|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-356 |
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: 579.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 3 PLVATVDLSAIRHNYALAKRCAPQRQAFAVVKANAYGHGAREVVTALhDDADGFAVACLEEAAEVRALHASARILLLEGC 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKAL-ADADGFAVACIEEALALREAGITKPILLLEGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 83 FEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLISHFAC 162
Cdd:cd06827 80 FSADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 163 ADERNHPLTEQQLESFLGLLDLDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLSAAELGLKPAMSLGAQLIS 242
Cdd:cd06827 160 ADEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 243 LREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDLPEARVGDPVE 322
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....
gi 15600123 323 LWGAGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVY 353
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-358 |
3.06e-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: 476.14 E-value: 3.06e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 1 MRPLVATVDLSAIRHNY-ALAKRCAPQRQAFAVVKANAYGHGAREVVTALHD-DADGFAVACLEEAAEVRALHASARILL 78
Cdd:COG0787 1 SRPAWAEIDLDALRHNLrVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEaGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 79 LEGcFEASEYALAGQLRLDLVIQGAEQGEAFLAAG--LDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNL 156
Cdd:COG0787 81 LGG-VPPEDLELAIEYDLEPVVHSLEQLEALAAAArrLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 157 ISHFACADERNHPLTEQQLESFLGLLD------LDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLsAAELGL 230
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAalpaagLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEV-AADLGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 231 KPAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLS 310
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVT 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15600123 311 DLPEARVGDPVELWGA-GLSVDEVARACGTLGYELLSKVTARVPRRYSH 358
Cdd:COG0787 319 DIPDVKVGDEVVLFGEqGITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-356 |
2.46e-159 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 450.78 E-value: 2.46e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 1 MRPLVATVDLSAIRHNYALAKRCAPQR-QAFAVVKANAYGHGAREVV-TALHDDADGFAVACLEEAAEVRALHASARILL 78
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPKsKLMAVVKANAYGHGAVEVAkTLLEAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 79 LEGCFEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLIS 158
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 159 HFACADERNHPLTEQQLESFL----GLLDLDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLSAAELGLKPAM 234
Cdd:PRK00053 161 HFATADEPDNSYTEQQLNRFEaalaGLPGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 235 SLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDLPE 314
Cdd:PRK00053 241 TLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDPQ 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15600123 315 ARVGDPVELWGAGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:PRK00053 321 DKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-356 |
6.83e-121 |
|
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: 353.20 E-value: 6.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 2 RPLVATVDLSAIRHNYALAKR-CAPQRQAFAVVKANAYGHGAREVV-TALHDDADGFAVACLEEAAEVRALHASARILLL 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNhIGPKSKIMAVVKANAYGHGLIEVAkTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 80 EGcFEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIP--LNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVREL-NL 156
Cdd:TIGR00492 81 GG-FFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELeGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 157 ISHFACADERNHPLTEQQLESFLGLLD------LDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLS-AAELG 229
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEglkqqnIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSdGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 230 LKPAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDL 309
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15600123 310 SDLPEARVGDPVELWGAGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
9.46e-71 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 220.17 E-value: 9.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 8 VDLSAIRHNYA-LAKRCAPQRQAFAVVKANAYGHGAREVVTALHD-DADGFAVACLEEAAEVRALHASARILLLEGcFEA 85
Cdd:pfam01168 1 IDLDALRHNLRrLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEgGADGFAVATLDEALELREAGITAPILVLGG-FPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 86 SEYALAGQLRLDLVIQGAEQGEAFLAAGLDI--PLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLISHFACA 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAARRLgkPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600123 164 DERNHPLTEQQLESFLGLLD------LDFDQRSLANSAAVLTiPAAHMDWLRPGIMLYGSTP 219
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAaleaagLRPPVVHLANSAAILL-HPLHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-356 |
2.83e-62 |
|
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: 194.98 E-value: 2.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 233 AMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPaGTPVLVGGRRAILAGRVSMDMLAVDLSDL 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15600123 313 PEARVGDPVELWGAG-LSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:smart01005 80 PDVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-356 |
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: 579.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 3 PLVATVDLSAIRHNYALAKRCAPQRQAFAVVKANAYGHGAREVVTALhDDADGFAVACLEEAAEVRALHASARILLLEGC 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKAL-ADADGFAVACIEEALALREAGITKPILLLEGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 83 FEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLISHFAC 162
Cdd:cd06827 80 FSADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNVASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 163 ADERNHPLTEQQLESFLGLLDLDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLSAAELGLKPAMSLGAQLIS 242
Cdd:cd06827 160 ADEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVMTLSSEIIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 243 LREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDLPEARVGDPVE 322
Cdd:cd06827 240 VRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPVE 319
|
330 340 350
....*....|....*....|....*....|....
gi 15600123 323 LWGAGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:cd06827 320 LWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVY 353
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
1-358 |
3.06e-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: 476.14 E-value: 3.06e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 1 MRPLVATVDLSAIRHNY-ALAKRCAPQRQAFAVVKANAYGHGAREVVTALHD-DADGFAVACLEEAAEVRALHASARILL 78
Cdd:COG0787 1 SRPAWAEIDLDALRHNLrVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEaGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 79 LEGcFEASEYALAGQLRLDLVIQGAEQGEAFLAAG--LDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNL 156
Cdd:COG0787 81 LGG-VPPEDLELAIEYDLEPVVHSLEQLEALAAAArrLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 157 ISHFACADERNHPLTEQQLESFLGLLD------LDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLsAAELGL 230
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAalpaagLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEV-AADLGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 231 KPAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLS 310
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVT 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15600123 311 DLPEARVGDPVELWGA-GLSVDEVARACGTLGYELLSKVTARVPRRYSH 358
Cdd:COG0787 319 DIPDVKVGDEVVLFGEqGITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-356 |
2.46e-159 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 450.78 E-value: 2.46e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 1 MRPLVATVDLSAIRHNYALAKRCAPQR-QAFAVVKANAYGHGAREVV-TALHDDADGFAVACLEEAAEVRALHASARILL 78
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPKsKLMAVVKANAYGHGAVEVAkTLLEAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 79 LEGCFEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLIS 158
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRLEGIFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 159 HFACADERNHPLTEQQLESFL----GLLDLDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLSAAELGLKPAM 234
Cdd:PRK00053 161 HFATADEPDNSYTEQQLNRFEaalaGLPGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKPAM 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 235 SLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDLPE 314
Cdd:PRK00053 241 TLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPDPQ 320
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 15600123 315 ARVGDPVELWGAGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:PRK00053 321 DKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-357 |
2.37e-138 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 397.18 E-value: 2.37e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 1 MRPLVATVDLSAIRHNYALAKRCAPQRQAFAVVKANAYGHGAREVVTALhDDADGFAVACLEEAAEVRALHASARILLLE 80
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSAL-GATDGFAVLNLEEAITLRERGWKGPILMLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 81 GCFEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLISHF 160
Cdd:PRK03646 80 GFFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMTLMSHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 161 ACADERNHplTEQQLESFLGLLDLDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLSA-AELGLKPAMSLGAQ 239
Cdd:PRK03646 160 ARADHPDG--ISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDiANTGLRPVMTLSSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 240 LISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDLPEARVGD 319
Cdd:PRK03646 238 IIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGT 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 15600123 320 PVELWGAGLSVDEVARACGTLGYELLSKVTARVPRRYS 357
Cdd:PRK03646 318 PVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
6-356 |
4.50e-135 |
|
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: 389.16 E-value: 4.50e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 6 ATVDLSAIRHNY-ALAKRCAPQRQAFAVVKANAYGHGAREVVTALHD-DADGFAVACLEEAAEVRALHASARILLLEGCF 83
Cdd:cd00430 4 AEIDLDALRHNLrVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEaGADYFAVATLEEALELREAGITAPILVLGGTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 84 EaSEYALAGQLRLDLVIQGAEQGEAF--LAAGLDIPLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLISHFA 161
Cdd:cd00430 84 P-EEAEEAIEYDLTPTVSSLEQAEALsaAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVFTHFA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 162 CADERNHPLTEQQLESFLGLLD------LDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLSAAeLGLKPAMS 235
Cdd:cd00430 163 TADEPDKAYTRRQLERFLEALAeleeagIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSP-LGLKPVMS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 236 LGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDLPEA 315
Cdd:cd00430 242 LKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTDIPDV 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 15600123 316 RVGDPVELWGAG----LSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:cd00430 322 KVGDEVVLFGRQgdeeITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-356 |
6.83e-121 |
|
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: 353.20 E-value: 6.83e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 2 RPLVATVDLSAIRHNYALAKR-CAPQRQAFAVVKANAYGHGAREVV-TALHDDADGFAVACLEEAAEVRALHASARILLL 79
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNhIGPKSKIMAVVKANAYGHGLIEVAkTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 80 EGcFEASEYALAGQLRLDLVIQGAEQGEAFLAAGLDIP--LNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVREL-NL 156
Cdd:TIGR00492 81 GG-FFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELeGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 157 ISHFACADERNHPLTEQQLESFLGLLD------LDFDQRSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLADLS-AAELG 229
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEglkqqnIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSdGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 230 LKPAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDL 309
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15600123 310 SDLPEARVGDPVELWGAGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
2-356 |
5.37e-91 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 278.43 E-value: 5.37e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 2 RPLVATVDLSAIRHNYALAKRCAPQR-QAFAVVKANAYGHGAREVV-TALHDDADGFAVACLEEAAEVRALHASARILLL 79
Cdd:PRK13340 39 RNAWLEISPGAFRHNIKTLRSLLANKsKVCAVMKADAYGHGIELLMpSIIKANVPCIGIASNEEARRVRELGFTGQLLRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 80 EGCfEASEYALAGQLRLDLVIQGAEQGE--AFLAAGLDIPLNVWLKLDS-GMHRLGFDPAALR-AWHA-RLRSHPGVREL 154
Cdd:PRK13340 119 RSA-SPAEIEQALRYDLEELIGDDEQAKllAAIAKKNGKPIDIHLALNSgGMSRNGLDMSTARgKWEAlRIATLPSLGIV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 155 NLISHFACADERNhplTEQQLESF----LGLLD---LDFDQRSL--ANSAAVLTIPAAHMDWLRPGIMLYGstplaDLSA 225
Cdd:PRK13340 198 GIMTHFPNEDEDE---VRWKLAQFkeqtAWLIGeagLKREKITLhvANSYATLNVPEAHLDMVRPGGILYG-----DRHP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 226 AELGLKPAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDML 305
Cdd:PRK13340 270 ANTEYKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTL 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 15600123 306 AVDLSDLPEARVGDPVELWG----AGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:PRK13340 350 MVDVTDIPNVKPGDEVVLFGkqgnAEITVDEVEEASGTIFPELYTAWGRTNPRIY 404
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
8-356 |
6.58e-79 |
|
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: 246.11 E-value: 6.58e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 8 VDLSAIRHNYALAKRCAPQR-QAFAVVKANAYGHGAREVVTALHD-DADGFAVACLEEAAEVRALHASARILLLeGCFEA 85
Cdd:cd06825 6 IDLSALEHNVKEIKRLLPSTcKLMAVVKANAYGHGDVEVARVLEQiGIDFFAVATIDEGIRLREAGIKGEILIL-GYTPP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 86 SEYALAGQLRLDLVIQGAEQGEAFLAAGLDIplNVWLKLDSGMHRLGFDPAALRAWHArLRSHPGVRELNLISHFA---C 162
Cdd:cd06825 85 VRAKELKKYSLTQTLISEAYAEELSKYAVNI--KVHLKVDTGMHRLGESPEDIDSILA-IYRLKNLKVSGIFSHLCvsdS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 163 ADERNHPLTEQQLESFLGLLDlDFDQRSLA-------NSAAVLTIPAAHMDWLRPGIMLYG--STPLaDLSAAELGLKPA 233
Cdd:cd06825 162 LDEDDIAFTKHQIACFDQVLA-DLKARGIEvgkihiqSSYGILNYPDLKYDYVRPGILLYGvlSDPN-DPTKLGLDLRPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 234 MSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRT-APAGTPVLVGGRRAILAGRVSMDMLAVDLSDL 312
Cdd:cd06825 240 LSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSlSNQKAYVLINGKRAPIIGNICMDQLMVDVTDI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15600123 313 PEARVGDPVELWG----AGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:cd06825 320 PEVKEGDTATLIGqdgdEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
9.46e-71 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 220.17 E-value: 9.46e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 8 VDLSAIRHNYA-LAKRCAPQRQAFAVVKANAYGHGAREVVTALHD-DADGFAVACLEEAAEVRALHASARILLLEGcFEA 85
Cdd:pfam01168 1 IDLDALRHNLRrLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEgGADGFAVATLDEALELREAGITAPILVLGG-FPP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 86 SEYALAGQLRLDLVIQGAEQGEAFLAAGLDI--PLNVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVRELNLISHFACA 163
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAARRLgkPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600123 164 DERNHPLTEQQLESFLGLLD------LDFDQRSLANSAAVLTiPAAHMDWLRPGIMLYGSTP 219
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAaleaagLRPPVVHLANSAAILL-HPLHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
233-356 |
2.83e-62 |
|
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: 194.98 E-value: 2.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 233 AMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPaGTPVLVGGRRAILAGRVSMDMLAVDLSDL 312
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALS-NGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 15600123 313 PEARVGDPVELWGAG-LSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:smart01005 80 PDVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
233-356 |
8.96e-61 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 191.04 E-value: 8.96e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 233 AMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSDL 312
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15600123 313 PEARVGDPVELWG----AGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:pfam00842 81 PEVKVGDEVTLFGkqgdEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
8-356 |
6.93e-60 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 206.35 E-value: 6.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 8 VDLSAIRHNYALAK-RCAPQRQAFAVVKANAYGHGAREVVTAL-HDDADGFAVACLEEAAEVR-------------ALHA 72
Cdd:PRK11930 464 INLNAIVHNLNYYRsKLKPETKIMCMVKAFAYGSGSYEIAKLLqEHRVDYLAVAYADEGVSLRkagitlpimvmnpEPTS 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 73 SARILLLEgcFEASEYALAGqlrLDLVIQGAEQgeaflAAGLDIPlnVWLKLDSGMHRLGFDPAALRAWHARLRSHPGVR 152
Cdd:PRK11930 544 FDTIIDYK--LEPEIYSFRL---LDAFIKAAQK-----KGITGYP--IHIKIDTGMHRLGFEPEDIPELARRLKKQPALK 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 153 ELNLISHFACADERNH-PLTEQQLESFL---GLLDLDFDQ---RSLANSAAVLTIPAAHMDWLRPGIMLYGSTPLAdlsA 225
Cdd:PRK11930 612 VRSVFSHLAGSDDPDHdDFTRQQIELFDegsEELQEALGYkpiRHILNSAGIERFPDYQYDMVRLGIGLYGVSASG---A 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 226 AELGLKPAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGT-PVLVGGRRAILAGRVSMDM 304
Cdd:PRK11930 689 GQQALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNICMDM 768
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 15600123 305 LAVDLSDLPeARVGDPVELWGAGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:PRK11930 769 CMIDVTDID-AKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
8-356 |
6.44e-44 |
|
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: 155.19 E-value: 6.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 8 VDLSAIRHNYALAK-RCAPQRQAFAVVKANAYGHGAREVV-TALHDDADGFAVACLEEAAEVRALHASARILLLEGCfEA 85
Cdd:cd06826 6 ISTGAFENNIKLLKkLLGGNTKLCAVMKADAYGHGIALVMpSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTA-TP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 86 SEYALAGQLRLDLVIQGAEQGEAF--LAAGLDIPLNVWLKLDS-GMHRLGFDpaaLRAWHA-----RLRSHPGVRELNLI 157
Cdd:cd06826 85 SEIEDALAYNIEELIGSLDQAEQIdsLAKRHGKTLPVHLALNSgGMSRNGLE---LSTAQGkedavAIATLPNLKIVGIM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 158 SHFACADERNHPLTEQQLESFLGLL----DLDFDQRSL--ANSAAVLTIPAAHMDWLRPGIMLYGSTPladlsaAELGLK 231
Cdd:cd06826 162 THFPVEDEDDVRAKLARFNEDTAWLisnaKLKREKITLhaANSFATLNVPEAHLDMVRPGGILYGDTP------PSPEYK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 232 PAMSLGAQLISLREVAVGESVGYGATWIAERPARIGTVSCGYADGYPRTAPAGTPVLVGGRRAILAGRVSMDMLAVDLSD 311
Cdd:cd06826 236 RIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVMVDVTD 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 15600123 312 LPEARVGDPVELWG----AGLSVDEVARACGTLGYELLSKVTARVPRRY 356
Cdd:cd06826 316 IPGVKAGDEVVLFGkqggAEITAAEIEEGSGTILAELYTLWGQTNPRVY 364
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
13-212 |
1.00e-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: 126.66 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 13 IRHNYALAKRCAPQR-QAFAVVKANAYGHGARevvtALHDDADGFAVACLEEAAEVRAL-HASARILLLEGCFEASEYAL 90
Cdd:cd06808 1 IRHNYRRLREAAPAGiTLFAVVKANANPEVAR----TLAALGTGFDVASLGEALLLRAAgIPPEPILFLGPCKQVSELED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 91 A-GQLRLDLVIQGAEQGEAF--LAAGLDIPLNVWLKLDSG--MHRLGFDPAALRAWHARLRSHPGVRELNLISHFACADE 165
Cdd:cd06808 77 AaEQGVIVVTVDSLEELEKLeeAALKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHLRLVGLHTHFGSADE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 15600123 166 RNHPlTEQQLESFLGLLD------LDFDQRSLANSAAVLTI---PAAHMDWLRPGI 212
Cdd:cd06808 157 DYSP-FVEALSRFVAALDqlgelgIDLEQLSIGGSFAILYLqelPLGTFIIVEPGR 211
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
5-152 |
1.97e-03 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 39.73 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 5 VATVDLSAIRHNYA-LAKRCAPQRQAFAV-VKAnaygHGAREVVTALHDD-ADGFAVACLEEaAEVRALHASARILLleg 81
Cdd:COG3616 10 ALVLDLDALERNIArMAARAAAHGVRLRPhGKT----HKSPELARRQLAAgAWGITVATLAE-AEVLAAAGVDDILL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 82 cfeAseYALAGQLRLDLVIQGAEQGEAF---------------LAAGLDIPLNVWLKLDSGMHRLG-FDPAALRAWHARL 145
Cdd:COG3616 82 ---A--YPLVGPAKLARLAALARAGARLtvlvdsveqaealaaAAAAAGRPLRVLVELDVGGGRTGvRPPEAALALARAI 156
|
....*..
gi 15600123 146 RSHPGVR 152
Cdd:COG3616 157 AASPGLR 163
|
|
| PLPDE_III_PvsE_like |
cd06843 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE ... |
3-165 |
7.71e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme PvsE; This subfamily is composed of PvsE from Vibrio parahaemolyticus and similar proteins. PvsE is a vibrioferrin biosynthesis protein which is homologous to eukaryotic ornithine decarboxylase (ODC) and diaminopimelate decarboxylase (DapDC). ODC and DapDC are fold type III PLP-dependent enzymes that contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. It has been suggested that PvsE may be involved in the biosynthesis of the polycarboxylate siderophore vibrioferrin. It may catalyze the decarboxylation of serine to yield ethanolamine. PvsE may require homodimer formation and the presence of the PLP cofactor for activity.
Pssm-ID: 143510 [Multi-domain] Cd Length: 377 Bit Score: 38.03 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 3 PLVATV-DLSAIRHNYALAKRCAPQR-QAFAVVKANAyghgAREVVTALHDDADGFAVACLEEAAEVRALHASARI---- 76
Cdd:cd06843 1 PLCAYVyDLAALRAHARALRASLPPGcELFYAIKANS----DPPILRALAPHVDGFEVASGGEIAHVRAAVPDAPLifgg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600123 77 ---------LLLEGCFEA----SEYALAgqlRLDLViqGAEQG---EAFLAAGLDIPlnvwlKLDSGMHRL-------GF 133
Cdd:cd06843 77 pgktdselaQALAQGVERihveSELELR---RLNAV--ARRAGrtaPVLLRVNLALP-----DLPSSTLTMggqptpfGI 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 15600123 134 DPAALRAWHARLRSHPGVR----ELNLISHFACADE 165
Cdd:cd06843 147 DEADLPDALELLRDLPNIRlrgfHFHLMSHNLDAAA 182
|
|
| |
