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Conserved domains on  [gi|616686459|gb|KAE84122|]
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hypothetical protein W632_02100 [Staphylococcus aureus VET0402R]

Protein Classification

alanine/ornithine racemase family PLP-dependent enzyme( domain architecture ID 10160088)

alanine/ornithine racemase family PLP-dependent enzyme similar to Acetoanaerobium sticklandii ornithine racemase (OR), which catalyzes the conversion of L-ornithine to D-ornithine, and could also racemize basic amino acids such as lysine and arginine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLPDE_III_AR_like_1 cd06815
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ...
1-333 2.34e-160

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: 452.77  E-value: 2.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTVFQSKNMQFTPVIKCIAGDRTIVESLKALGINHVAESRLDNIISIADQDL--TYTLLRTP 78
Cdd:cd06815    1 YPRLEINLSKIRHNAKVLVELCKSRGIEVTGVTKVVCGDPEIAEALLEGGITHLADSRIENLKKLKDLGIsgPKMLLRIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  79 AKKEISDMIEKVDMSIQTELSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFM 158
Cdd:cd06815   81 MLSEVEDVVKYADISLNSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDLLDFVEEILKLPGIELVGIGTNLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 159 CFKSDAPSDDDIFMINRFVSAVEREIGYRLKIISGGNSSMLPQLLYNDL-GKINELRIGETLFRGVDTTTNQAIAMLYQD 237
Cdd:cd06815  161 CYGGVLPTEENMGKLVELKEEIEKEFGIKLPIISGGNSASLPLLLKGELpGGINQLRIGEAILLGRETTYNEPIPGLYQD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 238 AITLEAEILEIKPRVNTQTHESFI----------------QAIVDIGYLDTKVDNISPMDQHINILGASSDHLMLDLNGQ 301
Cdd:cd06815  241 AFTLEAEIIEIKEKPSVPIGEIGLdafgnkpefedrgirkRAILAIGRQDVDPDGLTPVDNGIEILGASSDHLILDITDS 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 616686459 302 G-HYQVGDHISFSLNYEALSHSMYMKNLHKVYI 333
Cdd:cd06815  321 DrDYKVGDEIRFNLDYGALLRAMTSPYVEKVYI 353
 
Name Accession Description Interval E-value
PLPDE_III_AR_like_1 cd06815
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ...
1-333 2.34e-160

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: 452.77  E-value: 2.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTVFQSKNMQFTPVIKCIAGDRTIVESLKALGINHVAESRLDNIISIADQDL--TYTLLRTP 78
Cdd:cd06815    1 YPRLEINLSKIRHNAKVLVELCKSRGIEVTGVTKVVCGDPEIAEALLEGGITHLADSRIENLKKLKDLGIsgPKMLLRIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  79 AKKEISDMIEKVDMSIQTELSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFM 158
Cdd:cd06815   81 MLSEVEDVVKYADISLNSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDLLDFVEEILKLPGIELVGIGTNLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 159 CFKSDAPSDDDIFMINRFVSAVEREIGYRLKIISGGNSSMLPQLLYNDL-GKINELRIGETLFRGVDTTTNQAIAMLYQD 237
Cdd:cd06815  161 CYGGVLPTEENMGKLVELKEEIEKEFGIKLPIISGGNSASLPLLLKGELpGGINQLRIGEAILLGRETTYNEPIPGLYQD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 238 AITLEAEILEIKPRVNTQTHESFI----------------QAIVDIGYLDTKVDNISPMDQHINILGASSDHLMLDLNGQ 301
Cdd:cd06815  241 AFTLEAEIIEIKEKPSVPIGEIGLdafgnkpefedrgirkRAILAIGRQDVDPDGLTPVDNGIEILGASSDHLILDITDS 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 616686459 302 G-HYQVGDHISFSLNYEALSHSMYMKNLHKVYI 333
Cdd:cd06815  321 DrDYKVGDEIRFNLDYGALLRAMTSPYVEKVYI 353
YhfX COG3457
Predicted amino acid racemase [Amino acid transport and metabolism];
1-334 3.81e-92

Predicted amino acid racemase [Amino acid transport and metabolism];


Pssm-ID: 442680 [Multi-domain]  Cd Length: 356  Bit Score: 279.38  E-value: 3.81e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTVFQSKNMQFTPVIKCIAGDRTIVESLKALGINHVAESRLDNIISIADQ--DLTYTLLRTP 78
Cdd:COG3457    3 PPTLVIDLDKIRENARRLVELAAKHGIELYGVTKQFGGNPEIAKALLDGGIKGIVDSRIKNLKKLKRAgiPHPGHLLRIP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  79 AKKEISDMIEKVDMSIQTELSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFM 158
Cdd:COG3457   83 MLSEVEEVVRYADISLNSELETARALSEAAKKQGKVHKVILMVDLGDLREGGFPEELVDTVEEILKLPGIELAGLGTNLP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 159 CFKSDAPSDDDIFMINRFVSAVEREIGYRLKIISGGNSSMLPQLLYNDLGK-INELRIGETLFRGVDTTTNQAIAMLYQD 237
Cdd:COG3457  163 CFGGVLPTEENLGTLLELAELLEAKFGIKLPIVSGGNSTSLPLLAEGTLPKgINHLRPGEALLLGTDPLNARPIPGLEQD 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 238 AITLEAEILEI--KPRVNTQTHE--------SFI------QAIVDIGYLDTKVDNISPMDQHINILGASSDHLMLDLNG- 300
Cdd:COG3457  243 AFVLVAEIIELkeKPSVPIGEIGrdafgnapEFGdrgirkRAILAIGRQDVDPEGLTPIDYGIEILGASSDHLILDVTDs 322
                        330       340       350
                 ....*....|....*....|....*....|....
gi 616686459 301 QGHYQVGDHISFSLNYEALSHSMYMKNLHKVYID 334
Cdd:COG3457  323 KEDYKVGDTVVFCLRYQAFLTRSTSAYVEKIYSG 356
racem_Orr NF040742
ornithine racemase Orr; This type of ornithine racemase occurs in an operon for anaerobic ...
3-332 9.45e-80

ornithine racemase Orr; This type of ornithine racemase occurs in an operon for anaerobic oxidative degradation of L-ornithine as occurs in strict anaerobes such as Clostridium sticklandii. The enzyme from C. sticklandii was shown to act on the basic amino acids ornithine, lysine, and arginine. Additional close homologs, outside the family defined by this HMM, likely have similar activity profiles, but occur in different genomic contexts and would not receive the gene symbol orr.


Pssm-ID: 468706  Cd Length: 351  Bit Score: 247.51  E-value: 9.45e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   3 HVNINISKIKYNAKVLQTVFQSKNMQFTPVIKCIAGDRTIVESLKALGINHVAESRLDNIISIADQDLTYTLLRTPAKKE 82
Cdd:NF040742   3 RIEIDLNKLRHNTKTIVDLCKKKGIEVAGVTKVFCADPEIVQALVEGGVDYLADSRIENLKKLKDINLPKMLLRIPMISE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  83 ISDMIEKVDMSIQTELSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYD-VLDYIKEIIHLKNIHFVGLAFNFMCFK 161
Cdd:NF040742  83 VEEVVKYADISLNSELETIKLLSKEAKKQGKIHKIILMIDLGDLREGIFYEDeILDTVKEILKLKNIKLVGIGTNLTCYG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 162 SDAPSDDDIFMINRFVSAVEREIGYRLKIISGGNSSMLPQLLYNDLGK-INELRIGETLFRGVDTTTNQAIAMLYQDAIT 240
Cdd:NF040742 163 GVIPSEENLGKLVEIAEKIENKFNIKLEIISGGNSSSLYLIENGEMPKgINNLRLGESILLGRETAYGERIEGTHQDVFK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 241 LEAEILEIKPR----VNTQTHESFIQ------------AIVDIGYLDTKVDNISPMDQHINILGASSDHLMLDL-NGQGH 303
Cdd:NF040742 243 LVAEIIELKEKpsvpIGEIGVDAFGNkpvfedkgimkrAILAIGRQDIDPDSLTPVDSKIEILGASSDHLILDVtDSNKD 322
                        330       340
                 ....*....|....*....|....*....
gi 616686459 304 YQVGDHISFSLNYEALSHSMYMKNLHKVY 332
Cdd:NF040742 323 YKVGDKIEFNLDYGGLLSAMTSEYVKKVY 351
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
6-220 2.66e-23

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 96.14  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459    6 INISKIKYNAKVLQTVFQsKNMQFTPVIKCIA---GDRTIVESLKALGINHVAESRLDNIISI--ADQDLTYTLLRTPAK 80
Cdd:pfam01168   1 IDLDALRHNLRRLRRRAG-PGAKLMAVVKANAyghGAVEVARALLEGGADGFAVATLDEALELreAGITAPILVLGGFPP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   81 KEISDMIEK-VDMSIQTeLSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFMC 159
Cdd:pfam01168  80 EELALAAEYdLTPTVDS-LEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFAC 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616686459  160 fkSDAPSDDDIFM-INRFVSAVE--REIGYRLKIISGGNSSMLpqLLYNDLgkINELRIGETLF 220
Cdd:pfam01168 159 --ADEPDDPYTNAqLARFREAAAalEAAGLRPPVVHLANSAAI--LLHPLH--FDMVRPGIALY 216
alr PRK00053
alanine racemase; Reviewed
1-308 4.44e-05

alanine racemase; Reviewed


Pssm-ID: 234600 [Multi-domain]  Cd Length: 363  Bit Score: 44.78  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTvFQSKNMQFTPVIKCIA---GDRTIVESLKALGINHVAESRLDNIISIADQDLTYTLL-- 75
Cdd:PRK00053   3 PATAEIDLDALRHNLRQIRK-HAPPKSKLMAVVKANAyghGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILil 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  76 -RTPAKKEISDMIEKvdmSIQTelsTIHHINEVAEV----LGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHF 150
Cdd:PRK00053  82 gGFFPAEDLPLIIAY---NLTT---AVHSLEQLEALekaeLGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 151 VGLAFNFMCfkSDAPSDDDIFM-INRFVSAVEREIGYRLKIISGGNSS--MLPQLLYNDLgkineLRIGETLFrGVDTTT 227
Cdd:PRK00053 156 EGIFSHFAT--ADEPDNSYTEQqLNRFEAALAGLPGKGKPLRHLANSAaiLRWPDLHFDW-----VRPGIALY-GLSPSG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 228 NQAIA-MLYQDAITLEAEILEIKP----------RVNTQTHESFIqAIVDIGYLD---------TKVdnispmdqHIN-- 285
Cdd:PRK00053 228 EPLGLdFGLKPAMTLKSSLIAVRElkagegvgygGTFTAERDTRI-AVVPIGYADgyprnlpsgTPV--------LVNgr 298
                        330       340
                 ....*....|....*....|....*..
gi 616686459 286 ---ILGA-SSDHLMLDLNGQGHYQVGD 308
Cdd:PRK00053 299 rvpIVGRvSMDQLTVDLGPDPQDKVGD 325
 
Name Accession Description Interval E-value
PLPDE_III_AR_like_1 cd06815
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase-like 1; This subfamily ...
1-333 2.34e-160

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: 452.77  E-value: 2.34e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTVFQSKNMQFTPVIKCIAGDRTIVESLKALGINHVAESRLDNIISIADQDL--TYTLLRTP 78
Cdd:cd06815    1 YPRLEINLSKIRHNAKVLVELCKSRGIEVTGVTKVVCGDPEIAEALLEGGITHLADSRIENLKKLKDLGIsgPKMLLRIP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  79 AKKEISDMIEKVDMSIQTELSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFM 158
Cdd:cd06815   81 MLSEVEDVVKYADISLNSELETIKALSEEAKKQGKIHKIILMVDLGDLREGVLPEDLLDFVEEILKLPGIELVGIGTNLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 159 CFKSDAPSDDDIFMINRFVSAVEREIGYRLKIISGGNSSMLPQLLYNDL-GKINELRIGETLFRGVDTTTNQAIAMLYQD 237
Cdd:cd06815  161 CYGGVLPTEENMGKLVELKEEIEKEFGIKLPIISGGNSASLPLLLKGELpGGINQLRIGEAILLGRETTYNEPIPGLYQD 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 238 AITLEAEILEIKPRVNTQTHESFI----------------QAIVDIGYLDTKVDNISPMDQHINILGASSDHLMLDLNGQ 301
Cdd:cd06815  241 AFTLEAEIIEIKEKPSVPIGEIGLdafgnkpefedrgirkRAILAIGRQDVDPDGLTPVDNGIEILGASSDHLILDITDS 320
                        330       340       350
                 ....*....|....*....|....*....|...
gi 616686459 302 G-HYQVGDHISFSLNYEALSHSMYMKNLHKVYI 333
Cdd:cd06815  321 DrDYKVGDEIRFNLDYGALLRAMTSPYVEKVYI 353
YhfX COG3457
Predicted amino acid racemase [Amino acid transport and metabolism];
1-334 3.81e-92

Predicted amino acid racemase [Amino acid transport and metabolism];


Pssm-ID: 442680 [Multi-domain]  Cd Length: 356  Bit Score: 279.38  E-value: 3.81e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTVFQSKNMQFTPVIKCIAGDRTIVESLKALGINHVAESRLDNIISIADQ--DLTYTLLRTP 78
Cdd:COG3457    3 PPTLVIDLDKIRENARRLVELAAKHGIELYGVTKQFGGNPEIAKALLDGGIKGIVDSRIKNLKKLKRAgiPHPGHLLRIP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  79 AKKEISDMIEKVDMSIQTELSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFM 158
Cdd:COG3457   83 MLSEVEEVVRYADISLNSELETARALSEAAKKQGKVHKVILMVDLGDLREGGFPEELVDTVEEILKLPGIELAGLGTNLP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 159 CFKSDAPSDDDIFMINRFVSAVEREIGYRLKIISGGNSSMLPQLLYNDLGK-INELRIGETLFRGVDTTTNQAIAMLYQD 237
Cdd:COG3457  163 CFGGVLPTEENLGTLLELAELLEAKFGIKLPIVSGGNSTSLPLLAEGTLPKgINHLRPGEALLLGTDPLNARPIPGLEQD 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 238 AITLEAEILEI--KPRVNTQTHE--------SFI------QAIVDIGYLDTKVDNISPMDQHINILGASSDHLMLDLNG- 300
Cdd:COG3457  243 AFVLVAEIIELkeKPSVPIGEIGrdafgnapEFGdrgirkRAILAIGRQDVDPEGLTPIDYGIEILGASSDHLILDVTDs 322
                        330       340       350
                 ....*....|....*....|....*....|....
gi 616686459 301 QGHYQVGDHISFSLNYEALSHSMYMKNLHKVYID 334
Cdd:COG3457  323 KEDYKVGDTVVFCLRYQAFLTRSTSAYVEKIYSG 356
racem_Orr NF040742
ornithine racemase Orr; This type of ornithine racemase occurs in an operon for anaerobic ...
3-332 9.45e-80

ornithine racemase Orr; This type of ornithine racemase occurs in an operon for anaerobic oxidative degradation of L-ornithine as occurs in strict anaerobes such as Clostridium sticklandii. The enzyme from C. sticklandii was shown to act on the basic amino acids ornithine, lysine, and arginine. Additional close homologs, outside the family defined by this HMM, likely have similar activity profiles, but occur in different genomic contexts and would not receive the gene symbol orr.


Pssm-ID: 468706  Cd Length: 351  Bit Score: 247.51  E-value: 9.45e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   3 HVNINISKIKYNAKVLQTVFQSKNMQFTPVIKCIAGDRTIVESLKALGINHVAESRLDNIISIADQDLTYTLLRTPAKKE 82
Cdd:NF040742   3 RIEIDLNKLRHNTKTIVDLCKKKGIEVAGVTKVFCADPEIVQALVEGGVDYLADSRIENLKKLKDINLPKMLLRIPMISE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  83 ISDMIEKVDMSIQTELSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYD-VLDYIKEIIHLKNIHFVGLAFNFMCFK 161
Cdd:NF040742  83 VEEVVKYADISLNSELETIKLLSKEAKKQGKIHKIILMIDLGDLREGIFYEDeILDTVKEILKLKNIKLVGIGTNLTCYG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 162 SDAPSDDDIFMINRFVSAVEREIGYRLKIISGGNSSMLPQLLYNDLGK-INELRIGETLFRGVDTTTNQAIAMLYQDAIT 240
Cdd:NF040742 163 GVIPSEENLGKLVEIAEKIENKFNIKLEIISGGNSSSLYLIENGEMPKgINNLRLGESILLGRETAYGERIEGTHQDVFK 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 241 LEAEILEIKPR----VNTQTHESFIQ------------AIVDIGYLDTKVDNISPMDQHINILGASSDHLMLDL-NGQGH 303
Cdd:NF040742 243 LVAEIIELKEKpsvpIGEIGVDAFGNkpvfedkgimkrAILAIGRQDIDPDSLTPVDSKIEILGASSDHLILDVtDSNKD 322
                        330       340
                 ....*....|....*....|....*....
gi 616686459 304 YQVGDHISFSLNYEALSHSMYMKNLHKVY 332
Cdd:NF040742 323 YKVGDKIEFNLDYGGLLSAMTSEYVKKVY 351
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
6-220 2.66e-23

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 96.14  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459    6 INISKIKYNAKVLQTVFQsKNMQFTPVIKCIA---GDRTIVESLKALGINHVAESRLDNIISI--ADQDLTYTLLRTPAK 80
Cdd:pfam01168   1 IDLDALRHNLRRLRRRAG-PGAKLMAVVKANAyghGAVEVARALLEGGADGFAVATLDEALELreAGITAPILVLGGFPP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   81 KEISDMIEK-VDMSIQTeLSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFMC 159
Cdd:pfam01168  80 EELALAAEYdLTPTVDS-LEQLEALAAAARRLGKPLRVHLKIDTGMGRLGFRPEEALALLARLAALPGLRLEGLMTHFAC 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616686459  160 fkSDAPSDDDIFM-INRFVSAVE--REIGYRLKIISGGNSSMLpqLLYNDLgkINELRIGETLF 220
Cdd:pfam01168 159 --ADEPDDPYTNAqLARFREAAAalEAAGLRPPVVHLANSAAI--LLHPLH--FDMVRPGIALY 216
PLPDE_III_AR cd00430
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ...
1-308 3.42e-09

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: 57.51  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTVFqSKNMQFTPVIKCIA---GDRTIVESLKALGINHVAESRLDNIISIADQDLTYT--LL 75
Cdd:cd00430    1 RTWAEIDLDALRHNLRVIRRLL-GPGTKIMAVVKADAyghGAVEVAKALEEAGADYFAVATLEEALELREAGITAPilVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  76 RTPAKKEISDMIEK-VDMSIQTeLSTIHHINEVAEVLGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHFVGLA 154
Cdd:cd00430   80 GGTPPEEAEEAIEYdLTPTVSS-LEQAEALSAAAARLGKTLKVHLKIDTGMGRLGFRPEEAEELLEALKALPGLELEGVF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 155 FNFMCfkSDAPSDDDIFM-INRFVSAVE--REIGYRLKIISGGNSS---MLPQLLYnDLgkineLRIGETLFrGVDTTTN 228
Cdd:cd00430  159 THFAT--ADEPDKAYTRRqLERFLEALAelEEAGIPPPLKHLANSAailRFPEAHF-DM-----VRPGIALY-GLYPSPE 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 229 QAIAMLYQDAITLEAEILEIKP----------RVNTQTHESFIqAIVDIGYLD---------TKVdniSPMDQHINILGA 289
Cdd:cd00430  230 VKSPLGLKPVMSLKARVVQVKTvpagegvsygRTYTAPRPTRI-ATLPVGYADgypralsnkGEV---LIRGKRAPIVGR 305
                        330       340
                 ....*....|....*....|
gi 616686459 290 SS-DHLMLDLNGQGHYQVGD 308
Cdd:cd00430  306 VCmDQTMVDVTDIPDVKVGD 325
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
11-216 4.09e-09

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: 55.79  E-value: 4.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  11 IKYNAKVLQTVFqSKNMQFTPVIKC---IAGDRTIVESLKALGINHVAESRLDNIISIADQDLTYtLLRTPAKKEISDMI 87
Cdd:cd06808    1 IRHNYRRLREAA-PAGITLFAVVKAnanPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILF-LGPCKQVSELEDAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  88 EKVDMSIQTE-LSTIHHINEVAEVLGKKHKILLMVD--WKDGREGVLTYDVLDYIKEIIHLKNIHFVGLAFNFMCfksdA 164
Cdd:cd06808   79 EQGVIVVTVDsLEELEKLEEAALKAGPPARVLLRIDtgDENGKFGVRPEELKALLERAKELPHLRLVGLHTHFGS----A 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 616686459 165 PSDDDIFM--INRFVSAVE--REIGYRLKIISGGNSSMLPQLLYNDLGKINELRIG 216
Cdd:cd06808  155 DEDYSPFVeaLSRFVAALDqlGELGIDLEQLSIGGSFAILYLQELPLGTFIIVEPG 210
alr PRK00053
alanine racemase; Reviewed
1-308 4.44e-05

alanine racemase; Reviewed


Pssm-ID: 234600 [Multi-domain]  Cd Length: 363  Bit Score: 44.78  E-value: 4.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459   1 MAHVNINISKIKYNAKVLQTvFQSKNMQFTPVIKCIA---GDRTIVESLKALGINHVAESRLDNIISIADQDLTYTLL-- 75
Cdd:PRK00053   3 PATAEIDLDALRHNLRQIRK-HAPPKSKLMAVVKANAyghGAVEVAKTLLEAGADGFGVATLEEALELREAGITAPILil 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459  76 -RTPAKKEISDMIEKvdmSIQTelsTIHHINEVAEV----LGKKHKILLMVDWKDGREGVLTYDVLDYIKEIIHLKNIHF 150
Cdd:PRK00053  82 gGFFPAEDLPLIIAY---NLTT---AVHSLEQLEALekaeLGKPLKVHLKIDTGMHRLGVRPEEAEAALERLLACPNVRL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 151 VGLAFNFMCfkSDAPSDDDIFM-INRFVSAVEREIGYRLKIISGGNSS--MLPQLLYNDLgkineLRIGETLFrGVDTTT 227
Cdd:PRK00053 156 EGIFSHFAT--ADEPDNSYTEQqLNRFEAALAGLPGKGKPLRHLANSAaiLRWPDLHFDW-----VRPGIALY-GLSPSG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616686459 228 NQAIA-MLYQDAITLEAEILEIKP----------RVNTQTHESFIqAIVDIGYLD---------TKVdnispmdqHIN-- 285
Cdd:PRK00053 228 EPLGLdFGLKPAMTLKSSLIAVRElkagegvgygGTFTAERDTRI-AVVPIGYADgyprnlpsgTPV--------LVNgr 298
                        330       340
                 ....*....|....*....|....*..
gi 616686459 286 ---ILGA-SSDHLMLDLNGQGHYQVGD 308
Cdd:PRK00053 299 rvpIVGRvSMDQLTVDLGPDPQDKVGD 325
 
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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