|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-358 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143500 [Multi-domain] Cd Length: 354 Bit Score: 594.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 3 AATVVINRRALRHNLQRLRELAPASKLVAVVKANAYGHGLLETARTLPDADAFGVARLEEALRLRAGGIAQPILLLEGFF 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 83 EAADLPTIADQHLHTAVHNEEQLSALETAELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVrQPVNIVSHFAR 162
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNV-ASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 163 ADEPDCGATEQQLDIFNTFCEGKPGMRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPwGPDFGFQPVMSLVSKLI 242
Cdd:cd06827 160 ADEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKS-GADLGLKPVMTLSSEII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 243 AVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGPDAQDKAGDDV 322
Cdd:cd06827 239 AVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPV 318
|
330 340 350
....*....|....*....|....*....|....*.
gi 504643188 323 VMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:cd06827 319 ELWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-358 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 590.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 1 MQAATVVINRRALRHNLQRLRELAPA-SKLVAVVKANAYGHGLLETARTL--PDADAFGVARLEEALRLRAGGIAQPILL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPkSKLMAVVKANAYGHGAVEVAKTLleAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 78 LEGFFEAADLPTIADQHLHTAVHNEEQLSALETAELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRQpVNIV 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 158 SHFARADEPDCGATEQQLDIFNTFCEGKPG----MRSIAASGGILLWPQSHFDWARPGIILYGVSPLeNRPWGPDFGFQP 233
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGkgkpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPS-GEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 234 VMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGPD 313
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 504643188 314 AQDKAGDDVVMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:PRK00053 319 PQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-358 |
0e+00 |
|
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: 520.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 2 QAATVVINRRALRHNLQRLR-ELAPASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRnHIGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 79 EGFFeAADLPTIADQHLHTAVHNEEQLSALETAELSEP--VTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRQPVNI 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 157 VSHFARADEPDCGATEQQLDIFNTFCEGKPG------MRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPWGPDFG 230
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQqnieppFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 231 FQPVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDL 310
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504643188 311 GPDAQDKAGDDVVMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
4-359 |
2.28e-174 |
|
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: 488.85 E-value: 2.28e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 4 ATVVINRRALRHNLQRLRELA-PASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLLEG 80
Cdd:COG0787 4 AWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALLEagADGFAVATLEEALELREAGIDAPILVLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 81 FfEAADLPTIADQHLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRqPVNIVS 158
Cdd:COG0787 84 V-PPEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLE-VEGIMS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 159 HFARADEPDCGATEQQLDIFNTFCEG------KPGMRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPwgPDFGFQ 232
Cdd:COG0787 162 HFACADEPDHPFTAEQLERFEEAVAAlpaaglDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVA--ADLGLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 233 PVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGP 312
Cdd:COG0787 240 PVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504643188 313 DAQDKAGDDVVMWG-DGLPVERIAEITKVSAYELITRLTSRVAMKYID 359
Cdd:COG0787 320 IPDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
5.18e-84 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 254.07 E-value: 5.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 8 INRRALRHNLQRLRELA-PASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLLEGFfEA 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALLEggADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 85 ADLPTIADQHLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRqPVNIVSHFAR 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLR-LEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504643188 163 ADEPDCGATEQQLDIFNTFCEGKPG------MRSIAASGGILLWPQsHFDWARPGIILYGVSP 219
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 ... |
234-357 |
1.15e-55 |
|
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: 178.03 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 234 VMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAApSGTPVLVNGREVTIVGRVAMDMICVDLGPD 313
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRAL-SNGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 504643188 314 AQDKAGDDVVMWGDG-LPVERIAEITKVSAYELITRLTSRVAMKY 357
Cdd:smart01005 80 PDVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLPDE_III_AR_proteobact |
cd06827 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ... |
3-358 |
0e+00 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; This subfamily is composed mainly of proteobacterial alanine racemases (EC 5.1.1.1), fold type III PLP-dependent enzymes that catalyze the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. hese proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143500 [Multi-domain] Cd Length: 354 Bit Score: 594.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 3 AATVVINRRALRHNLQRLRELAPASKLVAVVKANAYGHGLLETARTLPDADAFGVARLEEALRLRAGGIAQPILLLEGFF 82
Cdd:cd06827 1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALADADGFAVACIEEALALREAGITKPILLLEGFF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 83 EAADLPTIADQHLHTAVHNEEQLSALETAELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVrQPVNIVSHFAR 162
Cdd:cd06827 81 SADELPLAAEYNLWTVVHSEEQLEWLEQAALSKPLNVWLKLDSGMHRLGFSPEEYAAAYQRLKASPNV-ASIVLMTHFAC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 163 ADEPDCGATEQQLDIFNTFCEGKPGMRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPwGPDFGFQPVMSLVSKLI 242
Cdd:cd06827 160 ADEPDSPGTAKQLAIFEQATAGLPGPRSLANSAAILAWPEAHGDWVRPGIMLYGASPFADKS-GADLGLKPVMTLSSEII 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 243 AVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGPDAQDKAGDDV 322
Cdd:cd06827 239 AVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHAPSGTPVLVNGQRTPLVGRVSMDMLTVDLTDLPEAKVGDPV 318
|
330 340 350
....*....|....*....|....*....|....*.
gi 504643188 323 VMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:cd06827 319 ELWGKGLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
|
|
| alr |
PRK00053 |
alanine racemase; Reviewed |
1-358 |
0e+00 |
|
alanine racemase; Reviewed
Pssm-ID: 234600 [Multi-domain] Cd Length: 363 Bit Score: 590.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 1 MQAATVVINRRALRHNLQRLRELAPA-SKLVAVVKANAYGHGLLETARTL--PDADAFGVARLEEALRLRAGGIAQPILL 77
Cdd:PRK00053 1 MRPATAEIDLDALRHNLRQIRKHAPPkSKLMAVVKANAYGHGAVEVAKTLleAGADGFGVATLEEALELREAGITAPILI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 78 LEGFFEAADLPTIADQHLHTAVHNEEQLSALETAELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRQpVNIV 157
Cdd:PRK00053 81 LGGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL-EGIF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 158 SHFARADEPDCGATEQQLDIFNTFCEGKPG----MRSIAASGGILLWPQSHFDWARPGIILYGVSPLeNRPWGPDFGFQP 233
Cdd:PRK00053 160 SHFATADEPDNSYTEQQLNRFEAALAGLPGkgkpLRHLANSAAILRWPDLHFDWVRPGIALYGLSPS-GEPLGLDFGLKP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 234 VMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGPD 313
Cdd:PRK00053 239 AMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLPSGTPVLVNGRRVPIVGRVSMDQLTVDLGPD 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 504643188 314 AQDKAGDDVVMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:PRK00053 319 PQDKVGDEVTLWGEALTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
|
|
| alr |
TIGR00492 |
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ... |
2-358 |
0e+00 |
|
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: 520.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 2 QAATVVINRRALRHNLQRLR-ELAPASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLL 78
Cdd:TIGR00492 1 RPATVEIDLAALKHNLSAIRnHIGPKSKIMAVVKANAYGHGLIEVAKTLLQagADYFGVANLEEAITLRKAGITAPILLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 79 EGFFeAADLPTIADQHLHTAVHNEEQLSALETAELSEP--VTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRQPVNI 156
Cdd:TIGR00492 81 GGFF-AEDLKILAAWDLTTTVHSVEQLQALEEALLKEPkrLKVHLKIDTGMNRLGVKPDEAALFVQKLRQLKKFLELEGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 157 VSHFARADEPDCGATEQQLDIFNTFCEGKPG------MRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPWGPDFG 230
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKQqnieppFRHIANSAAILNWPESHFDMVRPGIILYGLYPSADMSDGAPFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 231 FQPVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDL 310
Cdd:TIGR00492 240 LKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALSNGTPVLVNGKRVPIVGRVCMDMIMVDL 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504643188 311 GPDAQDKAGDDVVMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:TIGR00492 320 GPDLQDKTGDEVILWGEEISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
|
|
| Alr |
COG0787 |
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ... |
4-359 |
2.28e-174 |
|
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: 488.85 E-value: 2.28e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 4 ATVVINRRALRHNLQRLRELA-PASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLLEG 80
Cdd:COG0787 4 AWAEIDLDALRHNLRVLRALAgPGAKLMAVVKADAYGHGAVEVARALLEagADGFAVATLEEALELREAGIDAPILVLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 81 FfEAADLPTIADQHLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRqPVNIVS 158
Cdd:COG0787 84 V-PPEDLELAIEYDLEPVVHSLEQLEALAAAarRLGKPLPVHLKVDTGMNRLGFRPEEAPALAARLAALPGLE-VEGIMS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 159 HFARADEPDCGATEQQLDIFNTFCEG------KPGMRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPwgPDFGFQ 232
Cdd:COG0787 162 HFACADEPDHPFTAEQLERFEEAVAAlpaaglDPPLRHLANSAAILRYPEAHFDMVRPGIALYGLSPSPEVA--ADLGLK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 233 PVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGP 312
Cdd:COG0787 240 PVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLSNGGPVLINGKRAPIVGRVSMDQIMVDVTD 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 504643188 313 DAQDKAGDDVVMWG-DGLPVERIAEITKVSAYELITRLTSRVAMKYID 359
Cdd:COG0787 320 IPDVKVGDEVVLFGeQGITADELAEAAGTISYEILTRLGPRVPRVYVG 367
|
|
| PLPDE_III_AR |
cd00430 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ... |
4-358 |
2.13e-145 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes predominantly bacterial alanine racemases (AR), some serine racemases (SerRac), and putative bifunctional enzymes containing N-terminal UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase (murF) and C-terminal AR domains. These proteins are fold type III PLP-dependent enzymes that play essential roles in peptidoglycan biosynthesis. AR catalyzes the interconversion between L- and D-alanine, which is an essential component of the peptidoglycan layer of bacterial cell walls. SerRac converts L-serine into its D-enantiomer (D-serine) for peptidoglycan synthesis. murF catalyzes the addition of D-Ala-D-Ala to UDPMurNAc-tripeptide, the final step in the synthesis of the cytoplasmic precursor of bacterial cell wall peptidoglycan. Members of this family contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. AR and other members of this family require dimer formation and the presence of the PLP cofactor for catalytic activity. Fungal ARs and eukaryotic serine racemases, which are fold types I and II PLP-dependent enzymes respectively, are excluded from this family.
Pssm-ID: 143481 [Multi-domain] Cd Length: 367 Bit Score: 415.74 E-value: 2.13e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 4 ATVVINRRALRHNLQRLRELA-PASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLLeG 80
Cdd:cd00430 2 TWAEIDLDALRHNLRVIRRLLgPGTKIMAVVKADAYGHGAVEVAKALEEagADYFAVATLEEALELREAGITAPILVL-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 81 FFEAADLPTIADQHLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRqPVNIVS 158
Cdd:cd00430 81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAaaRLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLE-LEGVFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 159 HFARADEPDCGATEQQLDIFNTFCE------GKPGMRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPWGPdfGFQ 232
Cdd:cd00430 160 HFATADEPDKAYTRRQLERFLEALAeleeagIPPPLKHLANSAAILRFPEAHFDMVRPGIALYGLYPSPEVKSPL--GLK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 233 PVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGP 312
Cdd:cd00430 238 PVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNKGEVLIRGKRAPIVGRVCMDQTMVDVTD 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 504643188 313 DAQDKAGDDVVMWGDG----LPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:cd00430 318 IPDVKVGDEVVLFGRQgdeeITAEELAELAGTINYEILCRISKRVPRIYV 367
|
|
| dadX |
PRK03646 |
catabolic alanine racemase; |
1-358 |
3.30e-139 |
|
catabolic alanine racemase;
Pssm-ID: 179622 [Multi-domain] Cd Length: 355 Bit Score: 399.49 E-value: 3.30e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 1 MQAATVVINRRALRHNLQRLRELAPASKLVAVVKANAYGHGLLETARTLPDADAFGVARLEEALRLRAGGIAQPILLLEG 80
Cdd:PRK03646 1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSALGATDGFAVLNLEEAITLRERGWKGPILMLEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 81 FFEAADLPTIADQHLHTAVHNEEQLSALETAELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRQPVnIVSHF 160
Cdd:PRK03646 81 FFHAQDLELYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQTVWQQLRAMGNVGEMT-LMSHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 161 ARADEPDCgaTEQQLDIFNTFCEGKPGMRSIAASGGILLWPQSHFDWARPGIILYGVSPLENRPWGPDFGFQPVMSLVSK 240
Cdd:PRK03646 160 ARADHPDG--ISEAMARIEQAAEGLECERSLSNSAATLWHPQAHFDWVRPGIILYGASPSGQWRDIANTGLRPVMTLSSE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 241 LIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGPDAQDKAGD 320
Cdd:PRK03646 238 IIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHAPTGTPVLVDGVRTRTVGTVSMDMLAVDLTPCPQAGIGT 317
|
330 340 350
....*....|....*....|....*....|....*...
gi 504643188 321 DVVMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:PRK03646 318 PVELWGKEIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
|
|
| Ala_racemase_N |
pfam01168 |
Alanine racemase, N-terminal domain; |
8-219 |
5.18e-84 |
|
Alanine racemase, N-terminal domain;
Pssm-ID: 460095 [Multi-domain] Cd Length: 220 Bit Score: 254.07 E-value: 5.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 8 INRRALRHNLQRLRELA-PASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLLEGFfEA 84
Cdd:pfam01168 1 IDLDALRHNLRRLRRRAgPGAKLMAVVKANAYGHGAVEVARALLEggADGFAVATLDEALELREAGITAPILVLGGF-PP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 85 ADLPTIADQHLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRqPVNIVSHFAR 162
Cdd:pfam01168 80 EELALAAEYDLTPTVDSLEQLEALAAAarRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLR-LEGLMTHFAC 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504643188 163 ADEPDCGATEQQLDIFNTFCEGKPG------MRSIAASGGILLWPQsHFDWARPGIILYGVSP 219
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAaglrppVVHLANSAAILLHPL-HFDMVRPGIALYGLSP 220
|
|
| PLPDE_III_VanT |
cd06825 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ... |
4-358 |
2.12e-83 |
|
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: 257.67 E-value: 2.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 4 ATVVINRRALRHNLQRLRELAPA-SKLVAVVKANAYGHGLLETARTLPDA--DAFGVARLEEALRLRAGGIAQPILLLeG 80
Cdd:cd06825 2 AWLEIDLSALEHNVKEIKRLLPStCKLMAVVKANAYGHGDVEVARVLEQIgiDFFAVATIDEGIRLREAGIKGEILIL-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 81 FFEAADLPTIADQHLHTAVHNEEQlsALETAELSEPVTVWMKLDTGMHRLGVRPENAQAFyQRLCQCKNVRQpVNIVSHF 160
Cdd:cd06825 81 YTPPVRAKELKKYSLTQTLISEAY--AEELSKYAVNIKVHLKVDTGMHRLGESPEDIDSI-LAIYRLKNLKV-SGIFSHL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 161 ARAD---EPDCGATEQQLDIFNTFCEG------KPGMRSIAASGGILLWPQSHFDWARPGIILYGV--SPLENRPWGPDf 229
Cdd:cd06825 157 CVSDsldEDDIAFTKHQIACFDQVLADlkargiEVGKIHIQSSYGILNYPDLKYDYVRPGILLYGVlsDPNDPTKLGLD- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 230 gFQPVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRA-APSGTPVLVNGREVTIVGRVAMDMICV 308
Cdd:cd06825 236 -LRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSlSNQKAYVLINGKRAPIIGNICMDQLMV 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 504643188 309 DLG--PDAqdKAGDDVVMWGDG----LPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:cd06825 315 DVTdiPEV--KEGDTATLIGQDgdeeLSADEVARNAHTITNELLSRIGERVKRIYK 368
|
|
| PRK13340 |
PRK13340 |
alanine racemase; Reviewed |
8-359 |
3.42e-78 |
|
alanine racemase; Reviewed
Pssm-ID: 183984 [Multi-domain] Cd Length: 406 Bit Score: 245.69 E-value: 3.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 8 INRRALRHNLQRLRELAPA-SKLVAVVKANAYGHGLletARTLP-----DADAFGVARLEEALRLRAGGIAQPILLLEGF 81
Cdd:PRK13340 45 ISPGAFRHNIKTLRSLLANkSKVCAVMKADAYGHGI---ELLMPsiikaNVPCIGIASNEEARRVRELGFTGQLLRVRSA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 82 fEAADLpTIADQH-LHTAVHNEEQLSALET--AELSEPVTVWMKLDT-GMHRLGVRPENAQAFYQ--RLCQCKNVrQPVN 155
Cdd:PRK13340 122 -SPAEI-EQALRYdLEELIGDDEQAKLLAAiaKKNGKPIDIHLALNSgGMSRNGLDMSTARGKWEalRIATLPSL-GIVG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 156 IVSHFARADEpdcGATEQQLDIFNTFCEGKPGMRSI--------AASGGILLW-PQSHFDWARPGIILYGVSPLENRPwg 226
Cdd:PRK13340 199 IMTHFPNEDE---DEVRWKLAQFKEQTAWLIGEAGLkrekitlhVANSYATLNvPEAHLDMVRPGGILYGDRHPANTE-- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 227 pdfgFQPVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMI 306
Cdd:PRK13340 274 ----YKRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHASNKAPVLINGQRAPVVGRVSMNTL 349
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 504643188 307 CVDLGPDAQDKAGDDVVMWGD----GLPVERIAEITKVSAYELITRLTSRVAMKYID 359
Cdd:PRK13340 350 MVDVTDIPNVKPGDEVVLFGKqgnaEITVDEVEEASGTIFPELYTAWGRTNPRIYVP 406
|
|
| PRK11930 |
PRK11930 |
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ... |
8-358 |
4.14e-70 |
|
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional
Pssm-ID: 237026 [Multi-domain] Cd Length: 822 Bit Score: 234.08 E-value: 4.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 8 INRRALRHNLQRLRE-LAPASKLVAVVKANAYGHGLLETARTLPD--ADAFGVARLEEALRLRAGGIAQPILLLEGffEA 84
Cdd:PRK11930 464 INLNAIVHNLNYYRSkLKPETKIMCMVKAFAYGSGSYEIAKLLQEhrVDYLAVAYADEGVSLRKAGITLPIMVMNP--EP 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 85 ADLPTIADQHLHTAVHNEEQLSALETAELSEPVTVW---MKLDTGMHRLGVRPENAQAFYQRLCQCKNVRqPVNIVSHFA 161
Cdd:PRK11930 542 TSFDTIIDYKLEPEIYSFRLLDAFIKAAQKKGITGYpihIKIDTGMHRLGFEPEDIPELARRLKKQPALK-VRSVFSHLA 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 162 RADEPDCGA-TEQQLDIFNTFCE------GKPGMRSIAASGGILLWPQSHFDWARPGIILYGVSP--LENRpwgpdfGFQ 232
Cdd:PRK11930 621 GSDDPDHDDfTRQQIELFDEGSEelqealGYKPIRHILNSAGIERFPDYQYDMVRLGIGLYGVSAsgAGQQ------ALR 694
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 233 PVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGT-PVLVNGREVTIVGRVAMDMICVDLG 311
Cdd:PRK11930 695 NVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLGNGVgYVLVNGQKAPIVGNICMDMCMIDVT 774
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 504643188 312 pDAQDKAGDDVVMWGDGLPVERIAEITKVSAYELITRLTSRVAMKYI 358
Cdd:PRK11930 775 -DIDAKEGDEVIIFGEELPVTELADALNTIPYEILTSISPRVKRVYF 820
|
|
| Ala_racemase_C |
smart01005 |
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ... |
234-357 |
1.15e-55 |
|
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: 178.03 E-value: 1.15e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 234 VMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAApSGTPVLVNGREVTIVGRVAMDMICVDLGPD 313
Cdd:smart01005 1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRAL-SNGPVLINGQRVPVVGRVSMDQLMVDVTDI 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 504643188 314 AQDKAGDDVVMWGDG-LPVERIAEITKVSAYELITRLTSRVAMKY 357
Cdd:smart01005 80 PDVKVGDEVVLFGPQeITADELAEAAGTISYEILTRLGPRVPRVY 124
|
|
| Ala_racemase_C |
pfam00842 |
Alanine racemase, C-terminal domain; |
234-357 |
5.05e-54 |
|
Alanine racemase, C-terminal domain;
Pssm-ID: 459960 [Multi-domain] Cd Length: 128 Bit Score: 173.71 E-value: 5.05e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 234 VMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMICVDLGPD 313
Cdd:pfam00842 1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGEVLINGKRAPIVGRVCMDQLMVDVTDV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 504643188 314 AQDKAGDDVVMWGD----GLPVERIAEITKVSAYELITRLTSRVAMKY 357
Cdd:pfam00842 81 PEVKVGDEVTLFGKqgdeEITADELAEAAGTINYEILCSLGKRVPRVY 128
|
|
| PLPDE_III |
cd06808 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ... |
13-212 |
3.53e-47 |
|
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: 159.02 E-value: 3.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 13 LRHNLQRLRELAPA-SKLVAVVKANAYghglLETARTLPD-ADAFGVARLEEALRLRAGGIA-QPILLLEGFFEAADLPT 89
Cdd:cd06808 1 IRHNYRRLREAAPAgITLFAVVKANAN----PEVARTLAAlGTGFDVASLGEALLLRAAGIPpEPILFLGPCKQVSELED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 90 IADQ-HLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTG--MHRLGVRPENAQAFYQRLCQCKNVrQPVNIVSHFARAD 164
Cdd:cd06808 77 AAEQgVIVVTVDSLEELEKLEEAalKAGPPARVLLRIDTGdeNGKFGVRPEELKALLERAKELPHL-RLVGLHTHFGSAD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504643188 165 EpDCGATEQQLDIFNTFCEG------KPGMRSIAASGGILLW---PQSHFDWARPGI 212
Cdd:cd06808 156 E-DYSPFVEALSRFVAALDQlgelgiDLEQLSIGGSFAILYLqelPLGTFIIVEPGR 211
|
|
| PLPDE_III_AR2 |
cd06826 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ... |
8-326 |
5.09e-44 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is composed of bacterial alanine racemases (EC 5.1.1.1) with similarity to Yersinia pestis and Vibrio cholerae alanine racemase (AR) 2. ARs catalyze the interconversion between L- and D-alanine, an essential component of the peptidoglycan layer of bacterial cell walls. These proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.
Pssm-ID: 143499 [Multi-domain] Cd Length: 365 Bit Score: 155.58 E-value: 5.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 8 INRRALRHNLQRLRELAPA-SKLVAVVKANAYGHGLLETARTLPDAD--AFGVARLEEALRLRAGGIAQPILLLEgffeA 84
Cdd:cd06826 6 ISTGAFENNIKLLKKLLGGnTKLCAVMKADAYGHGIALVMPSIIAQNipCVGITSNEEARVVREAGFTGKILRVR----T 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 85 ADLPTIADQHlhtAVHNEEQLSALETAE--------LSEPVTVWMKLDT-GMHRLGV--RPENAQAFYQRLCQCKNVRqP 153
Cdd:cd06826 82 ATPSEIEDAL---AYNIEELIGSLDQAEqidslakrHGKTLPVHLALNSgGMSRNGLelSTAQGKEDAVAIATLPNLK-I 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 154 VNIVSHFARADEPDCGATEQQ--LDIFNTFCEGKPGMRSI----AASGGILLWPQSHFDWARPGIILYGVSPlenrpwgP 227
Cdd:cd06826 158 VGIMTHFPVEDEDDVRAKLARfnEDTAWLISNAKLKREKItlhaANSFATLNVPEAHLDMVRPGGILYGDTP-------P 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 228 DFGFQPVMSLVSKLIAVREHKAGEPVGYGGTWTSERDTRLGVVAMGYGDGYPRAAPSGTPVLVNGREVTIVGRVAMDMIC 307
Cdd:cd06826 231 SPEYKRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNKAHVLINGQRVPVVGKVSMNTVM 310
|
330
....*....|....*....
gi 504643188 308 VDLGPDAQDKAGDDVVMWG 326
Cdd:cd06826 311 VDVTDIPGVKAGDEVVLFG 329
|
|
| Dsd1 |
COG3616 |
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism]; |
5-151 |
2.29e-10 |
|
D-serine deaminase, pyridoxal phosphate-dependent [Amino acid transport and metabolism];
Pssm-ID: 442834 [Multi-domain] Cd Length: 357 Bit Score: 61.30 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 5 TVVINRRALRHNLQRLRE--------LAPASK---LVAVVKAnayghgLLEtartlPDADAFGVARLEEALRLRAGGIaQ 73
Cdd:COG3616 10 ALVLDLDALERNIARMAAraaahgvrLRPHGKthkSPELARR------QLA-----AGAWGITVATLAEAEVLAAAGV-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 74 PILLLEGFFEAADLPTIA-----DQHLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTGMHRLGVRP-ENAQAFYQRLC 145
Cdd:COG3616 78 DILLAYPLVGPAKLARLAalaraGARLTVLVDSVEQAEALAAAaaAAGRPLRVLVELDVGGGRTGVRPpEAALALARAIA 157
|
....*.
gi 504643188 146 QCKNVR 151
Cdd:COG3616 158 ASPGLR 163
|
|
| PLPDE_III_AR_like_1 |
cd06815 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ... |
4-322 |
4.49e-07 |
|
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: 51.01 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 4 ATVVINRRALRHNLQRLRELAPAS--KLVAVVKANAyghGLLETARTLPDADAFGVA--RLEEALRLRAGGIAQPILLLE 79
Cdd:cd06815 2 PRLEINLSKIRHNAKVLVELCKSRgiEVTGVTKVVC---GDPEIAEALLEGGITHLAdsRIENLKKLKDLGISGPKMLLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 80 --GFFEAADLPTIADQHLHTAVHNEEQLSAlETAELSEPVTVWMKLDTGMHRLGVRPENAQAFYQRLCQCKNVRQpVNIV 157
Cdd:cd06815 79 ipMLSEVEDVVKYADISLNSELETIKALSE-EAKKQGKIHKIILMVDLGDLREGVLPEDLLDFVEEILKLPGIEL-VGIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 158 SHFA--RADEPdcgaTEQQLDIFNTF---CEGKPGMRSIAASGGillwPQSHFDWARPGI-------------ILYGVSP 219
Cdd:cd06815 157 TNLGcyGGVLP----TEENMGKLVELkeeIEKEFGIKLPIISGG----NSASLPLLLKGElpgginqlrigeaILLGRET 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 220 LENRPWgPDFgFQPVMSLVSKLIAVREhKAGEPVG------YGGTWTSE-RDTRL-GVVAMGYGDgyprAAPSG-TPVLV 290
Cdd:cd06815 229 TYNEPI-PGL-YQDAFTLEAEIIEIKE-KPSVPIGeigldaFGNKPEFEdRGIRKrAILAIGRQD----VDPDGlTPVDN 301
|
330 340 350
....*....|....*....|....*....|...
gi 504643188 291 NgreVTIVGRVAmDMICVDLG-PDAQDKAGDDV 322
Cdd:cd06815 302 G---IEILGASS-DHLILDITdSDRDYKVGDEI 330
|
|
| PLPDE_III_DSD_D-TA_like |
cd07376 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes Similar to D-Serine Dehydratase and ... |
12-139 |
1.75e-06 |
|
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: 49.38 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 12 ALRHNLQRLRELAPAS--KLVAVVKAnaygHGLLETARTLPDADAFG--VARLEEALRLRAGG-----IAQPILLLEGFF 82
Cdd:cd07376 1 ALEANISRMAARARASgvRLRPHVKT----HKSPELAQRQLAAGARGvtVATLAEAETFAEAGvkdilMAYPLVGPAAIA 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 504643188 83 EAADLPTIAdQHLHTAVHNEEQLSALETAELSEPVT--VWMKLDTGMHRLGVRPENAQA 139
Cdd:cd07376 77 RLAGLLRQE-AEFHVLVDSPEALAALAAFAAAHGVRlrVMLEVDVGGHRSGVRPEEAAA 134
|
|
| PLPDE_III_DSD |
cd06817 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Eukaryotic D-Serine Dehydratase; This ... |
94-160 |
2.33e-06 |
|
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Eukaryotic D-Serine Dehydratase; This subfamily is composed of chicken D-serine dehydratase (DSD, EC 4.3.1.18) and similar eukaryotic proteins. Chicken DSD catalyzes the dehydration of D-serine to aminoacrylate, which is rapidly hydrolyzed to pyruvate and ammonia. It is a fold type III PLP-dependent enzyme 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. Experimental data suggest that chicken DSD also exists as dimers. Sequence comparison and biochemical experiments show that chicken DSD is distinct from the ubiquitous bacterial DSDs coded by dsdA gene, mammalian L-serine dehydratases (LSD) and mammalian serine racemase (SerRac), which are fold type II PLP-dependent enzymes.
Pssm-ID: 143491 [Multi-domain] Cd Length: 389 Bit Score: 48.87 E-value: 2.33e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504643188 94 HLHTAVHNEEQLSALETAEL---SEPVTVWMKLDTGMHRLGVRPENAQA--FYQRLCQCKNVRQPVNIVSHF 160
Cdd:cd06817 106 HLRVMVDNPEQLDFLEQFQPlksGKKWSVFIKVDCGTHRAGVPPESEDAkeLIQKLEKASEAVELFGFYSHA 177
|
|
| PLPDE_III_LS_D-TA_like |
cd06820 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ... |
5-151 |
2.15e-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: 45.77 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 5 TVVINRRALRHNLQRLRELAPASKLVavVKANAYGHGLLETARTLPDADAFG--VARLEEALRLRAGG-----IAQPILl 77
Cdd:cd06820 5 ALLIDLDRLERNIARMQAYADAHGLS--LRPHIKTHKSPEIARLQLAAGAIGitVATVGEAEVMADAGlsdifIAYPIV- 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504643188 78 leGFFEAADLPTIADQH-LHTAVHNEEQLSALET--AELSEPVTVWMKLDTGMHRLGVR-PENAQAFYQRLCQCKNVR 151
Cdd:cd06820 82 --GRQKLERLRALAERVtLSVGVDSAEVARGLAEvaEGAGRPLEVLVEVDSGMNRCGVQtPEDAVALARAIASAPGLR 157
|
|
| PLPDE_III_D-TA |
cd06821 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme D-Threonine Aldolase; D-threonine ... |
12-151 |
2.38e-05 |
|
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: 45.75 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 12 ALRHNLQRLRELA-PASKLVAVVKAnaygHGLLETARTLPDA--DAFGVARLEEALRLRAGGIAQpILL--------LEG 80
Cdd:cd06821 18 RIEENIRRMIRMAgDPQRLRPHVKT----HKMAEIVRLQLEAgiTKFKCATIAEAEMLAEAGAPD-VLLayplvgpnIER 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504643188 81 FFEAADlpTIADQHLHTAVHNEEQLSALETAELSE--PVTVWMKLDTGMHRLGVRP-ENAQAFYQRLCQCKNVR 151
Cdd:cd06821 93 FLELAK--KYPGTRFSALVDDLEAAEALSAAAGSAglTLSVLLDVNTGMNRTGIAPgEDAEELYRAIATLPGLV 164
|
|
| PLPDE_III_LS_D-TA |
cd06819 |
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Low Specificity D-Threonine Aldolase; ... |
7-134 |
2.90e-04 |
|
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: 42.20 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504643188 7 VINRRALRHNLQRLRELAPASKLVavVKANAYGHGLLETARTLPDADAFGV--ARLEEALRLRAGGI-----AQPILLLE 79
Cdd:cd06819 11 VLDLDALERNIKRMAAFAKAHGVR--LRPHAKTHKCPAIARRQIAAGAVGVccQKLSEAEVMAAAGIrdiliTNEVVGPA 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504643188 80 GFFEAADLPTIADqhLHTAVHNEEQLSALETA--ELSEPVTVWMKLDTGMHRLGVRP 134
Cdd:cd06819 89 KIARLAALARRAP--LIVCVDHPDNVRALAAAavEAGVRLDVLVEIDVGQGRCGVPP 143
|
|
| |
