|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
7-375 |
6.90e-162 |
|
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: 458.03 E-value: 6.90e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 7 HRHTQVTVDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILV 86
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 87 LGITEPEYAPLIAEQRISVAVGSLDWLQTAEKIltANATPDPIHVHLALDTGMGRIGFqTPADLARTVTWLRAHtAQFDF 166
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAA--ARRLGKPLPVHLKVDTGMNRLGF-RPEEAPALAARLAAL-PGLEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 167 EGIFTHFATADQSDDTYFTHQVNQWKRLIA---AVGELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGtALAAP 243
Cdd:COG0787 157 EGIMSHFACADEPDHPFTAEQLERFEEAVAalpAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSP-EVAAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 244 YELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRLQ-GFHVLVNGQYCEVIGRVCMDQLMV 322
Cdd:COG0787 236 LGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1655159621 323 RLP--AQVAVGTQVTLIGRDGdheITLQDVADYCGTIHYEIACGLAPRVPRIYQD 375
Cdd:COG0787 316 DVTdiPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
9-373 |
5.34e-156 |
|
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: 443.09 E-value: 5.34e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 9 HTQVTVDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLG 88
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 89 ITEPEYAPLIAEQRISVAVGSLDWLQTAEKIltANATPDPIHVHLALDTGMGRIGFqTPADLARTVTWLRAHtAQFDFEG 168
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAA--AARLGKTLKVHLKIDTGMGRLGF-RPEEAEELLEALKAL-PGLELEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 169 IFTHFATADQSDDTYFTHQVNQWKRLIAAVGEL---PRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGtALAAPYE 245
Cdd:cd00430 157 VFTHFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSP-EVKSPLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 246 LAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLMVRL 324
Cdd:cd00430 236 LKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1655159621 325 P--AQVAVGTQVTLIGRDGDHEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:cd00430 316 TdiPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-373 |
1.14e-153 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 436.92 E-value: 1.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 7 HRHTQVTVDLQAIKHNVE--MEMARKDplTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPI 84
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRqiRKHAPPK--SKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 85 LVL-GITEPEYAPLIAEQRISVAVGSLDWLQTAEKIltanATPDPIHVHLALDTGMGRIGFQtPADLARTVTWLRAhTAQ 163
Cdd:PRK00053 79 LILgGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKA----ELGKPLKVHLKIDTGMHRLGVR-PEEAEAALERLLA-CPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 164 FDFEGIFTHFATADQSDDTYFTHQVNQWKRLIAAV-GELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGTALAA 242
Cdd:PRK00053 153 VRLEGIFSHFATADEPDNSYTEQQLNRFEAALAGLpGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 243 PYELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLM 321
Cdd:PRK00053 233 DFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLT 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1655159621 322 VRLP--AQVAVGTQVTLIGRDgdheITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:PRK00053 313 VDLGpdPQDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
8-373 |
6.39e-126 |
|
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: 366.68 E-value: 6.39e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 8 RHTQVTVDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVL 87
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 88 GITEPEYAPLIAEQRISVAVGSLDWLQTAEKILTanATPDPIHVHLALDTGMGRIGFQTPADLArTVTWLRAHTAQFDFE 167
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALL--KEPKRLKVHLKIDTGMNRLGVKPDEAAL-FVQKLRQLKKFLELE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 168 GIFTHFATADQSDDTYFTHQVNQWKRLIAAV---GELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPS-GTALAAP 243
Cdd:TIGR00492 158 GIFSHFATADEPKTGTTQKQIERFNSFLEGLkqqNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSaDMSDGAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 244 YELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLMV 322
Cdd:TIGR00492 238 FGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1655159621 323 RLPA--QVAVGTQVTLIGRdgdhEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:TIGR00492 318 DLGPdlQDKTGDEVILWGE----EISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
14-235 |
3.68e-80 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 244.83 E-value: 3.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 14 VDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLGITEPE 93
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 94 YAPLIAEQRISVAVGSLDWLQTAEKILTANATpdPIHVHLALDTGMGRIGFqTPADLARTVTWLRAHtAQFDFEGIFTHF 173
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGK--PLRVHLKIDTGMGRLGF-RPEEALALLARLAAL-PGLRLEGLMTHF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655159621 174 ATADQSDDTYFTHQVNQWKRLIAAV---GELPRYVHVSNSATSLWHqACNGNVVRFGVALYGLNP 235
Cdd:pfam01168 157 ACADEPDDPYTNAQLARFREAAAALeaaGLRPPVVHLANSAAILLH-PLHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
249-373 |
1.57e-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: 196.13 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 249 ALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRLQGFHVLVNGQYCEVIGRVCMDQLMVRLP--A 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTdiP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655159621 327 QVAVGTQVTLIGRDgdhEITLQDVADYCGTIHYEIACGLAPRVPRIY 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 |
6.90e-162 |
|
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: 458.03 E-value: 6.90e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 7 HRHTQVTVDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILV 86
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 87 LGITEPEYAPLIAEQRISVAVGSLDWLQTAEKIltANATPDPIHVHLALDTGMGRIGFqTPADLARTVTWLRAHtAQFDF 166
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAA--ARRLGKPLPVHLKVDTGMNRLGF-RPEEAPALAARLAAL-PGLEV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 167 EGIFTHFATADQSDDTYFTHQVNQWKRLIA---AVGELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGtALAAP 243
Cdd:COG0787 157 EGIMSHFACADEPDHPFTAEQLERFEEAVAalpAAGLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSP-EVAAD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 244 YELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRLQ-GFHVLVNGQYCEVIGRVCMDQLMV 322
Cdd:COG0787 236 LGLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1655159621 323 RLP--AQVAVGTQVTLIGRDGdheITLQDVADYCGTIHYEIACGLAPRVPRIYQD 375
Cdd:COG0787 316 DVTdiPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
9-373 |
5.34e-156 |
|
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: 443.09 E-value: 5.34e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 9 HTQVTVDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLG 88
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 89 ITEPEYAPLIAEQRISVAVGSLDWLQTAEKIltANATPDPIHVHLALDTGMGRIGFqTPADLARTVTWLRAHtAQFDFEG 168
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAA--AARLGKTLKVHLKIDTGMGRLGF-RPEEAEELLEALKAL-PGLELEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 169 IFTHFATADQSDDTYFTHQVNQWKRLIAAVGEL---PRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGtALAAPYE 245
Cdd:cd00430 157 VFTHFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSP-EVKSPLG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 246 LAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLMVRL 324
Cdd:cd00430 236 LKPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDV 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1655159621 325 P--AQVAVGTQVTLIGRDGDHEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:cd00430 316 TdiPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
7-373 |
1.14e-153 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 436.92 E-value: 1.14e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 7 HRHTQVTVDLQAIKHNVE--MEMARKDplTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPI 84
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRqiRKHAPPK--SKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 85 LVL-GITEPEYAPLIAEQRISVAVGSLDWLQTAEKIltanATPDPIHVHLALDTGMGRIGFQtPADLARTVTWLRAhTAQ 163
Cdd:PRK00053 79 LILgGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKA----ELGKPLKVHLKIDTGMHRLGVR-PEEAEAALERLLA-CPN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 164 FDFEGIFTHFATADQSDDTYFTHQVNQWKRLIAAV-GELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGTALAA 242
Cdd:PRK00053 153 VRLEGIFSHFATADEPDNSYTEQQLNRFEAALAGLpGKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 243 PYELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLM 321
Cdd:PRK00053 233 DFGLKPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLT 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1655159621 322 VRLP--AQVAVGTQVTLIGRDgdheITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:PRK00053 313 VDLGpdPQDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
8-373 |
6.39e-126 |
|
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: 366.68 E-value: 6.39e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 8 RHTQVTVDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVL 87
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 88 GITEPEYAPLIAEQRISVAVGSLDWLQTAEKILTanATPDPIHVHLALDTGMGRIGFQTPADLArTVTWLRAHTAQFDFE 167
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALL--KEPKRLKVHLKIDTGMNRLGVKPDEAAL-FVQKLRQLKKFLELE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 168 GIFTHFATADQSDDTYFTHQVNQWKRLIAAV---GELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPS-GTALAAP 243
Cdd:TIGR00492 158 GIFSHFATADEPKTGTTQKQIERFNSFLEGLkqqNIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSaDMSDGAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 244 YELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLMV 322
Cdd:TIGR00492 238 FGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1655159621 323 RLPA--QVAVGTQVTLIGRdgdhEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:TIGR00492 318 DLGPdlQDKTGDEVILWGE----EISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
10-374 |
6.42e-109 |
|
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: 322.91 E-value: 6.42e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 10 TQVTVDLQAIKHNVEM--EMArkdPLTELWAVVKANGYGHGILQVAQAAKQAgaTGFCVAILDEALALRAAGFTEPILVL 87
Cdd:cd06827 2 ARATIDLAALRHNLRLvrELA---PNSKILAVVKANAYGHGLVRVAKALADA--DGFAVACIEEALALREAGITKPILLL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 88 -GITEPEYAPLIAEQRISVAVGS---LDWLQTAekiltanATPDPIHVHLALDTGMGRIGFQtPADLARTVTWLRAHTAQ 163
Cdd:cd06827 77 eGFFSADELPLAAEYNLWTVVHSeeqLEWLEQA-------ALSKPLNVWLKLDSGMHRLGFS-PEEYAAAYQRLKASPNV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 164 FDFeGIFTHFATADQSDDTYFTHQVNQWKRLIAAvGELPRyvHVSNSATSLWHQACNGNVVRFGVALYGLNPSGTALAAP 243
Cdd:cd06827 149 ASI-VLMTHFACADEPDSPGTAKQLAIFEQATAG-LPGPR--SLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 244 YELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRLQ-GFHVLVNGQYCEVIGRVCMDQLMV 322
Cdd:cd06827 225 LGLKPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPsGTPVLVNGQRTPLVGRVSMDMLTV 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1655159621 323 RLPA--QVAVGTQVTLIGrdgdHEITLQDVADYCGTIHYEIACGLAPRVPRIYQ 374
Cdd:cd06827 305 DLTDlpEAKVGDPVELWG----KGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
14-373 |
3.80e-90 |
|
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: 275.39 E-value: 3.80e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 14 VDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLGITEPE 93
Cdd:cd06825 6 IDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYTPPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 94 YAPLIAEQRISVAVGSLDWlqtAEKIltaNATPDPIHVHLALDTGMGRIGFqtPADLARTVTWLRAhTAQFDFEGIFTHF 173
Cdd:cd06825 86 RAKELKKYSLTQTLISEAY---AEEL---SKYAVNIKVHLKVDTGMHRLGE--SPEDIDSILAIYR-LKNLKVSGIFSHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 174 ATADQ--SDDTYFT-HQVNQWKRLIAAV---GELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLnPSGTALAAP--YE 245
Cdd:cd06825 157 CVSDSldEDDIAFTkHQIACFDQVLADLkarGIEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGV-LSDPNDPTKlgLD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 246 LAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL--QGFHVLVNGQYCEVIGRVCMDQLMVR 323
Cdd:cd06825 236 LRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLsnQKAYVLINGKRAPIIGNICMDQLMVD 315
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1655159621 324 LPA--QVAVGTQVTLIGRDGDHEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:cd06825 316 VTDipEVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
14-235 |
3.68e-80 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 244.83 E-value: 3.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 14 VDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLGITEPE 93
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 94 YAPLIAEQRISVAVGSLDWLQTAEKILTANATpdPIHVHLALDTGMGRIGFqTPADLARTVTWLRAHtAQFDFEGIFTHF 173
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGK--PLRVHLKIDTGMGRLGF-RPEEALALLARLAAL-PGLRLEGLMTHF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1655159621 174 ATADQSDDTYFTHQVNQWKRLIAAV---GELPRYVHVSNSATSLWHqACNGNVVRFGVALYGLNP 235
Cdd:pfam01168 157 ACADEPDDPYTNAQLARFREAAAALeaaGLRPPVVHLANSAAILLH-PLHFDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
10-373 |
6.35e-73 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 242.17 E-value: 6.35e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 10 TQVTVDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLGI 89
Cdd:PRK11930 460 TVLEINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNP 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 90 TEPEYAPLIaEQRISVAVGSLDWLQTAEKILTANATPD-PIHVHLalDTGMGRIGFQtPADLARTVTWLRAHTAqFDFEG 168
Cdd:PRK11930 540 EPTSFDTII-DYKLEPEIYSFRLLDAFIKAAQKKGITGyPIHIKI--DTGMHRLGFE-PEDIPELARRLKKQPA-LKVRS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 169 IFTHFATADQSD-DTYFTHQVNQWKRLIAAVGELPRYV---HVSNSATSLWHQACNGNVVRFGVALYGLNPSGTALAApy 244
Cdd:PRK11930 615 VFSHLAGSDDPDhDDFTRQQIELFDEGSEELQEALGYKpirHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQA-- 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 245 eLAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL--QGFHVLVNGQYCEVIGRVCMDQLMV 322
Cdd:PRK11930 693 -LRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLgnGVGYVLVNGQKAPIVGNICMDMCMI 771
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1655159621 323 RLP-AQVAVGTQVTLIGrdgdHEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:PRK11930 772 DVTdIDAKEGDEVIIFG----EELPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
8-373 |
1.17e-72 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 230.39 E-value: 1.17e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 8 RHTQVTVDLQAIKHNveMEMARK-DPLTELWAVVKANGYGHGILQVAQAAkqAGATGFCVAILDEALALRAAGFTEPILV 86
Cdd:PRK03646 2 RPIQASLDLQALKQN--LSIVREaAPGARVWSVVKANAYGHGIERIWSAL--GATDGFAVLNLEEAITLRERGWKGPILM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 87 L-GITEPEYAPLIAEQRISVAVGSLDWLQTAEKI-LTAnatpdPIHVHLALDTGMGRIGFQtPADLARTVTWLRAhTAQF 164
Cdd:PRK03646 78 LeGFFHAQDLELYDQHRLTTCVHSNWQLKALQNArLKA-----PLDIYLKVNSGMNRLGFQ-PERVQTVWQQLRA-MGNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 165 DFEGIFTHFATADQSDDTyfthqVNQWKRLIAAVGELPRYVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGTALA-AP 243
Cdd:PRK03646 151 GEMTLMSHFARADHPDGI-----SEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDiAN 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 244 YELAPALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLMV 322
Cdd:PRK03646 226 TGLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVGTVSMDMLAV 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1655159621 323 RLP--AQVAVGTQVTLIGRdgdhEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:PRK03646 306 DLTpcPQAGIGTPVELWGK----EIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
14-375 |
6.83e-71 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 227.20 E-value: 6.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 14 VDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPIL-VLGITEP 92
Cdd:PRK13340 45 ISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLrVRSASPA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 93 EYAplIAEQ-RISVAVGSLDWLQTAEKILTANATpdPIHVHLALDT-GMGRIGFQTPADLARTVTWLRAHTAQFDFEGIF 170
Cdd:PRK13340 125 EIE--QALRyDLEELIGDDEQAKLLAAIAKKNGK--PIDIHLALNSgGMSRNGLDMSTARGKWEALRIATLPSLGIVGIM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 171 THFATADQSDDTYFTHQVNQWKRLIAAVGELPR---YVHVSNSATSLWHQACNGNVVRFGVALYglnpsGTALAAPYELA 247
Cdd:PRK13340 201 THFPNEDEDEVRWKLAQFKEQTAWLIGEAGLKRekiTLHVANSYATLNVPEAHLDMVRPGGILY-----GDRHPANTEYK 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 248 PALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRLQ-GFHVLVNGQYCEVIGRVCMDQLMVRLP- 325
Cdd:PRK13340 276 RIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASnKAPVLINGQRAPVVGRVSMNTLMVDVTd 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1655159621 326 -AQVAVGTQVTLIGRDGDHEITLQDVADYCGTIHYEIACGLAPRVPRIYQD 375
Cdd:PRK13340 356 iPNVKPGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIYVP 406
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
249-373 |
4.74e-65 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 202.60 E-value: 4.74e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 249 ALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRLQG-FHVLVNGQYCEVIGRVCMDQLMVRLP-- 325
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNrGEVLINGKRAPIVGRVCMDQLMVDVTdv 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1655159621 326 AQVAVGTQVTLIGRDGDHEITLQDVADYCGTIHYEIACGLAPRVPRIY 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 |
1.57e-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: 196.13 E-value: 1.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 249 ALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRLQGFHVLVNGQYCEVIGRVCMDQLMVRLP--A 326
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTdiP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1655159621 327 QVAVGTQVTLIGRDgdhEITLQDVADYCGTIHYEIACGLAPRVPRIY 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 ... |
14-373 |
8.18e-50 |
|
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: 171.37 E-value: 8.18e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 14 VDLQAIKHNVEMEMARKDPLTELWAVVKANGYGHGILQVAQAAKQAGATgfCVAIL--DEALALRAAGFTEPILVLGITE 91
Cdd:cd06826 6 ISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIP--CVGITsnEEARVVREAGFTGKILRVRTAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 92 PEYAPLIAEQRISVAVGSLDWLQTAEKILTANATPdpIHVHLALDT-GMGRIGFQTPADLARTVTWLRAHTAQFDFEGIF 170
Cdd:cd06826 84 PSEIEDALAYNIEELIGSLDQAEQIDSLAKRHGKT--LPVHLALNSgGMSRNGLELSTAQGKEDAVAIATLPNLKIVGIM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 171 THFATADQSDDTYFTHQVNQWKRLIAAVGELPR---YVHVSNSATSLWHQACNGNVVRFGVALYGLNPSGTalaaPYEla 247
Cdd:cd06826 162 THFPVEDEDDVRAKLARFNEDTAWLISNAKLKRekiTLHAANSFATLNVPEAHLDMVRPGGILYGDTPPSP----EYK-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 248 PALSLTAQLSFVKRLAKGQSVSYGATYTADRAEWVGTVPIGYADGYERRL-QGFHVLVNGQYCEVIGRVCMDQLMVRLP- 325
Cdd:cd06826 236 RIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFsNKAHVLINGQRVPVVGKVSMNTVMVDVTd 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1655159621 326 -AQVAVGTQVTLIGRDGDHEITLQDVADYCGTIHYEIACGLAPRVPRIY 373
Cdd:cd06826 316 iPGVKAGDEVVLFGKQGGAEITAAEIEEGSGTILAELYTLWGQTNPRVY 364
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
19-227 |
1.09e-29 |
|
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: 113.57 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 19 IKHNVEmEMARKDPL-TELWAVVKANGYghgiLQVAQAAkQAGATGFCVAILDEALALRAAGF-TEPILVLG-ITEPEYA 95
Cdd:cd06808 1 IRHNYR-RLREAAPAgITLFAVVKANAN----PEVARTL-AALGTGFDVASLGEALLLRAAGIpPEPILFLGpCKQVSEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 96 PLIAEQ-RISVAVGSLDWLQTAEKIltANATPDPIHVHLALDTG--MGRIGFQtPADLARTVTWLRAHtAQFDFEGIFTH 172
Cdd:cd06808 75 EDAAEQgVIVVTVDSLEELEKLEEA--ALKAGPPARVLLRIDTGdeNGKFGVR-PEELKALLERAKEL-PHLRLVGLHTH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1655159621 173 FATADqSDDTYFTHQVNQWKRLIAAVGEL---PRYVHVSNSATSLWHQACNG---NVVRFG 227
Cdd:cd06808 151 FGSAD-EDYSPFVEALSRFVAALDQLGELgidLEQLSIGGSFAILYLQELPLgtfIIVEPG 210
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
12-255 |
3.80e-12 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 66.70 E-value: 3.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 12 VTVDLQAIKHNVE--MEMARKDPLtELWAVVKAngygHGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLGI 89
Cdd:COG3616 11 LVLDLDALERNIArmAARAAAHGV-RLRPHGKT----HKSPELARRQLAAGAWGITVATLAEAEVLAAAGVDDILLAYPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 90 TEPEYAPLIAE-----QRISVAVGSLDWLQTAEKILTANATpdPIHVHLALDTGMGRIGFQTPAD---LARTVtwlrAHT 161
Cdd:COG3616 86 VGPAKLARLAAlaragARLTVLVDSVEQAEALAAAAAAAGR--PLRVLVELDVGGGRTGVRPPEAalaLARAI----AAS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 162 AQFDFEGIFTHFATADQSDDTY--------FTHQVNQWKRLIAAVGELPRYVHVSNSATSLWHQACNG-NVVRFGVALYg 232
Cdd:COG3616 160 PGLRLAGLMTYEGHIYGADDAEerraaareELARLAAAAEALRAAGLPCPIVSGGGTPTFDFVADLPGvTELRPGSYVF- 238
|
250 260
....*....|....*....|....
gi 1655159621 233 lNPSG-TALAAPYELAPALSLTAQ 255
Cdd:COG3616 239 -HDAGyYRYGVCFPFDPALSVLAT 261
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
47-172 |
5.30e-10 |
|
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: 60.41 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 47 HGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLGITEPE----YAPLIAEQRISVAVGSLDWLQTAEKilTA 122
Cdd:cd06820 38 HKSPEIARLQLAAGAIGITVATVGEAEVMADAGLSDIFIAYPIVGRQklerLRALAERVTLSVGVDSAEVARGLAE--VA 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1655159621 123 NATPDPIHVHLALDTGMGRIGFQTPADlARTVTWLRAHTAQFDFEGIFTH 172
Cdd:cd06820 116 EGAGRPLEVLVEVDSGMNRCGVQTPED-AVALARAIASAPGLRFRGIFTY 164
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
14-154 |
3.85e-08 |
|
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: 54.53 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 14 VDLQAIKHNVEMeMArkdpltelwAVVKANGYG-------HGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEpILV 86
Cdd:cd06819 12 LDLDALERNIKR-MA---------AFAKAHGVRlrphaktHKCPAIARRQIAAGAVGVCCQKLSEAEVMAAAGIRD-ILI 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1655159621 87 LG--ITEPEYAPLIA---EQRISVAVGSLDWLQTAEKILTANATpdPIHVHLALDTGMGRIGFQTPAD---LARTV 154
Cdd:cd06819 81 TNevVGPAKIARLAAlarRAPLIVCVDHPDNVRALAAAAVEAGV--RLDVLVEIDVGQGRCGVPPGEAalaLARTI 154
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
47-172 |
2.24e-04 |
|
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: 42.84 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1655159621 47 HGILQVAQAAKQAGATGFCVAILDEALALRAAGFTEPILVLGITEPE-----YAPLIAEQRISVAVGSLDWLQTAEKIlt 121
Cdd:cd07376 27 HKSPELAQRQLAAGARGVTVATLAEAETFAEAGVKDILMAYPLVGPAaiarlAGLLRQEAEFHVLVDSPEALAALAAF-- 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1655159621 122 ANATPDPIHVHLALDTGMGRIGFQTPAdlARTVTWLRAHTAQ--FDFEGIFTH 172
Cdd:cd07376 105 AAAHGVRLRVMLEVDVGGHRSGVRPEE--AAALALADAVQASpgLRLAGVMAY 155
|
|
| |
