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Conserved domains on  [gi|2083174352|ref|WP_220740712|]
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alanine racemase [Leuconostoc miyukkimchii]

Protein Classification

alanine racemase( domain architecture ID 11434390)

alanine racemase catalyzes the interconversion of L-alanine and D-alanine in a pyridoxal 5-phosphate (PLP)-dependent manner

CATH:  3.20.20.10|2.40.37.10
EC:  5.1.1.1
Gene Ontology:  GO:0008784|GO:0006522|GO:0009252|GO:0030170
PubMed:  2197992
SCOP:  4003518|4003111

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Alr COG0787
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ...
 6-370 3.27e-127

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: 369.82  E-value: 3.27e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   6 TRPTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILI 84
Cdd:COG0787     1 SRPAWAEIDLDALRHNLRVLRALAGPGaKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  85 LGISPFEYAELMAVQHIITTVVSLSWLKEAAQYLSGEQR-LHVSLGVDTGMGRIGFRDRQsLAEAIAYLQDNKDIfDYVG 163
Cdd:COG0787    81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKpLPVHLKVDTGMNRLGFRPEE-APALAARLAALPGL-EVEG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 164 LATHFAESDSAETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHaDEVPHEVIRVGTVLYGVEPSrGELADGK 239
Cdd:COG0787   159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAagldPPLRHLANSAAILRY-PEAHFDMVRPGIALYGLSPS-PEVAADL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 240 NLEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMIR 318
Cdd:COG0787   237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLsNGGPVLINGKRAPIVGRVSMDQIMVD 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2083174352 319 LP--REYPDGTKVTFIGKDGdleNTLEDVAQHAGLAPWEIMTGMQGRLHRIVVD 370
Cdd:COG0787   317 VTdiPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVG 367
 
Name Accession Description Interval E-value
Alr COG0787
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ...
 6-370 3.27e-127

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: 369.82  E-value: 3.27e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   6 TRPTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILI 84
Cdd:COG0787     1 SRPAWAEIDLDALRHNLRVLRALAGPGaKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  85 LGISPFEYAELMAVQHIITTVVSLSWLKEAAQYLSGEQR-LHVSLGVDTGMGRIGFRDRQsLAEAIAYLQDNKDIfDYVG 163
Cdd:COG0787    81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKpLPVHLKVDTGMNRLGFRPEE-APALAARLAALPGL-EVEG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 164 LATHFAESDSAETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHaDEVPHEVIRVGTVLYGVEPSrGELADGK 239
Cdd:COG0787   159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAagldPPLRHLANSAAILRY-PEAHFDMVRPGIALYGLSPS-PEVAADL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 240 NLEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMIR 318
Cdd:COG0787   237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLsNGGPVLINGKRAPIVGRVSMDQIMVD 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2083174352 319 LP--REYPDGTKVTFIGKDGdleNTLEDVAQHAGLAPWEIMTGMQGRLHRIVVD 370
Cdd:COG0787   317 VTdiPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVG 367
PLPDE_III_AR cd00430
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ...
 8-369 2.47e-125

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: 364.90  E-value: 2.47e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   8 PTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILILG 86
Cdd:cd00430     1 RTWAEIDLDALRHNLRVIRRLLGPGtKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  87 ISPFEYAELMAVQHIITTVVSLSWLKEAAQYL-SGEQRLHVSLGVDTGMGRIGFRDRQSLaEAIAYLQDNKDIfDYVGLA 165
Cdd:cd00430    81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAaRLGKTLKVHLKIDTGMGRLGFRPEEAE-ELLEALKALPGL-ELEGVF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 166 THFAESDSAETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHaDEVPHEVIRVGTVLYGVEPSrGELADGKNL 241
Cdd:cd00430   159 THFATADEPDKAYTRRQLERFLEALAELEEagipPPLKHLANSAAILRF-PEAHFDMVRPGIALYGLYPS-PEVKSPLGL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 242 EPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKMTG-FNVIVDGQYAPIVGQVAMDQLMIRLP 320
Cdd:cd00430   237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNkGEVLIRGKRAPIVGRVCMDQTMVDVT 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2083174352 321 --REYPDGTKVTFIGKDGDLENTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:cd00430   317 diPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
alr PRK00053
alanine racemase; Reviewed
 7-369 1.02e-116

alanine racemase; Reviewed


Pssm-ID: 234600 [Multi-domain]  Cd Length: 363  Bit Score: 342.93  E-value: 1.02e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   7 RPTQIEISKKALKHNVSVVKS-VSGADKIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILIL 85
Cdd:PRK00053    2 RPATAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  86 -GISPFEYAELMAVQHIITTVVSLSWLKEAAQYLSGeQRLHVSLGVDTGMGRIGFRDRQsLAEAIAYLQDNKDIfDYVGL 164
Cdd:PRK00053   82 gGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELG-KPLKVHLKIDTGMHRLGVRPEE-AEAALERLLACPNV-RLEGI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 165 ATHFAESDSAETDYFYMQLKRWHDITDGLPEPEF--YHVANSGAAMYHADeVPHEVIRVGTVLYGVEPSRGELADGKNLE 242
Cdd:PRK00053  159 FSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKplRHLANSAAILRWPD-LHFDWVRPGIALYGLSPSGEPLGLDFGLK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 243 PVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMIRLP- 320
Cdd:PRK00053  238 PAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVDLGp 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2083174352 321 -REYPDGTKVTFIGKDgdleNTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:PRK00053  318 dPQDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
alr TIGR00492
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ...
 7-369 7.79e-101

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: 302.74  E-value: 7.79e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   7 RPTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILIL 85
Cdd:TIGR00492   1 RPATVEIDLAALKHNLSAIRNHIGPKsKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  86 GISPFEYAELMAVQHIITTVVSLSWLKEAAQY-LSGEQRLHVSLGVDTGMGRIGFRDRQSLAEaIAYLQDNKDIFDYVGL 164
Cdd:TIGR00492  81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEAlLKEPKRLKVHLKIDTGMNRLGVKPDEAALF-VQKLRQLKKFLELEGI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 165 ATHFAESDSAETDYFYMQLKRWHDITDGLP----EPEFYHVANSGAAMYHAdEVPHEVIRVGTVLYGVEPSrGELADGK- 239
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKqqniEPPFRHIANSAAILNWP-ESHFDMVRPGIILYGLYPS-ADMSDGAp 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 240 -NLEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMI 317
Cdd:TIGR00492 238 fGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMV 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2083174352 318 RLPREYPD--GTKVTFIGKdgdlENTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:TIGR00492 318 DLGPDLQDktGDEVILWGE----EISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
13-230 5.50e-61

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 195.52  E-value: 5.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  13 ISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILILGISPFE 91
Cdd:pfam01168   1 IDLDALRHNLRRLRRRAGPGaKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  92 YAELMAVQHIITTVVSLSWLKEAAQYLSGEQR-LHVSLGVDTGMGRIGFRDrQSLAEAIAYLQDNKDIfDYVGLATHFAE 170
Cdd:pfam01168  81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKpLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGL-RLEGLMTHFAC 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2083174352 171 SDSAETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHADEVphEVIRVGTVLYGVEP 230
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAaglrPPVVHLANSAAILLHPLHF--DMVRPGIALYGLSP 220
Ala_racemase_C smart01005
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ...
 244-368 3.23e-46

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: 153.76  E-value: 3.23e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  244 VMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKMTGFNVIVDGQYAPIVGQVAMDQLMIRLP--R 321
Cdd:smart01005   1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTdiP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2083174352  322 EYPDGTKVTFIGKDgdlENTLEDVAQHAGLAPWEIMTGMQGRLHRIV 368
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 3.27e-127

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: 369.82  E-value: 3.27e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   6 TRPTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILI 84
Cdd:COG0787     1 SRPAWAEIDLDALRHNLRVLRALAGPGaKLMAVVKADAYGHGAVEVARALLEAGADGFAVATLEEALELREAGIDAPILV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  85 LGISPFEYAELMAVQHIITTVVSLSWLKEAAQYLSGEQR-LHVSLGVDTGMGRIGFRDRQsLAEAIAYLQDNKDIfDYVG 163
Cdd:COG0787    81 LGGVPPEDLELAIEYDLEPVVHSLEQLEALAAAARRLGKpLPVHLKVDTGMNRLGFRPEE-APALAARLAALPGL-EVEG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 164 LATHFAESDSAETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHaDEVPHEVIRVGTVLYGVEPSrGELADGK 239
Cdd:COG0787   159 IMSHFACADEPDHPFTAEQLERFEEAVAALPAagldPPLRHLANSAAILRY-PEAHFDMVRPGIALYGLSPS-PEVAADL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 240 NLEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMIR 318
Cdd:COG0787   237 GLKPVMTLKARIIQVKTVPAGETVGYGRTYTAPRDTRIATVPIGYADGYPRSLsNGGPVLINGKRAPIVGRVSMDQIMVD 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2083174352 319 LP--REYPDGTKVTFIGKDGdleNTLEDVAQHAGLAPWEIMTGMQGRLHRIVVD 370
Cdd:COG0787   317 VTdiPDVKVGDEVVLFGEQG---ITADELAEAAGTISYEILTRLGPRVPRVYVG 367
PLPDE_III_AR cd00430
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ...
 8-369 2.47e-125

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: 364.90  E-value: 2.47e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   8 PTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILILG 86
Cdd:cd00430     1 RTWAEIDLDALRHNLRVIRRLLGPGtKIMAVVKADAYGHGAVEVAKALEEAGADYFAVATLEEALELREAGITAPILVLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  87 ISPFEYAELMAVQHIITTVVSLSWLKEAAQYL-SGEQRLHVSLGVDTGMGRIGFRDRQSLaEAIAYLQDNKDIfDYVGLA 165
Cdd:cd00430    81 GTPPEEAEEAIEYDLTPTVSSLEQAEALSAAAaRLGKTLKVHLKIDTGMGRLGFRPEEAE-ELLEALKALPGL-ELEGVF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 166 THFAESDSAETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHaDEVPHEVIRVGTVLYGVEPSrGELADGKNL 241
Cdd:cd00430   159 THFATADEPDKAYTRRQLERFLEALAELEEagipPPLKHLANSAAILRF-PEAHFDMVRPGIALYGLYPS-PEVKSPLGL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 242 EPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKMTG-FNVIVDGQYAPIVGQVAMDQLMIRLP 320
Cdd:cd00430   237 KPVMSLKARVVQVKTVPAGEGVSYGRTYTAPRPTRIATLPVGYADGYPRALSNkGEVLIRGKRAPIVGRVCMDQTMVDVT 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2083174352 321 --REYPDGTKVTFIGKDGDLENTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:cd00430   317 diPDVKVGDEVVLFGRQGDEEITAEELAELAGTINYEILCRISKRVPRIYV 367
alr PRK00053
alanine racemase; Reviewed
 7-369 1.02e-116

alanine racemase; Reviewed


Pssm-ID: 234600 [Multi-domain]  Cd Length: 363  Bit Score: 342.93  E-value: 1.02e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   7 RPTQIEISKKALKHNVSVVKS-VSGADKIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILIL 85
Cdd:PRK00053    2 RPATAEIDLDALRHNLRQIRKhAPPKSKLMAVVKANAYGHGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILIL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  86 -GISPFEYAELMAVQHIITTVVSLSWLKEAAQYLSGeQRLHVSLGVDTGMGRIGFRDRQsLAEAIAYLQDNKDIfDYVGL 164
Cdd:PRK00053   82 gGFFPAEDLPLIIAYNLTTAVHSLEQLEALEKAELG-KPLKVHLKIDTGMHRLGVRPEE-AEAALERLLACPNV-RLEGI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 165 ATHFAESDSAETDYFYMQLKRWHDITDGLPEPEF--YHVANSGAAMYHADeVPHEVIRVGTVLYGVEPSRGELADGKNLE 242
Cdd:PRK00053  159 FSHFATADEPDNSYTEQQLNRFEAALAGLPGKGKplRHLANSAAILRWPD-LHFDWVRPGIALYGLSPSGEPLGLDFGLK 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 243 PVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMIRLP- 320
Cdd:PRK00053  238 PAMTLKSSLIAVRELKAGEGVGYGGTFTAERDTRIAVVPIGYADGYPRNLpSGTPVLVNGRRVPIVGRVSMDQLTVDLGp 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 2083174352 321 -REYPDGTKVTFIGKDgdleNTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:PRK00053  318 dPQDKVGDEVTLWGEA----LTAEDVAEIIGTINYELLCKLSPRVPRVYV 363
alr TIGR00492
alanine racemase; This enzyme interconverts L-alanine and D-alanine. Its primary function is ...
 7-369 7.79e-101

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: 302.74  E-value: 7.79e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   7 RPTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILIL 85
Cdd:TIGR00492   1 RPATVEIDLAALKHNLSAIRNHIGPKsKIMAVVKANAYGHGLIEVAKTLLQAGADYFGVANLEEAITLRKAGITAPILLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  86 GISPFEYAELMAVQHIITTVVSLSWLKEAAQY-LSGEQRLHVSLGVDTGMGRIGFRDRQSLAEaIAYLQDNKDIFDYVGL 164
Cdd:TIGR00492  81 GGFFAEDLKILAAWDLTTTVHSVEQLQALEEAlLKEPKRLKVHLKIDTGMNRLGVKPDEAALF-VQKLRQLKKFLELEGI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 165 ATHFAESDSAETDYFYMQLKRWHDITDGLP----EPEFYHVANSGAAMYHAdEVPHEVIRVGTVLYGVEPSrGELADGK- 239
Cdd:TIGR00492 160 FSHFATADEPKTGTTQKQIERFNSFLEGLKqqniEPPFRHIANSAAILNWP-ESHFDMVRPGIILYGLYPS-ADMSDGAp 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 240 -NLEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMI 317
Cdd:TIGR00492 238 fGLKPVLSLTSKIIQVRTVKKGEPVSYGGTFTAEEDTRIGVVAIGYADGYPRALsNGTPVLVNGKRVPIVGRVCMDMIMV 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2083174352 318 RLPREYPD--GTKVTFIGKdgdlENTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:TIGR00492 318 DLGPDLQDktGDEVILWGE----EISIDEIAEMLGTIAYELICTLSKRVPRKYI 367
PLPDE_III_AR_proteobact cd06827
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Proteobacterial Alanine Racemases; ...
 8-369 3.29e-84

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: 259.74  E-value: 3.29e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   8 PTQIEISKKALKHNVSVVKSVSGADKIFLAVKSNAYGLGLIPTSKAAVEggVYGLAVAIIDEALALRHERITAPILILGi 87
Cdd:cd06827     1 PARATIDLAALRHNLRLVRELAPNSKILAVVKANAYGHGLVRVAKALAD--ADGFAVACIEEALALREAGITKPILLLE- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  88 SPFEYAEL-MAVQHIITTVV----SLSWLKEAAqylsGEQRLHVSLGVDTGMGRIGFRDRQsLAEAIAYLQDNKDIFDyV 162
Cdd:cd06827    78 GFFSADELpLAAEYNLWTVVhseeQLEWLEQAA----LSKPLNVWLKLDSGMHRLGFSPEE-YAAAYQRLKASPNVAS-I 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 163 GLATHFAESDSAETDYFYMQLKRWHDITDGLPEPefYHVANSGAAMYHaDEVPHEVIRVGTVLYGVEPSRGELADGKNLE 242
Cdd:cd06827   152 VLMTHFACADEPDSPGTAKQLAIFEQATAGLPGP--RSLANSAAILAW-PEAHGDWVRPGIMLYGASPFADKSGADLGLK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 243 PVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMIRLpR 321
Cdd:cd06827   229 PVMTLSSEIIAVRELKAGESVGYGATWTAPRPMRIGVVAIGYGDGYPRHApSGTPVLVNGQRTPLVGRVSMDMLTVDL-T 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2083174352 322 EYPD---GTKVTFIGKdgdlENTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:cd06827   308 DLPEakvGDPVELWGK----GLPVDEVAAAAGTIGYELLCRLTPRVPRVYV 354
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
13-230 5.50e-61

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 195.52  E-value: 5.50e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  13 ISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILILGISPFE 91
Cdd:pfam01168   1 IDLDALRHNLRRLRRRAGPGaKLMAVVKANAYGHGAVEVARALLEGGADGFAVATLDEALELREAGITAPILVLGGFPPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  92 YAELMAVQHIITTVVSLSWLKEAAQYLSGEQR-LHVSLGVDTGMGRIGFRDrQSLAEAIAYLQDNKDIfDYVGLATHFAE 170
Cdd:pfam01168  81 ELALAAEYDLTPTVDSLEQLEALAAAARRLGKpLRVHLKIDTGMGRLGFRP-EEALALLARLAALPGL-RLEGLMTHFAC 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2083174352 171 SDSAETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHADEVphEVIRVGTVLYGVEP 230
Cdd:pfam01168 159 ADEPDDPYTNAQLARFREAAAALEAaglrPPVVHLANSAAILLHPLHF--DMVRPGIALYGLSP 220
PLPDE_III_VanT cd06825
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, VanT and similar proteins; This ...
 11-368 2.26e-57

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: 191.03  E-value: 2.26e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  11 IEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILILGISP 89
Cdd:cd06825     4 LEIDLSALEHNVKEIKRLLPSTcKLMAVVKANAYGHGDVEVARVLEQIGIDFFAVATIDEGIRLREAGIKGEILILGYTP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  90 FEYAELMAVQHIITTVVSLSWLKEAAQYlsgEQRLHVSLGVDTGMGRIGFRDRQSlaEAIAYLQDNKDIfDYVGLATHFA 169
Cdd:cd06825    84 PVRAKELKKYSLTQTLISEAYAEELSKY---AVNIKVHLKVDTGMHRLGESPEDI--DSILAIYRLKNL-KVSGIFSHLC 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 170 ESDSAETD---YFYMQLKRWHDITDGLPEPEF----YHVANS-GAAMYhaDEVPHEVIRVGTVLYGVePSRGE--LADGK 239
Cdd:cd06825   158 VSDSLDEDdiaFTKHQIACFDQVLADLKARGIevgkIHIQSSyGILNY--PDLKYDYVRPGILLYGV-LSDPNdpTKLGL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 240 NLEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM--TGFNVIVDGQYAPIVGQVAMDQLMI 317
Cdd:cd06825   235 DLRPVLSLKAKVILVRKVAKGEAVGYGRLFVASRTTRIATVSIGYADGYPRSLsnQKAYVLINGKRAPIIGNICMDQLMV 314

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2083174352 318 RLPR--EYPDGTKVTFIGKDGDLENTLEDVAQHAGLAPWEIMTGMQGRLHRIV 368
Cdd:cd06825   315 DVTDipEVKEGDTATLIGQDGDEELSADEVARNAHTITNELLSRIGERVKRIY 367
dadX PRK03646
catabolic alanine racemase;
6-369 3.38e-57

catabolic alanine racemase;


Pssm-ID: 179622 [Multi-domain]  Cd Length: 355  Bit Score: 189.94  E-value: 3.38e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   6 TRPTQIEISKKALKHNVSVVKSVSGADKIFLAVKSNAYGLGLIPTSKAAveGGVYGLAVAIIDEALALRHERITAPILIL 85
Cdd:PRK03646    1 TRPIQASLDLQALKQNLSIVREAAPGARVWSVVKANAYGHGIERIWSAL--GATDGFAVLNLEEAITLRERGWKGPILML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  86 -GIspFEYAEL-MAVQHIITTVVSLSWLKEAAQYLSGEQRLHVSLGVDTGMGRIGFRDRQSLAeAIAYLQDNKDIFDYVg 163
Cdd:PRK03646   79 eGF--FHAQDLeLYDQHRLTTCVHSNWQLKALQNARLKAPLDIYLKVNSGMNRLGFQPERVQT-VWQQLRAMGNVGEMT- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 164 LATHFAESDsaETDYFYMQLKRWHDITDGLPEPefYHVANSGAAMYHAdEVPHEVIRVGTVLYGVEPSR--GELADgKNL 241
Cdd:PRK03646  155 LMSHFARAD--HPDGISEAMARIEQAAEGLECE--RSLSNSAATLWHP-QAHFDWVRPGIILYGASPSGqwRDIAN-TGL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 242 EPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQYAPIVGQVAMDQLMIRLP 320
Cdd:PRK03646  229 RPVMTLSSEIIGVQTLKAGERVGYGGRYTARREQRIGIVAAGYADGYPRHApTGTPVLVDGVRTRTVGTVSMDMLAVDLT 308

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2083174352 321 rEYPD---GTKVTFIGKdgdlENTLEDVAQHAGLAPWEIMTGMQGRLHRIVV 369
Cdd:PRK03646  309 -PCPQagiGTPVELWGK----EIKIDDVAAAAGTIGYELMCALALRVPVVTV 355
PRK11930 PRK11930
putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine ...
 9-367 7.87e-49

putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional


Pssm-ID: 237026 [Multi-domain]  Cd Length: 822  Bit Score: 175.92  E-value: 7.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   9 TQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILILGI 87
Cdd:PRK11930  460 TVLEINLNAIVHNLNYYRSKLKPEtKIMCMVKAFAYGSGSYEIAKLLQEHRVDYLAVAYADEGVSLRKAGITLPIMVMNP 539

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  88 SPFEYAELmaVQ-HIITTVVSLSWLKEAAQYLSGEQRLH--VSLGVDTGMGRIGFRDrQSLAEAIAYLQDNkdifDYVGL 164
Cdd:PRK11930  540 EPTSFDTI--IDyKLEPEIYSFRLLDAFIKAAQKKGITGypIHIKIDTGMHRLGFEP-EDIPELARRLKKQ----PALKV 612

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 165 A---THFAESDSAETDYFYM-QLKRW----HDITDGLPEPEFYHVANSGAAMYHADevPH-EVIRVGTVLYGVEPSrgeL 235
Cdd:PRK11930  613 RsvfSHLAGSDDPDHDDFTRqQIELFdegsEELQEALGYKPIRHILNSAGIERFPD--YQyDMVRLGIGLYGVSAS---G 687

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 236 ADGKNLEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM---TGFnVIVDGQYAPIVGQVAM 312
Cdd:PRK11930  688 AGQQALRNVSTLKTTILQIKHVPKGETVGYGRKGVVTKPSRIATIPIGYADGLNRRLgngVGY-VLVNGQKAPIVGNICM 766

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2083174352 313 DQLMIrlpreypdgtKVTFI-GKDGDL------ENTLEDVAQHAGLAPWEIMTGMQGRLHRI 367
Cdd:PRK11930  767 DMCMI----------DVTDIdAKEGDEviifgeELPVTELADALNTIPYEILTSISPRVKRV 818
PRK13340 PRK13340
alanine racemase; Reviewed
 4-370 6.90e-47

alanine racemase; Reviewed


Pssm-ID: 183984 [Multi-domain]  Cd Length: 406  Bit Score: 164.41  E-value: 6.90e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352   4 AITRPTQIEISKKALKHNVSVVKSVSGAD-KIFLAVKSNAYGLG---LIPTskaAVEGGVYGLAVAIIDEALALRHERIT 79
Cdd:PRK13340   36 IQPRNAWLEISPGAFRHNIKTLRSLLANKsKVCAVMKADAYGHGielLMPS---IIKANVPCIGIASNEEARRVRELGFT 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  80 APILIL-GISPFEYAElmAVQHIITTVV----SLSWLKEAAQYLSGEQRLHVSLGvDTGMGRIGFRDR--QSLAEAIAYL 152
Cdd:PRK13340  113 GQLLRVrSASPAEIEQ--ALRYDLEELIgddeQAKLLAAIAKKNGKPIDIHLALN-SGGMSRNGLDMStaRGKWEALRIA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 153 QD-NKDIfdyVGLATHFAESDSAETDYfymQLKRWHDITDGLP-------EPEFYHVANSGAAMYHAdEVPHEVIRVGTV 224
Cdd:PRK13340  190 TLpSLGI---VGIMTHFPNEDEDEVRW---KLAQFKEQTAWLIgeaglkrEKITLHVANSYATLNVP-EAHLDMVRPGGI 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 225 LYGVE-PSRGELadgknlEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKM-TGFNVIVDGQ 302
Cdd:PRK13340  263 LYGDRhPANTEY------KRIMTFKSRIASVNTLPKGSTVGYDRTFTLKRDSRLANLPVGYSDGYPRHAsNKAPVLINGQ 336

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2083174352 303 YAPIVGQVAMDQLMIRLPrEYPD---GTKVTFIGKDGDLENTLEDVAQHAGLAPWEIMTGMQGRLHRIVVD 370
Cdd:PRK13340  337 RAPVVGRVSMNTLMVDVT-DIPNvkpGDEVVLFGKQGNAEITVDEVEEASGTIFPELYTAWGRTNPRIYVP 406
Ala_racemase_C smart01005
Alanine racemase, C-terminal domain; Alanine racemase plays a role in providing the D-alanine ...
 244-368 3.23e-46

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: 153.76  E-value: 3.23e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  244 VMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKMTGFNVIVDGQYAPIVGQVAMDQLMIRLP--R 321
Cdd:smart01005   1 VMTLKARVIQVREVPAGETVGYGATFTADRDTRIATVPIGYADGYPRALSNGPVLINGQRVPVVGRVSMDQLMVDVTdiP 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2083174352  322 EYPDGTKVTFIGKDgdlENTLEDVAQHAGLAPWEIMTGMQGRLHRIV 368
Cdd:smart01005  81 DVKVGDEVVLFGPQ---EITADELAEAAGTISYEILTRLGPRVPRVY 124
Ala_racemase_C pfam00842
Alanine racemase, C-terminal domain;
244-368 3.53e-46

Alanine racemase, C-terminal domain;


Pssm-ID: 459960 [Multi-domain]  Cd Length: 128  Bit Score: 154.06  E-value: 3.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 244 VMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKMTGFN-VIVDGQYAPIVGQVAMDQLMIRLP-- 320
Cdd:pfam00842   1 VMTLKSRVIQVKTVPAGEGVGYGRTYTAERDTRIATVPIGYADGYPRALSNRGeVLINGKRAPIVGRVCMDQLMVDVTdv 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2083174352 321 REYPDGTKVTFIGKDGDLENTLEDVAQHAGLAPWEIMTGMQGRLHRIV 368
Cdd:pfam00842  81 PEVKVGDEVTLFGKQGDEEITADELAEAAGTINYEILCSLGKRVPRVY 128
PLPDE_III_AR2 cd06826
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ...
 11-350 4.45e-31

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: 120.91  E-value: 4.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  11 IEISKKALKHNVSVVKSVSGADKIFLAV-KSNAYGLGLIPTSKAAVEGGVYGLAVAIIDEALALRHERITAPILIL-GIS 88
Cdd:cd06826     4 LEISTGAFENNIKLLKKLLGGNTKLCAVmKADAYGHGIALVMPSIIAQNIPCVGITSNEEARVVREAGFTGKILRVrTAT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  89 PFEYAELMA--VQHIITTVVSLSWLKEAAQYLSGEQRLHVSLGvDTGMGRIG--FRDRQSLAEAIAYL-QDNKDIfdyVG 163
Cdd:cd06826    84 PSEIEDALAynIEELIGSLDQAEQIDSLAKRHGKTLPVHLALN-SGGMSRNGleLSTAQGKEDAVAIAtLPNLKI---VG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 164 LATHFAesdSAETDYFYMQLKRWHDITD------GLPEPEF-YHVANSGAAMyhadEVPH---EVIRVGTVLYGVEPSRG 233
Cdd:cd06826   160 IMTHFP---VEDEDDVRAKLARFNEDTAwlisnaKLKREKItLHAANSFATL----NVPEahlDMVRPGGILYGDTPPSP 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352 234 ELadgknlEPVMALRSEMNFVKQLPAGEGISYSHKYTTSGNEWIGTVPIGYGDGWLRKMTG-FNVIVDGQYAPIVGQVAM 312
Cdd:cd06826   233 EY------KRIMSFKSRVASLNTYPKGSTVGYDRTFTLTRDSLLANIPVGYSDGYRRSFSNkAHVLINGQRVPVVGKVSM 306

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 2083174352 313 DQLMIRLPrEYPD---GTKVTFIGKDGDLENTLEDVAQHAG 350
Cdd:cd06826   307 NTVMVDVT-DIPGvkaGDEVVLFGKQGGAEITAAEIEEGSG 346
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 18-223 2.17e-25

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme family is predominantly composed of two-domain proteins with similarity to bacterial alanine racemases (AR) including eukaryotic ornithine decarboxylases (ODC), prokaryotic diaminopimelate decarboxylases (DapDC), biosynthetic arginine decarboxylases (ADC), carboxynorspermidine decarboxylases (CANSDC), and similar proteins. AR-like proteins contain an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. They exist as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. These proteins play important roles in the biosynthesis of amino acids and polyamine. The family also includes the single-domain YBL036c-like proteins, which contain a single PLP-binding TIM-barrel domain without any N- or C-terminal extensions. Due to the lack of a second domain, these proteins may possess only limited D- to L-alanine racemase activity or non-specific racemase activity.


Pssm-ID: 143484 [Multi-domain]  Cd Length: 211  Bit Score: 102.01  E-value: 2.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  18 LKHNVSVVKSVSGAD-KIFLAVKSNAYglglIPTSKAAVEGGVyGLAVAIIDEALALRHERI-TAPILILG--ISPFEYA 93
Cdd:cd06808     1 IRHNYRRLREAAPAGiTLFAVVKANAN----PEVARTLAALGT-GFDVASLGEALLLRAAGIpPEPILFLGpcKQVSELE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2083174352  94 ELMAVQHIITTVVSLSWLKEAAQYLSGEQR-LHVSLGVDTG--MGRIGFRDRQsLAEAIAYLQDNKDIfDYVGLATHFAE 170
Cdd:cd06808    76 DAAEQGVIVVTVDSLEELEKLEEAALKAGPpARVLLRIDTGdeNGKFGVRPEE-LKALLERAKELPHL-RLVGLHTHFGS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2083174352 171 SDSaETDYFYMQLKRWHDITDGLPE----PEFYHVANSGAAMYHADE--VPHEVIRVGT 223
Cdd:cd06808   154 ADE-DYSPFVEALSRFVAALDQLGElgidLEQLSIGGSFAILYLQELplGTFIIVEPGR 211
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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