLDAPITCW---LKVNTGMHRLGIAPEQFEAFYSRLQKTPNA 150
Cdd:PRK11930 539 PE------PTSFDTII--DYKLepeiysfrllDAFIKAAQKKGITGYpihIKIDTGMHRLGFEPEDIPELARRLKKQPAL 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 151 K-NTVnlMTHFSCADDVD-NAKTVQQITLFDNLVNGIdQAHC-------LSNSAGIIAWPSGHGDWVRPGLMLYGVSPma 221
Cdd:PRK11930 611 KvRSV--FSHLAGSDDPDhDDFTRQQIELFDEGSEEL-QEALgykpirhILNSAGIERFPDYQYDMVRLGIGLYGVSA-- 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 222 nSIGQQHKLKPVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGT-PVIIGEQRYGIVGSV 300
Cdd:PRK11930 686 -SGAGQQALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNI 764
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 639323649 301 AMDMISVDIGanehNI--KVGDRVTMWGPELPVEEIALCADTIPYELLCNITPRV 353
Cdd:PRK11930 765 CMDMCMIDVT----DIdaKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRV 815
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
1.91e-78 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 239.82 E-value: 1.91e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 8 INLTALAHNLAQVKGFA-PNSKVMAVLKANAYGHGLVTIAQHL--NNADAFAVARIDEGLALRAGGLTKPIVLLEGFfNK 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALleGGADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 85 ADLPILLANNFQTIIHDEYQLAALEKA--KLDAPITCWLKVNTGMHRLGIAPEQFEAFYSRLQKTPNAKNtVNLMTHFSC 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRL-EGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639323649 163 ADDVDNAKTVQQITLFDNLVNGIDQAH------CLSNSAGIIAWPsGHGDWVRPGLMLYGVSP 219
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAGlrppvvHLANSAAILLHP-LHFDMVRPGIALYGLSP 220
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
4-347 |
8.40e-72 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 229.13 E-value: 8.40e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 4 ATAEINLTALAHNLAQVKGFAPN-SKVMAVLKANAYGHG--LVTIAQHLNNADAFAVARIDEGLALRAGGLTKPIVLLEG 80
Cdd:PRK13340 41 AWLEISPGAFRHNIKTLRSLLANkSKVCAVMKADAYGHGieLLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLRVRS 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 81 FfNKADLPILLANNFQTIIHDEYQLAALEK--AKLDAPITCWLKVNT-GMHRLGIAPEQFEAFYSRLQ--KTPNAKNtVN 155
Cdd:PRK13340 121 A-SPAEIEQALRYDLEELIGDDEQAKLLAAiaKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWEALRiaTLPSLGI-VG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 156 LMTHFSCAD--DVDnaktvQQITLFDNLVNGIDQAHCL---------SNSAGIIAWPSGHGDWVRPGLMLYGVSPMANSi 224
Cdd:PRK13340 199 IMTHFPNEDedEVR-----WKLAQFKEQTAWLIGEAGLkrekitlhvANSYATLNVPEAHLDMVRPGGILYGDRHPANT- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 225 gqqhKLKPVMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDM 304
Cdd:PRK13340 273 ----EYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNT 348
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 639323649 305 ISVDIgANEHNIKVGDRVTMWG----PELPVEEIALCADTIPYELLC 347
Cdd:PRK13340 349 LMVDV-TDIPNVKPGDEVVLFGkqgnAEITVDEVEEASGTIFPELYT 394
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-357 |
3.76e-56 |
|
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: 179.19 E-value: 3.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 233 VMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKeGTPVIIGEQRYGIVGSVAMDMISVDIGAN 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 639323649 313 EhNIKVGDRVTMWGP-ELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:smart01005 80 P-DVKVGDEVVLFGPqEITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
233-357 |
8.08e-55 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 176.02 E-value: 8.08e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 233 VMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIGaN 312
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVT-D 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 639323649 313 EHNIKVGDRVTMWGP----ELPVEEIALCADTIPYELLCNITPRVSYEY 357
Cdd:pfam00842 80 VPEVKVGDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
7-353 |
3.20e-34 |
|
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: 129.38 E-value: 3.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 7 EINLTALAHNLAQVKGFAP-NSKVMAVLKANAYGHG--LVTIAQHLNNADAFAVARIDEGLALRAGGLTKPIVLLEGFfN 83
Cdd:cd06826 5 EISTGAFENNIKLLKKLLGgNTKLCAVMKADAYGHGiaLVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTA-T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 84 KADLPILLANNFQTIIHDEYQLAALEK--AKLDAPITCWLKVNT-GMHRLGI--APEQFEAFYSRLQKTPNAKnTVNLMT 158
Cdd:cd06826 84 PSEIEDALAYNIEELIGSLDQAEQIDSlaKRHGKTLPVHLALNSgGMSRNGLelSTAQGKEDAVAIATLPNLK-IVGIMT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 159 HFSC--ADDV-DNAKTVQQITLFDNLVNGIDQAHCL---SNSAGIIAWPSGHGDWVRPGLMLYGVSPMANSIgqqhklKP 232
Cdd:cd06826 163 HFPVedEDDVrAKLARFNEDTAWLISNAKLKREKITlhaANSFATLNVPEAHLDMVRPGGILYGDTPPSPEY------KR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 233 VMRLTTRVIAVRDVPANEAVGYGGRWKSDKPTKLAVVAMGYGDGYPRHAKEGTPVIIGEQRYGIVGSVAMDMISVDIgAN 312
Cdd:cd06826 237 IMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMVDV-TD 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 639323649 313 EHNIKVGDRVTMWG----PELPVEEIALCADTIPYELLC---NITPRV 353
Cdd:cd06826 316 IPGVKAGDEVVLFGkqggAEITAAEIEEGSGTILAELYTlwgQTNPRV 363
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
13-212 |
7.76e-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: 124.35 E-value: 7.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 13 LAHNLAQVKGFAP-NSKVMAVLKANAYGHGLVTIAQHlnnADAFAVARIDEGLALRAGGL-TKPIVLLEGFFNKADLPIL 90
Cdd:cd06808 1 IRHNYRRLREAAPaGITLFAVVKANANPEVARTLAAL---GTGFDVASLGEALLLRAAGIpPEPILFLGPCKQVSELEDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639323649 91 LANN-FQTIIHDEYQLAALEKA--KLDAPITCWLKVNTG--MHRLGIAPEQFEAFYSRLQKTPNAKnTVNLMTHFSCADD 165
Cdd:cd06808 78 AEQGvIVVTVDSLEELEKLEEAalKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLR-LVGLHTHFGSADE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 639323649 166 vDNAKTVQQIT----LFDNLVNG---IDQAHcLSNSAGIIAW---PSGHGDWVRPGL 212
Cdd:cd06808 157 -DYSPFVEALSrfvaALDQLGELgidLEQLS-IGGSFAILYLqelPLGTFIIVEPGR 211
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| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
95-149 |
1.01e-04 |
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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: 43.82 E-value: 1.01e-04
10 20 30 40 50
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gi 639323649 95 FQTIIHDEYQLAALEKAKLDA--PITCWLKVNTGMHRLGIAPEQ-FEAFYSRLQKTPN 149
Cdd:cd06821 105 FSALVDDLEAAEALSAAAGSAglTLSVLLDVNTGMNRTGIAPGEdAEELYRAIATLPG 162
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