|
Name |
Accession |
Description |
Interval |
E-value |
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
6-370 |
7.64e-171 |
|
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: 480.76 E-value: 7.64e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 6 HRPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILI 85
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 86 LSVVDLAYVPLLIQYDLSVTVATQEWLEaALQQLTPESNTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLWEG 165
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLE-ALAAAARRLGKPLPVHLKVDTGMNRLGF-RPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 166 IFTHFSTADEIDTSYFEKQAGRFKAVLAVLEEL---PRYVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPsYA 242
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAgldPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAAD-LG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 243 LKPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFT-VLVNGKRCEIVGRVCMDQCMIRL 321
Cdd:COG0787 238 LKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGpVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488284520 322 --AEEVPVGSVVTLVGKDGneeNTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:COG0787 318 tdIPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVY 365
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-370 |
4.83e-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: 460.81 E-value: 4.83e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 8 PTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILS 87
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 88 VVDLAYVPLLIQYDLSVTVATQEWLEaALQQLTPESNTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLWEGIF 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAE-ALSAAAARLGKTLKVHLKIDTGMGRLGF-RPEEAEELLEALKALPGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 168 THFSTADEIDTSYFEKQAGRFKAVLAVLEEL---PRYVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPSyALK 244
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL-GLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 245 PALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL-QGFTVLVNGKRCEIVGRVCMDQCMIRL-- 321
Cdd:cd00430 238 PVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDVtd 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488284520 322 AEEVPVGSVVTLVGKDGNEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:cd00430 318 IPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
6-370 |
3.21e-161 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 456.18 E-value: 3.21e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 6 HRPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILI 85
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 86 LSVVDLA-YVPLLIQYDLSVTVATQEWLEAALQQltpESNTPLRVHLKVDTGMGRIGFLtPEETKQAVRFVQSHKEFLWE 164
Cdd:PRK00053 81 LGGFFPAeDLPLIIAYNLTTAVHSLEQLEALEKA---ELGKPLKVHLKIDTGMHRLGVR-PEEAEAALERLLACPNVRLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 165 GIFTHFSTADEIDTSYFEKQAGRFKAVLAVLEELPR-YVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPSYAL 243
Cdd:PRK00053 157 GIFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 244 KPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL-QGFTVLVNGKRCEIVGRVCMDQCMIRL- 321
Cdd:PRK00053 237 KPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVDLg 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 488284520 322 -AEEVPVGSVVTLVGKDGNEENtlqmVAEKLETIHYEVACTFSQRIPREY 370
Cdd:PRK00053 317 pDPQDKVGDEVTLWGEALTAED----VAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-370 |
6.31e-131 |
|
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: 379.39 E-value: 6.31e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 7 RPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILIL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 87 SVVDLAYVPLLIQYDLSVTVATQEWLEAALQQLTPESNTpLRVHLKVDTGMGRIGFLTPEETKQAVRFVQSHKEFLWEGI 166
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKR-LKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 167 FTHFSTADEIDTSYFEKQAGRFKAVLAVLEE---LPRYVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGN-KLAPSYA 242
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQqniEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADmSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 243 LKPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL-QGFTVLVNGKRCEIVGRVCMDQCMIRL 321
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488284520 322 AEEVP--VGSVVTLVGkdgnEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:TIGR00492 320 GPDLQdkTGDEVILWG----EEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-232 |
8.41e-88 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 264.09 E-value: 8.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 13 IDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSVVDLA 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 93 YVPLLIQYDLSVTVATQEWLEaALQQLTPESNTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLWEGIFTHFST 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLE-ALAAAARRLGKPLRVHLKIDTGMGRLGF-RPEEALALLARLAALPGLRLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284520 173 ADEIDTSYFEKQAGRFKAVLAVLEEL---PRYVHVSNSATALWHPDvPGNMIRYGVAMYGLNP 232
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAglrPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
246-370 |
1.47e-59 |
|
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: 188.43 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 246 ALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFTVLVNGKRCEIVGRVCMDQCMIRL--AE 323
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVtdIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488284520 324 EVPVGSVVTLVGKDgneENTLQMVAEKLETIHYEVACTFSQRIPREY 370
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 ... |
6-370 |
7.64e-171 |
|
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: 480.76 E-value: 7.64e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 6 HRPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILI 85
Cdd:COG0787 1 SRPAWAEIDLDALRHNLRVLRALAGPGAKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 86 LSVVDLAYVPLLIQYDLSVTVATQEWLEaALQQLTPESNTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLWEG 165
Cdd:COG0787 81 LGGVPPEDLELAIEYDLEPVVHSLEQLE-ALAAAARRLGKPLPVHLKVDTGMNRLGF-RPEEAPALAARLAALPGLEVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 166 IFTHFSTADEIDTSYFEKQAGRFKAVLAVLEEL---PRYVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPsYA 242
Cdd:COG0787 159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAAgldPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVAAD-LG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 243 LKPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFT-VLVNGKRCEIVGRVCMDQCMIRL 321
Cdd:COG0787 238 LKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGpVLINGKRAPIVGRVSMDQIMVDV 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488284520 322 --AEEVPVGSVVTLVGKDGneeNTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:COG0787 318 tdIPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVY 365
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
8-370 |
4.83e-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: 460.81 E-value: 4.83e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 8 PTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILS 87
Cdd:cd00430 1 RTWAEIDLDALRHNLRVIRRLLGPGTKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 88 VVDLAYVPLLIQYDLSVTVATQEWLEaALQQLTPESNTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLWEGIF 167
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAE-ALSAAAARLGKTLKVHLKIDTGMGRLGF-RPEEAEELLEALKALPGLELEGVF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 168 THFSTADEIDTSYFEKQAGRFKAVLAVLEEL---PRYVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPSyALK 244
Cdd:cd00430 159 THFATADEPDKAYTRRQLERFLEALAELEEAgipPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL-GLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 245 PALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL-QGFTVLVNGKRCEIVGRVCMDQCMIRL-- 321
Cdd:cd00430 238 PVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALsNKGEVLIRGKRAPIVGRVCMDQTMVDVtd 317
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 488284520 322 AEEVPVGSVVTLVGKDGNEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:cd00430 318 IPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIY 366
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
6-370 |
3.21e-161 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 456.18 E-value: 3.21e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 6 HRPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILI 85
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 86 LSVVDLA-YVPLLIQYDLSVTVATQEWLEAALQQltpESNTPLRVHLKVDTGMGRIGFLtPEETKQAVRFVQSHKEFLWE 164
Cdd:PRK00053 81 LGGFFPAeDLPLIIAYNLTTAVHSLEQLEALEKA---ELGKPLKVHLKIDTGMHRLGVR-PEEAEAALERLLACPNVRLE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 165 GIFTHFSTADEIDTSYFEKQAGRFKAVLAVLEELPR-YVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPSYAL 243
Cdd:PRK00053 157 GIFSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPSGEPLGLDFGL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 244 KPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL-QGFTVLVNGKRCEIVGRVCMDQCMIRL- 321
Cdd:PRK00053 237 KPAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVDLg 316
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 488284520 322 -AEEVPVGSVVTLVGKDGNEENtlqmVAEKLETIHYEVACTFSQRIPREY 370
Cdd:PRK00053 317 pDPQDKVGDEVTLWGEALTAED----VAEIIGTINYELLCKLSPRVPRVY 362
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
7-370 |
6.31e-131 |
|
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: 379.39 E-value: 6.31e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 7 RPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILIL 86
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRNHIGPKSKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 87 SVVDLAYVPLLIQYDLSVTVATQEWLEAALQQLTPESNTpLRVHLKVDTGMGRIGFLTPEETKQAVRFVQSHKEFLWEGI 166
Cdd:TIGR00492 81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEALLKEPKR-LKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 167 FTHFSTADEIDTSYFEKQAGRFKAVLAVLEE---LPRYVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGN-KLAPSYA 242
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQqniEPPFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADmSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 243 LKPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL-QGFTVLVNGKRCEIVGRVCMDQCMIRL 321
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488284520 322 AEEVP--VGSVVTLVGkdgnEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:TIGR00492 320 GPDLQdkTGDEVILWG----EEISIDEIAEMLGTIAYELICTLSKRVPRKY 366
|
|
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
8-370 |
1.31e-106 |
|
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: 316.75 E-value: 1.31e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 8 PTRLHIDTQAITENVQKECQRLPEGTALfAVVKANGYGHGAVESAKAAKKggATGFCVALLDEAIELREAGVQDPILIL- 86
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKIL-AVVKANAYGHGLVRVAKALAD--ADGFAVACIEEALALREAGITKPILLLe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 87 ---SVVDLayvPLLIQYDLSVTVATQEWLEAALQQLTPesnTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLW 163
Cdd:cd06827 78 gffSADEL---PLAAEYNLWTVVHSEEQLEWLEQAALS---KPLNVWLKLDSGMHRLGF-SPEEYAAAYQRLKASPNVAS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 164 EGIFTHFSTADEIDTSYFEKQAGRFKAVLAVLEeLPRyvHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGNKLAPSYAL 243
Cdd:cd06827 151 IVLMTHFACADEPDSPGTAKQLAIFEQATAGLP-GPR--SLANSAAILAWPEAHGDWVRPGIMLYGASPFADKSGADLGL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 244 KPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFT-VLVNGKRCEIVGRVCMDQCMIRLA 322
Cdd:cd06827 228 KPVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTpVLVNGQRTPLVGRVSMDMLTVDLT 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 488284520 323 E--EVPVGSVVTLVGKdgneENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:cd06827 308 DlpEAKVGDPVELWGK----GLPVDEVAAAAGTIGYELLCRLTPRVPRVY 353
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
11-370 |
2.29e-94 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This subfamily is composed of Enterococcus gallinarum VanT and similar proteins. VanT is a membrane-bound serine racemase (EC 5.1.1.18) that is essential for vancomycin resistance in Enterococcus gallinarum. It converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. The C-terminal region of this protein contains a PLP-binding TIM-barrel domain followed by beta-sandwich domain, which is homologous to the fold type III PLP-dependent enzyme, bacterial alanine racemase (AR). AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. On the basis of this similarity, it has been suggested that dimer formation of VanT is required for its catalytic activity, and that it catalyzes the racemization of serine in a mechanistically similar manner to that of alanine by bacterial AR. Some biochemical evidence indicates that VanT also exhibits alanine racemase activity and plays a role in the racemization of L-alanine. VanT contains a unique N-terminal transmembrane domain, which may function as an L-serine transporter. VanT serine racemases are not related to eukaryotic serine racemases, which are fold type II PLP-dependent enzymes.
Pssm-ID: 143498 [Multi-domain] Cd Length: 368 Bit Score: 286.17 E-value: 2.29e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 11 LHIDTQAITENVqKECQRL-PEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSVV 89
Cdd:cd06825 4 LEIDLSALEHNV-KEIKRLlPSTCKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 90 DLAYVPLLIQYDLSVTVATQEWLEAALQQltpesNTPLRVHLKVDTGMGRIGFltPEETKQAVRFVQSHKEFLWEGIFTH 169
Cdd:cd06825 83 PPVRAKELKKYSLTQTLISEAYAEELSKY-----AVNIKVHLKVDTGMHRLGE--SPEDIDSILAIYRLKNLKVSGIFSH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 170 FSTADEIDTS---YFEKQAGRFKAVLAVLEE----LPRyVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSGN---KLAP 239
Cdd:cd06825 156 LCVSDSLDEDdiaFTKHQIACFDQVLADLKArgieVGK-IHIQSSYGILNYPDLKYDYVRPGILLYGVLSDPNdptKLGL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 240 SyaLKPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL--QGFTVLVNGKRCEIVGRVCMDQC 317
Cdd:cd06825 235 D--LRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLsnQKAYVLINGKRAPIIGNICMDQL 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 488284520 318 MIRLA--EEVPVGSVVTLVGKDGNEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:cd06825 313 MVDVTdiPEVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIY 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
13-232 |
8.41e-88 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 264.09 E-value: 8.41e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 13 IDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSVVDLA 92
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAGPGAKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 93 YVPLLIQYDLSVTVATQEWLEaALQQLTPESNTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLWEGIFTHFST 172
Cdd:pfam01168 81 ELALAAEYDLTPTVDSLEQLE-ALAAAARRLGKPLRVHLKIDTGMGRLGF-RPEEALALLARLAALPGLRLEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284520 173 ADEIDTSYFEKQAGRFKAVLAVLEEL---PRYVHVSNSATALWHPDvPGNMIRYGVAMYGLNP 232
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAAglrPPVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
7-370 |
1.11e-75 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 237.71 E-value: 1.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 7 RPTRLHIDTQAITENVQKECQRLPEGTALfAVVKANGYGHGAVESAKAAkkGGATGFCVALLDEAIELREAGVQDPILIL 86
Cdd:PRK03646 2 RPIQASLDLQALKQNLSIVREAAPGARVW-SVVKANAYGHGIERIWSAL--GATDGFAVLNLEEAITLRERGWKGPILML 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 87 S-VVDLAYVPLLIQYDLSvTVATQEWLEAALQQltPESNTPLRVHLKVDTGMGRIGFlTPEETKQAVRFVQSHKEFLWEG 165
Cdd:PRK03646 79 EgFFHAQDLELYDQHRLT-TCVHSNWQLKALQN--ARLKAPLDIYLKVNSGMNRLGF-QPERVQTVWQQLRAMGNVGEMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 166 IFTHFSTADEIDTSyfEKQAGRFKAVLavlEELPRYVHVSNSATALWHPDVPGNMIRYGVAMYGLNPSG--NKLAPSyAL 243
Cdd:PRK03646 155 LMSHFARADHPDGI--SEAMARIEQAA---EGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGqwRDIANT-GL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 244 KPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL-QGFTVLVNGKRCEIVGRVCMDQCMIRLA 322
Cdd:PRK03646 229 RPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVGTVSMDMLAVDLT 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 488284520 323 eEVP---VGSVVTLVGKdgneENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:PRK03646 309 -PCPqagIGTPVELWGK----EIKIDDVAAAAGTIGYELMCALALRVPVVT 354
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
9-370 |
1.62e-74 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 246.41 E-value: 1.62e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 9 TRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSV 88
Cdd:PRK11930 460 TVLEINLNAIVHNLNYYRSKLKPETKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNP 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 89 VDLAYvPLLIQYDLSVTVATQEWLEAALQQLTPESNTPLRVHLKVDTGMGRIGFLtPEETKQAVRFVQSHKEFLWEGIFT 168
Cdd:PRK11930 540 EPTSF-DTIIDYKLEPEIYSFRLLDAFIKAAQKKGITGYPIHIKIDTGMHRLGFE-PEDIPELARRLKKQPALKVRSVFS 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 169 HFSTADEIDTSYF-EKQAGRFKAVLAVLEELPRYV---HVSNSATALWHPDVPGNMIRYGVAMYGLNPSGnklAPSYALK 244
Cdd:PRK11930 618 HLAGSDDPDHDDFtRQQIELFDEGSEELQEALGYKpirHILNSAGIERFPDYQYDMVRLGIGLYGVSASG---AGQQALR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 245 PALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL---QGFtVLVNGKRCEIVGRVCMDQCMIRL 321
Cdd:PRK11930 695 NVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLgngVGY-VLVNGQKAPIVGNICMDMCMIDV 773
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 488284520 322 ----AEEvpvGSVVTLVGkdgnEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:PRK11930 774 tdidAKE---GDEVIIFG----EELPVTELADALNTIPYEILTSISPRVKRVY 819
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
6-370 |
7.51e-65 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 211.41 E-value: 7.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 6 HRPTRLHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILI 85
Cdd:PRK13340 38 PRNAWLEISPGAFRHNIKTLRSLLANKSKVCAVMKADAYGHGIELLMPSIIKANVPCIGIASNEEARRVRELGFTGQLLR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 86 LSVVDLAYVPLLIQYDLSVTVATQEWLEAaLQQLTPESNTPLRVHLKVDT-GMGRIGF--LTPEETKQAVRFVQsHKEFL 162
Cdd:PRK13340 118 VRSASPAEIEQALRYDLEELIGDDEQAKL-LAAIAKKNGKPIDIHLALNSgGMSRNGLdmSTARGKWEALRIAT-LPSLG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 163 WEGIFTHFSTADEidtSYFEKQAGRFKAVLAVLEE---LPR---YVHVSNSATALWHPDVPGNMIRYGVAMYGlnpSGNK 236
Cdd:PRK13340 196 IVGIMTHFPNEDE---DEVRWKLAQFKEQTAWLIGeagLKRekiTLHVANSYATLNVPEAHLDMVRPGGILYG---DRHP 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 237 LAPSYalKPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFT-VLVNGKRCEIVGRVCMD 315
Cdd:PRK13340 270 ANTEY--KRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKApVLINGQRAPVVGRVSMN 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 488284520 316 QCMIRLAE--EVPVGSVVTLVGKDGNEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:PRK13340 348 TLMVDVTDipNVKPGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIY 404
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
246-370 |
2.34e-62 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 195.66 E-value: 2.34e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 246 ALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQG-FTVLVNGKRCEIVGRVCMDQCMIRL--A 322
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNrGEVLINGKRAPIVGRVCMDQLMVDVtdV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488284520 323 EEVPVGSVVTLVGKDGNEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:pfam00842 81 PEVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
246-370 |
1.47e-59 |
|
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: 188.43 E-value: 1.47e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 246 ALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHLQGFTVLVNGKRCEIVGRVCMDQCMIRL--AE 323
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVtdIP 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 488284520 324 EVPVGSVVTLVGKDgneENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:smart01005 81 DVKVGDEVVLFGPQ---EITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
11-370 |
1.00e-40 |
|
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: 147.10 E-value: 1.00e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 11 LHIDTQAITENVQKECQRLPEGTALFAVVKANGYGHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSVVD 90
Cdd:cd06826 4 LEISTGAFENNIKLLKKLLGGNTKLCAVMKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVRTAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 91 LAYVPLLIQYDL-----SVTVATQewleaaLQQLTPESNTPLRVHLKVDT-GMGRIGF-LTPEETK-QAVRFVqSHKEFL 162
Cdd:cd06826 84 PSEIEDALAYNIeeligSLDQAEQ------IDSLAKRHGKTLPVHLALNSgGMSRNGLeLSTAQGKeDAVAIA-TLPNLK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 163 WEGIFTHFSTADEidtSYFEKQAGRFKAVLA-VLEE--LPR---YVHVSNSATALWHPDVPGNMIRYGVAMYGLNPsgnk 236
Cdd:cd06826 157 IVGIMTHFPVEDE---DDVRAKLARFNEDTAwLISNakLKRekiTLHAANSFATLNVPEAHLDMVRPGGILYGDTP---- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 237 laPSYALKPALRLTSELIHVKRLAAGEGIGYGETYVTEAEEWIGTVPIGYADGWLRHL--QGFtVLVNGKRCEIVGRVCM 314
Cdd:cd06826 230 --PSPEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFsnKAH-VLINGQRVPVVGKVSM 306
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 488284520 315 DQCMIRLAE--EVPVGSVVTLVGKDGNEENTLQMVAEKLETIHYEVACTFSQRIPREY 370
Cdd:cd06826 307 NTVMVDVTDipGVKAGDEVVLFGKQGGAEITAAEIEEGSGTILAELYTLWGQTNPRVY 364
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
18-224 |
4.69e-31 |
|
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: 117.03 E-value: 4.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 18 ITENVQKECQRLPEGTALFAVVKANGyghgAVESAKAAKKGGaTGFCVALLDEAIELREAGV-QDPILILSVV-DLAYVP 95
Cdd:cd06808 1 IRHNYRRLREAAPAGITLFAVVKANA----NPEVARTLAALG-TGFDVASLGEALLLRAAGIpPEPILFLGPCkQVSELE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 96 LLIQY-DLSVTVATQEWLEAaLQQLTPESNTPLRVHLKVDTG--MGRIGfLTPEETKQAVRFVQSHKEFLWEGIFTHFST 172
Cdd:cd06808 76 DAAEQgVIVVTVDSLEELEK-LEEAALKAGPPARVLLRIDTGdeNGKFG-VRPEELKALLERAKELPHLRLVGLHTHFGS 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488284520 173 ADEiDTSYFEKQAGRFKAVLAVLEEL---PRYVHVSNSATALWHPDVPG---NMIRYG 224
Cdd:cd06808 154 ADE-DYSPFVEALSRFVAALDQLGELgidLEQLSIGGSFAILYLQELPLgtfIIVEPG 210
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
46-169 |
2.67e-09 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 58.22 E-value: 2.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 46 HGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDpILIL-SVVDLAYVPLLIQY-----DLSVTV---ATQEWLEAAL 116
Cdd:COG3616 43 HKSPELARRQLAAGAWGITVATLAEAEVLAAAGVDD-ILLAyPLVGPAKLARLAALaragaRLTVLVdsvEQAEALAAAA 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 488284520 117 QqltpESNTPLRVHLKVDTGMGRIGFLTPEETKQAVRFVQSHKEFLWEGIFTH 169
Cdd:COG3616 122 A----AAGRPLRVLVELDVGGGRTGVRPPEAALALARAIAASPGLRLAGLMTY 170
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
46-166 |
4.23e-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: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 46 HGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDpILILS-VVDLAYVPLLIQ----YDLSVTVATQEWLEAaLQQLT 120
Cdd:cd06819 42 HKCPAIARRQIAAGAVGVCCQKLSEAEVMAAAGIRD-ILITNeVVGPAKIARLAAlarrAPLIVCVDHPDNVRA-LAAAA 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488284520 121 PESNTPLRVHLKVDTGMGRIGFLTPEETKQAVRFVQSHKEFLWEGI 166
Cdd:cd06819 120 VEAGVRLDVLVEIDVGQGRCGVPPGEAALALARTIAALPGLRFAGL 165
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
46-169 |
8.04e-07 |
|
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: 50.39 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 46 HGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDpILIlsvvdlAY-----------VPLLIQYDLSVTVATQEWLEA 114
Cdd:cd06820 38 HKSPEIARLQLAAGAIGITVATVGEAEVMADAGLSD-IFI------AYpivgrqklerlRALAERVTLSVGVDSAEVARG 110
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 488284520 115 aLQQLTPESNTPLRVHLKVDTGMGRIGFLTPEETKQAVRFVQSHKEFLWEGIFTH 169
Cdd:cd06820 111 -LAEVAEGAGRPLEVLVEVDSGMNRCGVQTPEDAVALARAIASAPGLRFRGIFTY 164
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
10-170 |
6.97e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily is composed of uncharacterized bacterial proteins with similarity to bacterial alanine racemases (AR), which are fold type III PLP-dependent enzymes containing 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. It catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. Members of this subfamily may act as PLP-dependent enzymes.
Pssm-ID: 143490 [Multi-domain] Cd Length: 353 Bit Score: 47.54 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 10 RLHIDTQAITENVQKECQRL-PEGTALFAVVKANgygHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSV 88
Cdd:cd06815 3 RLEINLSKIRHNAKVLVELCkSRGIEVTGVTKVV---CGDPEIAEALLEGGITHLADSRIENLKKLKDLGISGPKMLLRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 89 VDLAYVPLLIQY-DLSVT--VATQEWL-EAALQQltpesNTPLRVHLKVDTGMGRIGFLtPEETKQAVRFVQSHKEFLWE 164
Cdd:cd06815 80 PMLSEVEDVVKYaDISLNseLETIKALsEEAKKQ-----GKIHKIILMVDLGDLREGVL-PEDLLDFVEEILKLPGIELV 153
|
....*.
gi 488284520 165 GIFTHF 170
Cdd:cd06815 154 GIGTNL 159
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
17-263 |
7.12e-05 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase; This family includes eukaryotic D-serine dehydratases (DSD), cryptic DSDs from bacteria, D-threonine aldolases (D-TA), low specificity D-TAs, and similar uncharacterized proteins. DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. D-TA reversibly catalyzes the aldol cleavage of D-threonine into glycine and acetaldehyde, and the synthesis of D-threonine from glycine and acetaldehyde. Members of this family are fold type III PLP-dependent enzymes, similar to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143511 [Multi-domain] Cd Length: 345 Bit Score: 44.38 E-value: 7.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 17 AITENVQKECQRLPE-GTALFAVVKAngygHGAVESAKAAKKGGATGFCVALLDEAIELREAGVQDPILILSVVDLAYVP 95
Cdd:cd07376 1 ALEANISRMAARARAsGVRLRPHVKT----HKSPELAQRQLAAGARGVTVATLAEAETFAEAGVKDILMAYPLVGPAAIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 96 LLI-----QYDLSVTVATQEWLeAALQQLTPESNTPLRVHLKVDTGMGRIGFlTPEETKQ--AVRFVQSHKEFLWEGIFT 168
Cdd:cd07376 77 RLAgllrqEAEFHVLVDSPEAL-AALAAFAAAHGVRLRVMLEVDVGGHRSGV-RPEEAAAlaLADAVQASPGLRLAGVMA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 169 HFSTADEIDTSYFEKQAG-----RFKAVLAVLEE-LPR-YVHVSNSATALWHPDVPG-NMIRYGVamYGLNPSGNKLAPS 240
Cdd:cd07376 155 YEGHIYGAGGAREGAQARdqavaAVRAAAAAAERgLACpTVSGGGTPTYQLTAGDRAvTELRAGS--YVFMDTGFDTLGA 232
|
250 260
....*....|....*....|....
gi 488284520 241 YALKP-ALRLTSElihVKRLAAGE 263
Cdd:cd07376 233 CAQRPaAFRVTTV---ISRPAPTG 253
|
|
| PLPDE_III_DSD_D-TA_like_3 |
cd06814 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
106-165 |
7.08e-03 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and D-Threonine Aldolase, Unknown Group 3; This subfamily is composed of uncharacterized bacterial proteins with similarity to eukaryotic D-serine dehydratases (DSD) and D-threonine aldolases (D-TA). 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. DSD and D-TA 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 their similarity to AR, it is possible members of this family also form dimers in solution.
Pssm-ID: 143489 [Multi-domain] Cd Length: 379 Bit Score: 38.09 E-value: 7.08e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284520 106 VATQEWLEAaLQQLTPESNTPLRVHLKVDTGMGRIGFLTPEETKQAVRFVQSHKEFLWEG 165
Cdd:cd06814 114 IDTPERLAQ-YRALARSLGLTLRINLELDVGLHRGGFADPQTLPKALTAIDAPPRLRFSG 172
|
|
| |
