|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-375 |
1.82e-151 |
|
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: 431.45 E-value: 1.82e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVL 86
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 87 GITRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGIDSGMGRIGFTqVVDFLAAVAFIKQNPeYFIFE 166
Cdd:COG0787 82 GGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLG--KPLPVHLKVDTGMNRLGFR-PEEAPALAARLAALP-GLEVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 167 GIFTHFATADEQDTTYFQQQVKKFNAYVAQLDQ---RPRYVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISELp 243
Cdd:COG0787 158 GIMSHFACADEPDHPFTAEQLERFEEAVAALPAaglDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAADL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 244 yPLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRLQ-GFHVLVDGHPCEIVGRICMDQFMI 322
Cdd:COG0787 237 -GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2159754603 323 RLP--KPYDVGTKVTLIGEDqgaEITLQEVAAYSDTIHYELACILTNRLPRKYIN 375
Cdd:COG0787 316 DVTdiPDVKVGDEVVLFGEQ---GITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-374 |
1.50e-145 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 416.50 E-value: 1.50e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVL 86
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 87 -GITRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQshiePLAVHLGIDSGMGRIGFtQVVDFLAAVAFIKQNPEyFIF 165
Cdd:PRK00053 82 gGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGK----PLKVHLKIDTGMHRLGV-RPEEAEAALERLLACPN-VRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 166 EGIFTHFATADEQDTTYFQQQVKKFNAYVAQLDQRPR-YVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAiSELPY 244
Cdd:PRK00053 156 EGIFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEP-LGLDF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 245 PLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCEIVGRICMDQFMIR 323
Cdd:PRK00053 235 GLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2159754603 324 LPKP--YDVGTKVTLIGEDqgaeITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:PRK00053 315 LGPDpqDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
9-374 |
3.04e-145 |
|
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: 415.74 E-value: 3.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 9 AQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVLGI 88
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 89 TRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGIDSGMGRIGFTqVVDFLAAVAFIKQNPEyFIFEGI 168
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLG--KTLKVHLKIDTGMGRLGFR-PEEAEELLEALKALPG-LELEGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 169 FTHFATADEQDTTYFQQQVKKFNAYVAQLDQR---PRYVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISELpyP 245
Cdd:cd00430 158 FTHFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL--G 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 246 LQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCEIVGRICMDQFMIRL 324
Cdd:cd00430 236 LKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2159754603 325 PKPYDV--GTKVTLIGEDQGAEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:cd00430 316 TDIPDVkvGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-374 |
7.18e-122 |
|
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: 356.66 E-value: 7.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 87 GITRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGIDSGMGRIGFT--QVVDFlaaVAFIKQNPEYFI 164
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEP--KRLKVHLKIDTGMNRLGVKpdEAALF---VQKLRQLKKFLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 165 FEGIFTHFATADEQDTTYFQQQVKKFNAYVAQLDQR---PRYVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISE 241
Cdd:TIGR00492 156 LEGIFSHFATADEPKTGTTQKQIERFNSFLEGLKQQniePPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 242 LPYPLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCEIVGRICMDQF 320
Cdd:TIGR00492 236 APFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMI 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754603 321 MIRLPKPYD--VGTKVTLIGEdqgaEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:TIGR00492 316 MVDLGPDLQdkTGDEVILWGE----EISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-234 |
4.15e-77 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 237.12 E-value: 4.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 13 IDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVLGITRPE 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 93 LAEIAASQHISLTVGSKDWLVAAKNAmtKQSHIEPLAVHLGIDSGMGRIGFTqVVDFLAAVAFIKQNPEyFIFEGIFTHF 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAA--ARRLGKPLRVHLKIDTGMGRLGFR-PEEALALLARLAALPG-LRLEGLMTHF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159754603 173 ATADEQDTTYFQQQVKKFNAYVAQLDQ---RPRYVHVSNSATSLWHDAcNGNMVRFGVAIYGLNP 234
Cdd:pfam01168 157 ACADEPDDPYTNAQLARFREAAAALEAaglRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
249-373 |
5.37e-58 |
|
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: 184.58 E-value: 5.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 249 ALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRLQGFHVLVDGHPCEIVGRICMDQFMIRLPKPY 328
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2159754603 329 DV--GTKVTLIGEDqgaEITLQEVAAYSDTIHYELACILTNRLPRKY 373
Cdd:smart01005 81 DVkvGDEVVLFGPQ---EITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-375 |
1.82e-151 |
|
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: 431.45 E-value: 1.82e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVL 86
Cdd:COG0787 2 RPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 87 GITRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGIDSGMGRIGFTqVVDFLAAVAFIKQNPeYFIFE 166
Cdd:COG0787 82 GGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLG--KPLPVHLKVDTGMNRLGFR-PEEAPALAARLAALP-GLEVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 167 GIFTHFATADEQDTTYFQQQVKKFNAYVAQLDQ---RPRYVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISELp 243
Cdd:COG0787 158 GIMSHFACADEPDHPFTAEQLERFEEAVAALPAaglDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAADL- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 244 yPLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRLQ-GFHVLVDGHPCEIVGRICMDQFMI 322
Cdd:COG0787 237 -GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2159754603 323 RLP--KPYDVGTKVTLIGEDqgaEITLQEVAAYSDTIHYELACILTNRLPRKYIN 375
Cdd:COG0787 316 DVTdiPDVKVGDEVVLFGEQ---GITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-374 |
1.50e-145 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 416.50 E-value: 1.50e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVL 86
Cdd:PRK00053 2 RPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 87 -GITRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQshiePLAVHLGIDSGMGRIGFtQVVDFLAAVAFIKQNPEyFIF 165
Cdd:PRK00053 82 gGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGK----PLKVHLKIDTGMHRLGV-RPEEAEAALERLLACPN-VRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 166 EGIFTHFATADEQDTTYFQQQVKKFNAYVAQLDQRPR-YVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAiSELPY 244
Cdd:PRK00053 156 EGIFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEP-LGLDF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 245 PLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCEIVGRICMDQFMIR 323
Cdd:PRK00053 235 GLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVD 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2159754603 324 LPKP--YDVGTKVTLIGEDqgaeITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:PRK00053 315 LGPDpqDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
9-374 |
3.04e-145 |
|
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: 415.74 E-value: 3.04e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 9 AQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVLGI 88
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 89 TRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGIDSGMGRIGFTqVVDFLAAVAFIKQNPEyFIFEGI 168
Cdd:cd00430 82 TPPEEAEEAIEYDLTPTVSSLEQAEALSAAAARLG--KTLKVHLKIDTGMGRLGFR-PEEAEELLEALKALPG-LELEGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 169 FTHFATADEQDTTYFQQQVKKFNAYVAQLDQR---PRYVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISELpyP 245
Cdd:cd00430 158 FTHFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL--G 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 246 LQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCEIVGRICMDQFMIRL 324
Cdd:cd00430 236 LKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2159754603 325 PKPYDV--GTKVTLIGEDQGAEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:cd00430 316 TDIPDVkvGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-374 |
7.18e-122 |
|
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: 356.66 E-value: 7.18e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 87 GITRPELAEIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGIDSGMGRIGFT--QVVDFlaaVAFIKQNPEYFI 164
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEP--KRLKVHLKIDTGMNRLGVKpdEAALF---VQKLRQLKKFLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 165 FEGIFTHFATADEQDTTYFQQQVKKFNAYVAQLDQR---PRYVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISE 241
Cdd:TIGR00492 156 LEGIFSHFATADEPKTGTTQKQIERFNSFLEGLKQQniePPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 242 LPYPLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCEIVGRICMDQF 320
Cdd:TIGR00492 236 APFGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMI 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754603 321 MIRLPKPYD--VGTKVTLIGEdqgaEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:TIGR00492 316 MVDLGPDLQdkTGDEVILWGE----EISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-234 |
4.15e-77 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 237.12 E-value: 4.15e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 13 IDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVLGITRPE 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 93 LAEIAASQHISLTVGSKDWLVAAKNAmtKQSHIEPLAVHLGIDSGMGRIGFTqVVDFLAAVAFIKQNPEyFIFEGIFTHF 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAA--ARRLGKPLRVHLKIDTGMGRLGFR-PEEALALLARLAALPG-LRLEGLMTHF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2159754603 173 ATADEQDTTYFQQQVKKFNAYVAQLDQ---RPRYVHVSNSATSLWHDAcNGNMVRFGVAIYGLNP 234
Cdd:pfam01168 157 ACADEPDDPYTNAQLARFREAAAALEAaglRPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
13-374 |
8.16e-71 |
|
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: 226.08 E-value: 8.16e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 13 IDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVLGITRPE 92
Cdd:cd06825 6 IDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYTPPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 93 LAEIAASQHISLTVGSKDWLVaaknAMTKQSHiePLAVHLGIDSGMGRIGFT-QVVDFLAAVAFIKqnpeYFIFEGIFTH 171
Cdd:cd06825 86 RAKELKKYSLTQTLISEAYAE----ELSKYAV--NIKVHLKVDTGMHRLGESpEDIDSILAIYRLK----NLKVSGIFSH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 172 FATAD---EQDTTYFQQQVKKFNAYVAQLDQR---PRYVHVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISELPYP 245
Cdd:cd06825 156 LCVSDsldEDDIAFTKHQIACFDQVLADLKARgieVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVLSDPNDPTKLGLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 246 LQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL--QGFHVLVDGHPCEIVGRICMDQFMIR 323
Cdd:cd06825 236 LRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLsnQKAYVLINGKRAPIIGNICMDQLMVD 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2159754603 324 LPKPYDV--GTKVTLIGEDQGAEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:cd06825 316 VTDIPEVkeGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
7-374 |
1.64e-65 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 211.90 E-value: 1.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREeVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAgaTGFCVAILDEALGLREAHFTAPILVL 86
Cdd:PRK03646 2 RPIQASLDLQALKQNLSI-VREAAPGARVWSVVKANAYGHGIERIWSALGAT--DGFAVLNLEEAITLRERGWKGPILML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 87 G--ITRPELAEIAasQHISLTVGSKDW-LVAAKNAMTKQshiePLAVHLGIDSGMGRIGFtQVVDFLAA---------VA 154
Cdd:PRK03646 79 EgfFHAQDLELYD--QHRLTTCVHSNWqLKALQNARLKA----PLDIYLKVNSGMNRLGF-QPERVQTVwqqlramgnVG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 155 FIKqnpeyfifegIFTHFATADEQDTTyfQQQVKKFNAYVAQLDQRpryVHVSNSATSLWHDACNGNMVRFGVAIYGLNP 234
Cdd:PRK03646 152 EMT----------LMSHFARADHPDGI--SEAMARIEQAAEGLECE---RSLSNSAATLWHPQAHFDWVRPGIILYGASP 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 235 SGTAISELPYPLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCEIVG 313
Cdd:PRK03646 217 SGQWRDIANTGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVG 296
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2159754603 314 RICMDQFMIRL-PKPY-DVGTKVTLIGEdqgaEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:PRK03646 297 TVSMDMLAVDLtPCPQaGIGTPVELWGK----EIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
13-374 |
7.70e-61 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 209.43 E-value: 7.70e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 13 IDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVLGitrPE 92
Cdd:PRK11930 464 INLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMN---PE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 93 LAEIAA--SQHISLTVGSKDwLVAAKNAMTKQSHIEPLAVHLGIDSGMGRIGFtQVVDFLAAVAFIKQNPeYFIFEGIFT 170
Cdd:PRK11930 541 PTSFDTiiDYKLEPEIYSFR-LLDAFIKAAQKKGITGYPIHIKIDTGMHRLGF-EPEDIPELARRLKKQP-ALKVRSVFS 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 171 HFATADEQDTTYF-QQQVKKFNAYVAQLDQRPRYV---HVSNSATSLWHDACNGNMVRFGVAIYGLNPSGTAISELpypl 246
Cdd:PRK11930 618 HLAGSDDPDHDDFtRQQIELFDEGSEELQEALGYKpirHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQAL---- 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 247 QPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL--QGFHVLVDGHPCEIVGRICMDQFMIrl 324
Cdd:PRK11930 694 RNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLgnGVGYVLVNGQKAPIVGNICMDMCMI-- 771
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 2159754603 325 pkpyDV-------GTKVTLIGEdqgaEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:PRK11930 772 ----DVtdidakeGDEVIIFGE----ELPVTELADALNTIPYEILTSISPRVKRVYF 820
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
7-375 |
5.35e-60 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 199.08 E-value: 5.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 7 RNAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPIL-V 85
Cdd:PRK13340 39 RNAWLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLrV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 86 LGITRPELaEIAASQHISLTVGSKDwlvAAK--NAMTKQSHiEPLAVHLGIDS-GMGRIGF--TQVVDFLAAVAfIKQNP 160
Cdd:PRK13340 119 RSASPAEI-EQALRYDLEELIGDDE---QAKllAAIAKKNG-KPIDIHLALNSgGMSRNGLdmSTARGKWEALR-IATLP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 161 EYFIFeGIFTHFATADEQDTtyfQQQVKKFNAY------VAQLDQRPRYVHVSNSATSLWHDACNGNMVRFGVAIYGlnp 234
Cdd:PRK13340 193 SLGIV-GIMTHFPNEDEDEV---RWKLAQFKEQtawligEAGLKREKITLHVANSYATLNVPEAHLDMVRPGGILYG--- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 235 sGTAISELPYPlqPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRLQ-GFHVLVDGHPCEIVG 313
Cdd:PRK13340 266 -DRHPANTEYK--RIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASnKAPVLINGQRAPVVG 342
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2159754603 314 RICMDQFMIRLPKPYDV--GTKVTLIGEDQGAEITLQEVAAYSDTIHYELACILTNRLPRKYIN 375
Cdd:PRK13340 343 RVSMNTLMVDVTDIPNVkpGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIYVP 406
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
249-373 |
1.82e-59 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 188.34 E-value: 1.82e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 249 ALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRLQG-FHVLVDGHPCEIVGRICMDQFMIRLP-- 325
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNrGEVLINGKRAPIVGRVCMDQLMVDVTdv 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2159754603 326 KPYDVGTKVTLIGEDQGAEITLQEVAAYSDTIHYELACILTNRLPRKY 373
Cdd:pfam00842 81 PEVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
249-373 |
5.37e-58 |
|
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: 184.58 E-value: 5.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 249 ALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRLQGFHVLVDGHPCEIVGRICMDQFMIRLPKPY 328
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2159754603 329 DV--GTKVTLIGEDqgaEITLQEVAAYSDTIHYELACILTNRLPRKY 373
Cdd:smart01005 81 DVkvGDEVVLFGPQ---EITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
8-374 |
6.61e-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: 155.58 E-value: 6.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 8 NAQVVIDRQAIKYNVREEVKRLKQGTELFAVVKADGYGHG---MVPVAQAAQAAgatgfCVAIL--DEALGLREAHFTAP 82
Cdd:cd06826 1 NAWLEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGialVMPSIIAQNIP-----CVGITsnEEARVVREAGFTGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 83 ILVLGITRPELAEIAASQHISLTVGSKDwLVAAKNAMTKQSHIePLAVHLGIDS-GMGRIGftqvVDFLA------AVAF 155
Cdd:cd06826 76 ILRVRTATPSEIEDALAYNIEELIGSLD-QAEQIDSLAKRHGK-TLPVHLALNSgGMSRNG----LELSTaqgkedAVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 156 IKQNPEYFIfeGIFTHFATADEQDT----TYFQQQVKKFNAyVAQLDQRPRYVHVSNSATSLWHDACNGNMVRFGVAIYG 231
Cdd:cd06826 150 ATLPNLKIV--GIMTHFPVEDEDDVraklARFNEDTAWLIS-NAKLKREKITLHAANSFATLNVPEAHLDMVRPGGILYG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 232 LNPSGTaiselpyPLQPALSLTSEIVFCKQIHAGDSVSYGATYTAKADEYIGTVPMGYADGWLRRL-QGFHVLVDGHPCE 310
Cdd:cd06826 227 DTPPSP-------EYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFsNKAHVLINGQRVP 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2159754603 311 IVGRICMDQFMIRLPKPYDV--GTKVTLIGEDQGAEITLQEVAAYSDTIHYELACILTNRLPRKYI 374
Cdd:cd06826 300 VVGKVSMNTVMVDVTDIPGVkaGDEVVLFGKQGGAEITAAEIEEGSGTILAELYTLWGQTNPRVYV 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
18-226 |
3.27e-25 |
|
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: 101.63 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 18 IKYNVREEVKRLKQGTELFAVVKADGYghgmvPVAQAAQAAGATGFCVAILDEALGLREAHF-TAPILVLG--ITRPELA 94
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANAN-----PEVARTLAALGTGFDVASLGEALLLRAAGIpPEPILFLGpcKQVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 95 EIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGIDSG--MGRIGFtQVVDFLAAVAFIKQNPeYFIFEGIFTHF 172
Cdd:cd06808 76 DAAEQGVIVVTVDSLEELEKLEEAALKAG--PPARVLLRIDTGdeNGKFGV-RPEELKALLERAKELP-HLRLVGLHTHF 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 173 ATADEqDTTYFQQQVKKFNAYVAQLDQ---RPRYVHVSNSATSLWHDACNG---NMVRFG 226
Cdd:cd06808 152 GSADE-DYSPFVEALSRFVAALDQLGElgiDLEQLSIGGSFAILYLQELPLgtfIIVEPG 210
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
17-256 |
2.88e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar 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 similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 45.53 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 17 AIKYNVREEVKRLKQ-GTELFAVVKAdgygHGMVPVAQAAQAAGATGFCVAILDEALGLREAHFTAPILVLGITRP---- 91
Cdd:cd07376 1 ALEANISRMAARARAsGVRLRPHVKT----HKSPELAQRQLAAGARGVTVATLAEAETFAEAGVKDILMAYPLVGPaaia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 92 ELAEIAAS-QHISLTVGSKDWLVAAKNAmtKQSHIEPLAVHLGIDSGMGRIGFTQVVDFLAAVAFIKQNPEYFIFEGIFT 170
Cdd:cd07376 77 RLAGLLRQeAEFHVLVDSPEALAALAAF--AAAHGVRLRVMLEVDVGGHRSGVRPEEAAALALADAVQASPGLRLAGVMA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 171 H--------FATADEQDTTyfqQQVKKFNAYVAQLDQ---RPrYVHVSNSATSLWHDACNG-NMVRFGVAIYglNPSGTA 238
Cdd:cd07376 155 YeghiygagGAREGAQARD---QAVAAVRAAAAAAERglaCP-TVSGGGTPTYQLTAGDRAvTELRAGSYVF--MDTGFD 228
|
250
....*....|....*...
gi 2159754603 239 ISELPYPLQPALSLTSEI 256
Cdd:cd07376 229 TLGACAQRPAAFRVTTVI 246
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
62-160 |
2.87e-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: 39.51 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 62 GFCVAILDEAL-----GLREAHFTAPIL-VLGITRpeLAEIAASQHISLTVGSKDWLVAAKNAMTKQShiEPLAVHLGID 135
Cdd:cd06819 58 GVCCQKLSEAEvmaaaGIRDILITNEVVgPAKIAR--LAALARRAPLIVCVDHPDNVRALAAAAVEAG--VRLDVLVEID 133
|
90 100
....*....|....*....|....*
gi 2159754603 136 SGMGRIGFTQVVDFLAAVAFIKQNP 160
Cdd:cd06819 134 VGQGRCGVPPGEAALALARTIAALP 158
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
61-171 |
5.07e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine Aldolase-like; This subfamily is composed of uncharacterized bacterial proteins with similarity to low specificity D-threonine aldolase (D-TA), which is a fold type III PLP-dependent enzyme that catalyzes the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Low specificity D-TAs 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: 143494 [Multi-domain] Cd Length: 353 Bit Score: 38.45 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2159754603 61 TGFCVAILDEA-----LGLREAHFTAPILvlgiTRPELAEIAA-SQHISLTVGSKDWLVAAKNAMTKQSHIEPLAVHLGI 134
Cdd:cd06820 53 IGITVATVGEAevmadAGLSDIFIAYPIV----GRQKLERLRAlAERVTLSVGVDSAEVARGLAEVAEGAGRPLEVLVEV 128
|
90 100 110
....*....|....*....|....*....|....*..
gi 2159754603 135 DSGMGRIGFTQVVDFLAAVAFIKQNPEyFIFEGIFTH 171
Cdd:cd06820 129 DSGMNRCGVQTPEDAVALARAIASAPG-LRFRGIFTY 164
|
|
| |
