|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
6-368 |
3.81e-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: 3.81e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 6 HRSTQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILV 85
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 86 LGITPVQQAKIAAQADISLTVAT---LKWLEDAAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGI 162
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSleqLEALAAAARRLGKPLPVHLKVDTGMNRLGFRP-EEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 163 FTHFATADEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPSGtAIAPPYKL 239
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPaagLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSP-EVAADLGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 240 QPALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMS-GSYVSVAGELCPIVGRVCMDQIMIKVP 318
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMVDVT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2335315052 319 KF--YPLGTKVTLIGTDQkinLSAETAAEYAHTINYEILCNLSDRIPRKYVN 368
Cdd:COG0787 319 DIpdVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-367 |
1.02e-163 |
|
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: 462.35 E-value: 1.02e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 8 STQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVLG 87
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 88 ITPVQQAKIAAQADISLTV---ATLKWLEDAAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGIFT 164
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVsslEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRP-EEAEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 165 HFATADEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPSGtAIAPPYKLQP 241
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAELEeagIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSP-EVKSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 242 ALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSG-SYVSVAGELCPIVGRVCMDQIMIKVPKF 320
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNkGEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2335315052 321 YP--LGTKVTLIGTDQKINLSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:cd00430 319 PDvkVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
6-367 |
1.69e-157 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 446.55 E-value: 1.69e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 6 HRSTQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILV 85
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 86 L-GITPVQQAKIAAQADISLTVATLKWLED-AAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGIF 163
Cdd:PRK00053 81 LgGFFPAEDLPLIIAYNLTTAVHSLEQLEAlEKAELGKPLKVHLKIDTGMHRLGVRP-EEAEAALERLLACPNVRLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 164 THFATADEVDTQYFRFQVENFQHLTADLP-VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPSGTAIAPPYKLQPA 242
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPgKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 243 LSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSGSY-VSVAGELCPIVGRVCMDQIMIKVPK-- 319
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTpVLVNGRRVPIVGRVSMDQLTVDLGPdp 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2335315052 320 FYPLGTKVTLIGTDqkinLSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:PRK00053 320 QDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-367 |
1.90e-123 |
|
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: 360.13 E-value: 1.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 7 RSTQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 87 GITPVQQAKIAAQADISLTVATLKWL---EDAAAVLEQPLKVHLALDTGMGRIGlTKRAEVLQACDFIQQHSQLLP-EGI 162
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLqalEEALLKEPKRLKVHLKIDTGMNRLG-VKPDEAALFVQKLRQLKKFLElEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 163 FTHFATADEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPS-GTAIAPPYK 238
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKqqnIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSaDMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 239 LQPALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMS-GSYVSVAGELCPIVGRVCMDQIMIKV 317
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSnGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2335315052 318 PKFYPLGTKVTLIGTDQKInlSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEI--SIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-228 |
3.60e-88 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 264.86 E-value: 3.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 13 VDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVLGITPVQ 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 93 QAKIAAQADISLTVATLKWLE---DAAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGIFTHFATA 169
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEalaAAARRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2335315052 170 DEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHlDCQYNMIRLGIALYGLNP 228
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEaagLRPPVVHLANSAAILLH-PLHFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
242-366 |
2.68e-57 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 182.27 E-value: 2.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 242 ALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSGSYVSVAGELCPIVGRVCMDQIMIKVPKF- 320
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIp 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2335315052 321 -YPLGTKVTLIGTDQkinLSAETAAEYAHTINYEILCNLSDRIPRKY 366
Cdd:smart01005 81 dVKVGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
6-368 |
3.81e-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: 3.81e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 6 HRSTQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILV 85
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 86 LGITPVQQAKIAAQADISLTVAT---LKWLEDAAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGI 162
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSleqLEALAAAARRLGKPLPVHLKVDTGMNRLGFRP-EEAPALAARLAALPGLEVEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 163 FTHFATADEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPSGtAIAPPYKL 239
Cdd:COG0787 160 MSHFACADEPDHPFTAEQLERFEEAVAALPaagLDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSP-EVAADLGL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 240 QPALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMS-GSYVSVAGELCPIVGRVCMDQIMIKVP 318
Cdd:COG0787 239 KPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSnGGPVLINGKRAPIVGRVSMDQIMVDVT 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2335315052 319 KF--YPLGTKVTLIGTDQkinLSAETAAEYAHTINYEILCNLSDRIPRKYVN 368
Cdd:COG0787 319 DIpdVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-367 |
1.02e-163 |
|
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: 462.35 E-value: 1.02e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 8 STQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVLG 87
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 88 ITPVQQAKIAAQADISLTV---ATLKWLEDAAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGIFT 164
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVsslEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRP-EEAEELLEALKALPGLELEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 165 HFATADEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPSGtAIAPPYKLQP 241
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAELEeagIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSP-EVKSPLGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 242 ALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSG-SYVSVAGELCPIVGRVCMDQIMIKVPKF 320
Cdd:cd00430 239 VMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNkGEVLIRGKRAPIVGRVCMDQTMVDVTDI 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2335315052 321 YP--LGTKVTLIGTDQKINLSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:cd00430 319 PDvkVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
6-367 |
1.69e-157 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 446.55 E-value: 1.69e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 6 HRSTQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILV 85
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 86 L-GITPVQQAKIAAQADISLTVATLKWLED-AAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGIF 163
Cdd:PRK00053 81 LgGFFPAEDLPLIIAYNLTTAVHSLEQLEAlEKAELGKPLKVHLKIDTGMHRLGVRP-EEAEAALERLLACPNVRLEGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 164 THFATADEVDTQYFRFQVENFQHLTADLP-VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPSGTAIAPPYKLQPA 242
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPgKGKPLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGLKPA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 243 LSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSGSY-VSVAGELCPIVGRVCMDQIMIKVPK-- 319
Cdd:PRK00053 240 MTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTpVLVNGRRVPIVGRVSMDQLTVDLGPdp 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2335315052 320 FYPLGTKVTLIGTDqkinLSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:PRK00053 320 QDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-367 |
1.90e-123 |
|
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: 360.13 E-value: 1.90e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 7 RSTQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 87 GITPVQQAKIAAQADISLTVATLKWL---EDAAAVLEQPLKVHLALDTGMGRIGlTKRAEVLQACDFIQQHSQLLP-EGI 162
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLqalEEALLKEPKRLKVHLKIDTGMNRLG-VKPDEAALFVQKLRQLKKFLElEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 163 FTHFATADEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHLDCQYNMIRLGIALYGLNPS-GTAIAPPYK 238
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKqqnIEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSaDMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 239 LQPALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMS-GSYVSVAGELCPIVGRVCMDQIMIKV 317
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSnGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2335315052 318 PKFYPLGTKVTLIGTDQKInlSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEI--SIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
9-367 |
6.02e-110 |
|
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: 325.22 E-value: 6.02e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 9 TQIIVDRQALRNNFQHEKQLLnPQTNIFAVVKANAYGHGAVVVATTLSQmgVDGFCVATLDEALELRQAGLQEPILVL-G 87
Cdd:cd06827 2 ARATIDLAALRHNLRLVRELA-PNSKILAVVKANAYGHGLVRVAKALAD--ADGFAVACIEEALALREAGITKPILLLeG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 88 ITPVQQAKIAAQADISLTV---ATLKWLEdaAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGIFT 164
Cdd:cd06827 79 FFSADELPLAAEYNLWTVVhseEQLEWLE--QAALSKPLNVWLKLDSGMHRLGFSP-EEYAAAYQRLKASPNVASIVLMT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 165 HFATADEVDTQYFRFQVENFQHLTADLPvnfkYIHC-ANSATSLWHLDCQYNMIRLGIALYGLNPSGTAIAPPYKLQPAL 243
Cdd:cd06827 156 HFACADEPDSPGTAKQLAIFEQATAGLP----GPRSlANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGLKPVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 244 SLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRM-SGSYVSVAGELCPIVGRVCMDQIMIKV---PK 319
Cdd:cd06827 232 TLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHApSGTPVLVNGQRTPLVGRVSMDMLTVDLtdlPE 311
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2335315052 320 fYPLGTKVTLIGTdqkiNLSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:cd06827 312 -AKVGDPVELWGK----GLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
13-366 |
1.41e-97 |
|
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: 294.26 E-value: 1.41e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 13 VDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVLGITPVQ 92
Cdd:cd06825 6 IDLSALEHNVKEIKRLLPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYTPPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 93 QAKIAAQADISLTVATLKWLEDAAAvLEQPLKVHLALDTGMGRIGLTKR--AEVLQACDFiqqhSQLLPEGIFTHFATAD 170
Cdd:cd06825 86 RAKELKKYSLTQTLISEAYAEELSK-YAVNIKVHLKVDTGMHRLGESPEdiDSILAIYRL----KNLKVSGIFSHLCVSD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 171 EVDTQYFRF---QVENFQHLTADL-PVNFKY--IHCANSATSLWHLDCQYNMIRLGIALYGLnPSGTAIAPPYK--LQPA 242
Cdd:cd06825 161 SLDEDDIAFtkhQIACFDQVLADLkARGIEVgkIHIQSSYGILNYPDLKYDYVRPGILLYGV-LSDPNDPTKLGldLRPV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 243 LSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMS--GSYVSVAGELCPIVGRVCMDQIMIKVPKF 320
Cdd:cd06825 240 LSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLSnqKAYVLINGKRAPIIGNICMDQLMVDVTDI 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2335315052 321 --YPLGTKVTLIGTDQKINLSAETAAEYAHTINYEILCNLSDRIPRKY 366
Cdd:cd06825 320 peVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-228 |
3.60e-88 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 264.86 E-value: 3.60e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 13 VDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVLGITPVQ 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 93 QAKIAAQADISLTVATLKWLE---DAAAVLEQPLKVHLALDTGMGRIGLTKrAEVLQACDFIQQHSQLLPEGIFTHFATA 169
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLEalaAAARRLGKPLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGLRLEGLMTHFACA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2335315052 170 DEVDTQYFRFQVENFQHLTADLP---VNFKYIHCANSATSLWHlDCQYNMIRLGIALYGLNP 228
Cdd:pfam01168 160 DEPDDPYTNAQLARFREAAAALEaagLRPPVVHLANSAAILLH-PLHFDMVRPGIALYGLSP 220
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
8-366 |
6.18e-80 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 260.66 E-value: 6.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 8 STQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVLG 87
Cdd:PRK11930 459 ETVLEINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMN 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 88 ITPVQQAKIAaQADISLTVATLKWLEDAAAVLEQP----LKVHLALDTGMGRIGLTKRaEVLQACDFIQQHSQLLPEGIF 163
Cdd:PRK11930 539 PEPTSFDTII-DYKLEPEIYSFRLLDAFIKAAQKKgitgYPIHIKIDTGMHRLGFEPE-DIPELARRLKKQPALKVRSVF 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 164 THFATADEVDTQYF-RFQVENFQHLTADLPVNFKYI---HCANSATSLWHLDCQYNMIRLGIALYGLNPSGTAIAppyKL 239
Cdd:PRK11930 617 SHLAGSDDPDHDDFtRQQIELFDEGSEELQEALGYKpirHILNSAGIERFPDYQYDMVRLGIGLYGVSASGAGQQ---AL 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 240 QPALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMS--GSYVSVAGELCPIVGRVCMDQIMIKV 317
Cdd:PRK11930 694 RNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGngVGYVLVNGQKAPIVGNICMDMCMIDV 773
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2335315052 318 PKFY-PLGTKVTLIGTDqkinLSAETAAEYAHTINYEILCNLSDRIPRKY 366
Cdd:PRK11930 774 TDIDaKEGDEVIIFGEE----LPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
3-368 |
3.71e-70 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 225.27 E-value: 3.71e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 3 PAIHRSTQIIVDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEP 82
Cdd:PRK13340 35 QIQPRNAWLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 83 IL-VLGITPvQQAKIAAQADISLTVAT---LKWLEDAAAVLEQPLKVHLALDT-GMGRIGL---TKRA--EVLQacdfIQ 152
Cdd:PRK13340 115 LLrVRSASP-AEIEQALRYDLEELIGDdeqAKLLAAIAKKNGKPIDIHLALNSgGMSRNGLdmsTARGkwEALR----IA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 153 QHSQLLPEGIFTHFATAD--EVDTQYFRFQVENfQHL--TADLPVNFKYIHCANSATSLWHLDCQYNMIRLGIALYGlnp 228
Cdd:PRK13340 190 TLPSLGIVGIMTHFPNEDedEVRWKLAQFKEQT-AWLigEAGLKREKITLHVANSYATLNVPEAHLDMVRPGGILYG--- 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 229 SGTAIAPPYKlqPALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMS-GSYVSVAGELCPIVGR 307
Cdd:PRK13340 266 DRHPANTEYK--RIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASnKAPVLINGQRAPVVGR 343
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2335315052 308 VCMDQIMIKV---PKFYPlGTKVTLIGTDQKINLSAETAAEYAHTINYEILCNLSDRIPRKYVN 368
Cdd:PRK13340 344 VSMNTLMVDVtdiPNVKP-GDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIYVP 406
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-367 |
9.54e-67 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 214.59 E-value: 9.54e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 1 MKPAihrstQIIVDRQALRNNFQHEKQLlNPQTNIFAVVKANAYGHGAVVVATTLSqmGVDGFCVATLDEALELRQAGLQ 80
Cdd:PRK03646 1 TRPI-----QASLDLQALKQNLSIVREA-APGARVWSVVKANAYGHGIERIWSALG--ATDGFAVLNLEEAITLRERGWK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 81 EPILVL-GITPVQQAKIAAQADISLTVAT---LKWLEDAAavLEQPLKVHLALDTGMGRIGLtkraevlQACDFIQQHSQ 156
Cdd:PRK03646 73 GPILMLeGFFHAQDLELYDQHRLTTCVHSnwqLKALQNAR--LKAPLDIYLKVNSGMNRLGF-------QPERVQTVWQQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 157 LLPEG------IFTHFATADEVDTqyFRFQVENFQHLTADLPVNfkyIHCANSATSLWHLDCQYNMIRLGIALYGLNPSG 230
Cdd:PRK03646 144 LRAMGnvgemtLMSHFARADHPDG--ISEAMARIEQAAEGLECE---RSLSNSAATLWHPQAHFDWVRPGIILYGASPSG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 231 TA--IAPPyKLQPALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRM-SGSYVSVAGELCPIVGR 307
Cdd:PRK03646 219 QWrdIANT-GLRPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVGT 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2335315052 308 VCMDQIMI---KVPKfYPLGTKVTLIGTDQKINlsaETAAEyAHTINYEILCNLSDRIPRKYV 367
Cdd:PRK03646 298 VSMDMLAVdltPCPQ-AGIGTPVELWGKEIKID---DVAAA-AGTIGYELMCALALRVPVVTV 355
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
242-366 |
1.06e-58 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 186.03 E-value: 1.06e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 242 ALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSGS-YVSVAGELCPIVGRVCMDQIMIKVP-- 318
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRgEVLINGKRAPIVGRVCMDQLMVDVTdv 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2335315052 319 KFYPLGTKVTLIGTDQKINLSAETAAEYAHTINYEILCNLSDRIPRKY 366
Cdd:pfam00842 81 PEVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
242-366 |
2.68e-57 |
|
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins.
Pssm-ID: 214969 [Multi-domain] Cd Length: 124 Bit Score: 182.27 E-value: 2.68e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 242 ALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSGSYVSVAGELCPIVGRVCMDQIMIKVPKF- 320
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTDIp 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2335315052 321 -YPLGTKVTLIGTDQkinLSAETAAEYAHTINYEILCNLSDRIPRKY 366
Cdd:smart01005 81 dVKVGDEVVLFGPQE---ITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
13-367 |
2.33e-48 |
|
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: 167.13 E-value: 2.33e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 13 VDRQALRNNFQHEKQLLNPQTNIFAVVKANAYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEPILVLGITPVQ 92
Cdd:cd06826 6 ISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTATPS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 93 QAKIAAQADISLTVATLKWLEDAAAVLEQ---PLKVHLALDT-GMGRIGL-TKRAEVLQACDFIQQHSQLLPEGIFTHFA 167
Cdd:cd06826 86 EIEDALAYNIEELIGSLDQAEQIDSLAKRhgkTLPVHLALNSgGMSRNGLeLSTAQGKEDAVAIATLPNLKIVGIMTHFP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 168 TADEvdtQYFRFQVENFQHLTADLPVNFKY------IHCANSATSLWHLDCQYNMIRLGIALYGLNPSGtaiaPPYKlqP 241
Cdd:cd06826 166 VEDE---DDVRAKLARFNEDTAWLISNAKLkrekitLHAANSFATLNVPEAHLDMVRPGGILYGDTPPS----PEYK--R 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 242 ALSLQTEIVHIKQVAPGQKISYGATYTSAQSEIIATLPLGYADGWLRRMSG-SYVSVAGELCPIVGRVCMDQIMIKVPKF 320
Cdd:cd06826 237 IMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNkAHVLINGQRVPVVGKVSMNTVMVDVTDI 316
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2335315052 321 --YPLGTKVTLIGTDQKINLSAETAAEYAHTINYEILCNLSDRIPRKYV 367
Cdd:cd06826 317 pgVKAGDEVVLFGKQGGAEITAAEIEEGSGTILAELYTLWGQTNPRVYV 365
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
18-221 |
5.97e-30 |
|
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: 113.95 E-value: 5.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 18 LRNNFQHEKQLLNPQTNIFAVVKANAyghgAVVVATTLSQmGVDGFCVATLDEALELRQAGL-QEPILVLGITP-VQQAK 95
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANA----NPEVARTLAA-LGTGFDVASLGEALLLRAAGIpPEPILFLGPCKqVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 96 IAAQA-DISLTVATLKWLE---DAAAVLEQPLKVHLALDTG--MGRIGLTKrAEVLQACDFIQQHSQLLPEGIFTHFATA 169
Cdd:cd06808 76 DAAEQgVIVVTVDSLEELEkleEAALKAGPPARVLLRIDTGdeNGKFGVRP-EELKALLERAKELPHLRLVGLHTHFGSA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2335315052 170 DEvDTQYFRFQVENFQHLTADLP---VNFKYIHCANS-ATSLWHLDCQY--NMIRLGI 221
Cdd:cd06808 155 DE-DYSPFVEALSRFVAALDQLGelgIDLEQLSIGGSfAILYLQELPLGtfIIVEPGR 211
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
59-165 |
6.59e-10 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 59.76 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 59 GVDGFCVATLDEALELRQAGLQEpiLVLGITPVQQAKIA-----AQADISLTV-----ATLKWLEDAAAVLEQPLKVHLA 128
Cdd:COG3616 56 GAWGITVATLAEAEVLAAAGVDD--ILLAYPLVGPAKLArlaalARAGARLTVlvdsvEQAEALAAAAAAAGRPLRVLVE 133
|
90 100 110
....*....|....*....|....*....|....*..
gi 2335315052 129 LDTGMGRIGLTKRAEVLQACDFIQQHSQLLPEGIFTH 165
Cdd:COG3616 134 LDVGGGRTGVRPPEAALALARAIAASPGLRLAGLMTY 170
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
43-171 |
2.15e-05 |
|
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: 46.06 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 43 AYGHGAVVVATTLSQMGVDGFCVATLDEALELRQAGLQEpIL----VLGITPVQQ-AKIAAQADISLTV---ATLKWLED 114
Cdd:cd06819 39 AKTHKCPAIARRQIAAGAVGVCCQKLSEAEVMAAAGIRD-ILitneVVGPAKIARlAALARRAPLIVCVdhpDNVRALAA 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2335315052 115 AAAVLEQPLKVHLALDTGMGRIGLTKRAEVLQACDFIQQHSQLLPEGI------FTHFATADE 171
Cdd:cd06819 118 AAVEAGVRLDVLVEIDVGQGRCGVPPGEAALALARTIAALPGLRFAGLqayhghLQHIRDYEE 180
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
57-165 |
9.06e-05 |
|
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: 43.84 E-value: 9.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 57 QMGVDGFCVATLDEALELRQAGLQEpILV----LGITPVQQ-AKIAAQADISLTV---ATLKWLEDAAAVLEQPLKVHLA 128
Cdd:cd06820 49 AAGAIGITVATVGEAEVMADAGLSD-IFIaypiVGRQKLERlRALAERVTLSVGVdsaEVARGLAEVAEGAGRPLEVLVE 127
|
90 100 110
....*....|....*....|....*....|....*..
gi 2335315052 129 LDTGMGRIGLTKRAEVLQACDFIQQHSQLLPEGIFTH 165
Cdd:cd06820 128 VDSGMNRCGVQTPEDAVALARAIASAPGLRFRGIFTY 164
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
46-162 |
2.17e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine aldolase (D-TA, EC 4.3.1.18) reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Its activity is present in several genera of bacteria but not in fungi. It requires PLP and a divalent cation such as Co2+, Ni2+, Mn2+, or Mg2+ as cofactors for catalytic activity and thermal stability. Members of this subfamily show similarity to bacterial alanine racemase (AR), a fold type III PLP-dependent enzyme which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.
Pssm-ID: 143495 [Multi-domain] Cd Length: 361 Bit Score: 39.58 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 46 HGAVVVATTLSQMGVDGFCVATLDEALELRQAGLqEPILV----LGITPVQQAKIAAQ---ADISLTV---ATLKWLEDA 115
Cdd:cd06821 43 HKMAEIVRLQLEAGITKFKCATIAEAEMLAEAGA-PDVLLayplVGPNIERFLELAKKypgTRFSALVddlEAAEALSAA 121
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2335315052 116 AAVLEQPLKVHLALDTGMGRIGLTKRAEVLQACDFIQQHSQLLPEGI 162
Cdd:cd06821 122 AGSAGLTLSVLLDVNTGMNRTGIAPGEDAEELYRAIATLPGLVLAGL 168
|
|
| PLPDE_III_cryptic_DSD |
cd06818 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bacterial Cryptic D-Serine Dehydratase; ... |
12-191 |
5.72e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Bacterial Cryptic D-Serine Dehydratase; This subfamily is composed of Burkholderia cepacia cryptic D-serine dehydratase (cryptic DSD), which is also called D-serine deaminase, and similar bacterial proteins. Members of this subfamily are fold type III PLP-dependent enzymes with 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 dimers 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, it is possible cryptic DSDs may also form dimers. Cryptic DSDs are distinct from the ubiquitous bacterial DSDs coded by the dsdA gene, mammalian L-serine dehydratases (LSD) and mammalian serine racemase (SerRac), which are fold type II PLP-dependent enzymes. At present, the enzymatic and biochemical properties of cryptic DSDs are still poorly understood. Typically, DSDs catalyze the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia.
Pssm-ID: 143492 [Multi-domain] Cd Length: 382 Bit Score: 38.42 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 12 IVDRQALRNNFQHEKQLlnpqtnifavvkANAYG-----HGAVVVATTLSQM----GVDGFCVATLDEALELRQAGLQEP 82
Cdd:cd06818 7 VLDASALAHNLAWMQAF------------AAAHGvklapHGKTTMAPQLFRRqleaGAWGITVATVAQARVALAFGVRRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 83 IL---VLGITPVQQ--AKIAAQADISL-----TVATLKWLEDAAAVLEQPLKVHLALDTGMGRIGLTKRAEVLQACDFIQ 152
Cdd:cd06818 75 LLanqLVGKANLRRlaALLAADPDFEFfclvdSVDNVRALAAFFAALERPLNVLIELGVPGGRTGVRTEAEALALADAIA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 2335315052 153 QHSQLLPEGIFTHFATADEVDTQYFRFQVENFQHLTADL 191
Cdd:cd06818 155 ASPALRLAGVEGYEGVAAHDDSEETLAAVRAFLARAVDL 193
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
57-165 |
8.57e-03 |
|
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: 37.83 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2335315052 57 QMGVDGFCVATLDEALELRQAGLQEpiLVLGITPVQQAKIAAQADISLTVATLKWLED---AAAVLEQ-------PLKVH 126
Cdd:cd07376 38 AAGARGVTVATLAEAETFAEAGVKD--ILMAYPLVGPAAIARLAGLLRQEAEFHVLVDspeALAALAAfaaahgvRLRVM 115
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2335315052 127 LALDTGMGRIGLTK-RAEVLQACDFIQQHSQLLPEGIFTH 165
Cdd:cd07376 116 LEVDVGGHRSGVRPeEAAALALADAVQASPGLRLAGVMAY 155
|
|
| |
