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Conserved domains on  [gi|1274916373|gb|ATS02352|]
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YggS family pyridoxal phosphate-dependent enzyme [Porphyromonas gingivalis]

Protein Classification

YggS family pyridoxal phosphate enzyme( domain architecture ID 10001087)

YggS family pyridoxal phosphate enzyme is a pyridoxal 5-phosphate (PLP)-dependent enzyme, similar to Mycobacterium tuberculosis pyridoxal phosphate homeostasis protein that is involved in PLP homeostasis

CATH:  3.20.20.10
Gene Ontology:  GO:0030170

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
1-222 5.39e-114

Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and metabolism];


:

Pssm-ID: 440094  Cd Length: 227  Bit Score: 325.07  E-value: 5.39e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373   1 MTLIAERLVPILRSL----------PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD-DVEWHFIG 69
Cdd:COG0325     1 MMSIAENLAAVRERIaaaaaragrdPEEVTLVAVSKTVPAEAIREAYAAGQRDFGENRVQEALEKIEALADlDIEWHFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  70 PLQTNKVKYIVPFISMIQSVSSLKLFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELPQVLEAVLARgsdTGVKI 149
Cdd:COG0325    81 HLQSNKVKYVAELFDLIHSVDRLKLAEELNKRAAKAGRPLDVLLQVNISGEESKSGVAPEELPALAEAIAAL---PNLRL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274916373 150 AGLMGMATFTDDREQIRREFRRLASLFREMKERFfsdsADFCELSMGMSGDFELAIEEGSTIVRIGTTIFGER 222
Cdd:COG0325   158 RGLMTIAPLTEDPEEVRPAFARLRELFDRLRAQG----PGLDELSMGMSGDYEIAIEEGATMVRVGTAIFGAR 226
 
Name Accession Description Interval E-value
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
1-222 5.39e-114

Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and metabolism];


Pssm-ID: 440094  Cd Length: 227  Bit Score: 325.07  E-value: 5.39e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373   1 MTLIAERLVPILRSL----------PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD-DVEWHFIG 69
Cdd:COG0325     1 MMSIAENLAAVRERIaaaaaragrdPEEVTLVAVSKTVPAEAIREAYAAGQRDFGENRVQEALEKIEALADlDIEWHFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  70 PLQTNKVKYIVPFISMIQSVSSLKLFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELPQVLEAVLARgsdTGVKI 149
Cdd:COG0325    81 HLQSNKVKYVAELFDLIHSVDRLKLAEELNKRAAKAGRPLDVLLQVNISGEESKSGVAPEELPALAEAIAAL---PNLRL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274916373 150 AGLMGMATFTDDREQIRREFRRLASLFREMKERFfsdsADFCELSMGMSGDFELAIEEGSTIVRIGTTIFGER 222
Cdd:COG0325   158 RGLMTIAPLTEDPEEVRPAFARLRELFDRLRAQG----PGLDELSMGMSGDYEIAIEEGATMVRVGTAIFGAR 226
PLPDE_III_YBL036c_like cd00635
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins; This family ...
4-220 4.12e-106

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins; This family contains mostly uncharacterized proteins, widely distributed among eukaryotes, bacteria and archaea, that bear similarity to the yeast hypothetical protein YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. YBL036c is a single domain monomeric protein with a typical TIM barrel fold. It binds the PLP cofactor and has been shown to exhibit amino acid racemase activity. The YBL036c structure is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. The lack of a second domain in YBL036c may explain limited D- to L-alanine racemase or non-specific racemase activity.


Pssm-ID: 143483  Cd Length: 222  Bit Score: 304.78  E-value: 4.12e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373   4 IAERLVPILRSL----------PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD-DVEWHFIGPLQ 72
Cdd:cd00635     1 IAENLEEVRERIaaaaeragrdPDEVTLVAVSKTVPAEAIREAIEAGQRDFGENRVQEALDKAEELPDpDIEWHFIGHLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  73 TNKVKYIVPFISMIQSVSSLKLFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELPQVLEAVLARGsdtGVKIAGL 152
Cdd:cd00635    81 TNKVKYAVRLFDLIHSVDSLKLAEELNKRAEKEGRVLDVLVQVNIGGEESKSGVAPEELEELLEEIAALP---NLRIRGL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274916373 153 MGMATFTDDREQIRREFRRLASLFREMKERFFsdsADFCELSMGMSGDFELAIEEGSTIVRIGTTIFG 220
Cdd:cd00635   158 MTIAPLTEDPEEVRPYFRELRELRDELGAKGG---VNLKELSMGMSGDFEIAIEEGATLVRIGTAIFG 222
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
16-222 2.76e-57

pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from Escherichia coli and YBL036C, an uncharacterized pyridoxal protein of Saccharomyces cerevisiae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129155 [Multi-domain]  Cd Length: 229  Bit Score: 181.19  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  16 PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD--DVEWHFIGPLQTNKVKYIVPFISMIQSVSSLK 93
Cdd:TIGR00044  26 PEEVKLLAVSKTKPASAIQEAYDAGQRAFGENYVQELVEKIRHLEElgLLEWHFIGPLQSNKSRLVVENFDWCHTIDSLK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  94 LFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELpqvLEAVLARGSDTGVKIAGLMGMATFTDDREQIRREFRRLA 173
Cdd:TIGR00044 106 IATKLNEQREALLPPLNVLLQINISDEESKSGIQPEEL---LELAAQLEELKHLKLRGLMTIGAPTDSYVDQEEVFRQMK 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1274916373 174 SLFREMKERFFSDSADfcELSMGMSGDFELAIEEGSTIVRIGTTIFGER 222
Cdd:TIGR00044 183 VLFAQIKQRSPHGTID--TLSMGMSDDFEEAIAAGATMVRIGTAIFGAR 229
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
11-222 4.61e-18

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 79.19  E-value: 4.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  11 ILRSLPQGVRLAAVSKF----HPVEE-LMEAYEAGQRVFAESRVQELMSKVEAMPDdVEWHFIGPLQTNKVKYIVPFiSM 85
Cdd:pfam01168  13 LRRRAGPGAKLMAVVKAnaygHGAVEvARALLEGGADGFAVATLDEALELREAGIT-APILVLGGFPPEELALAAEY-DL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  86 IQSVSSLKLFDEISRQASKVGRTVPVLLEVhiaseDT---KSGFTPEELPQVLEAVLARGsdtGVKIAGLMGMATFTDDR 162
Cdd:pfam01168  91 TPTVDSLEQLEALAAAARRLGKPLRVHLKI-----DTgmgRLGFRPEEALALLARLAALP---GLRLEGLMTHFACADEP 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274916373 163 EQ--IRREFRRlaslFREMKERFFSDSADFCELSMGMSGDFELAIEEgSTIVRIGTTIFGER 222
Cdd:pfam01168 163 DDpyTNAQLAR----FREAAAALEAAGLRPPVVHLANSAAILLHPLH-FDMVRPGIALYGLS 219
 
Name Accession Description Interval E-value
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
1-222 5.39e-114

Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and metabolism];


Pssm-ID: 440094  Cd Length: 227  Bit Score: 325.07  E-value: 5.39e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373   1 MTLIAERLVPILRSL----------PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD-DVEWHFIG 69
Cdd:COG0325     1 MMSIAENLAAVRERIaaaaaragrdPEEVTLVAVSKTVPAEAIREAYAAGQRDFGENRVQEALEKIEALADlDIEWHFIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  70 PLQTNKVKYIVPFISMIQSVSSLKLFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELPQVLEAVLARgsdTGVKI 149
Cdd:COG0325    81 HLQSNKVKYVAELFDLIHSVDRLKLAEELNKRAAKAGRPLDVLLQVNISGEESKSGVAPEELPALAEAIAAL---PNLRL 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1274916373 150 AGLMGMATFTDDREQIRREFRRLASLFREMKERFfsdsADFCELSMGMSGDFELAIEEGSTIVRIGTTIFGER 222
Cdd:COG0325   158 RGLMTIAPLTEDPEEVRPAFARLRELFDRLRAQG----PGLDELSMGMSGDYEIAIEEGATMVRVGTAIFGAR 226
PLPDE_III_YBL036c_like cd00635
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins; This family ...
4-220 4.12e-106

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins; This family contains mostly uncharacterized proteins, widely distributed among eukaryotes, bacteria and archaea, that bear similarity to the yeast hypothetical protein YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. YBL036c is a single domain monomeric protein with a typical TIM barrel fold. It binds the PLP cofactor and has been shown to exhibit amino acid racemase activity. The YBL036c structure is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. The lack of a second domain in YBL036c may explain limited D- to L-alanine racemase or non-specific racemase activity.


Pssm-ID: 143483  Cd Length: 222  Bit Score: 304.78  E-value: 4.12e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373   4 IAERLVPILRSL----------PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD-DVEWHFIGPLQ 72
Cdd:cd00635     1 IAENLEEVRERIaaaaeragrdPDEVTLVAVSKTVPAEAIREAIEAGQRDFGENRVQEALDKAEELPDpDIEWHFIGHLQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  73 TNKVKYIVPFISMIQSVSSLKLFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELPQVLEAVLARGsdtGVKIAGL 152
Cdd:cd00635    81 TNKVKYAVRLFDLIHSVDSLKLAEELNKRAEKEGRVLDVLVQVNIGGEESKSGVAPEELEELLEEIAALP---NLRIRGL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1274916373 153 MGMATFTDDREQIRREFRRLASLFREMKERFFsdsADFCELSMGMSGDFELAIEEGSTIVRIGTTIFG 220
Cdd:cd00635   158 MTIAPLTEDPEEVRPYFRELRELRDELGAKGG---VNLKELSMGMSGDFEIAIEEGATLVRIGTAIFG 222
PLPDE_III_YBL036c_euk cd06822
Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, ...
19-220 2.60e-67

Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, Eukaryotic YBL036c-like proteins; This subfamily contains mostly uncharacterized eukaryotic proteins with similarity to the yeast hypothetical protein YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. YBL036c is a single domain monomeric protein with a typical TIM barrel fold. It binds the PLP cofactor and has been shown to exhibit amino acid racemase activity. The YBL036c structure is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. The lack of a second domain in YBL036c may explain limited D- to L-alanine racemase or non-specific racemase activity. Some members of this subfamily are also referred to as PROSC (Proline synthetase co-transcribed bacterial homolog).


Pssm-ID: 143496  Cd Length: 227  Bit Score: 206.67  E-value: 2.60e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  19 VRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPDDVEWHFIGPLQTNKVKYI--VPFISMIQSVSSLKLFD 96
Cdd:cd06822    24 PRLVAVSKTKPAELIKEAYDAGQRHFGENYVQELIEKAPDLPIDIKWHFIGHLQSNKVKKLlkVPNLYMVETVDSEKLAD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  97 EISRQASKVGRTVP--VLLEVHIASEDTKSGFTPEELPQVLEAVLARGSdtGVKIAGLMGMATFTDDREQIRRE-FRRLA 173
Cdd:cd06822   104 KLNKAWEKLGEREPlkVMVQVNTSGEESKSGLEPSEAVELVKHIIEECP--NLKFSGLMTIGSFGYSLSSGPNPdFLCLV 181
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1274916373 174 SLfREMKERFFSDSADFCELSMGMSGDFELAIEEGSTIVRIGTTIFG 220
Cdd:cd06822   182 DC-RKKVCEKLGINPDDLELSMGMSADFEHAIEMGSTNVRVGSAIFG 227
PLPDE_III_Yggs_like cd06824
Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, ...
16-221 3.43e-62

Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, Yggs-like proteins; This subfamily contains mainly uncharacterized proteobacterial proteins with similarity to the hypothetical Escherichia coli protein YggS, a homolog of yeast YBL036c, which is homologous to a Pseudomonas aeruginosa gene that is co-transcribed with a known proline biosynthetic gene. Like yeast YBL036c, Yggs is a single domain monomeric protein with a typical TIM-barrel fold. Its structure, which shows a covalently-bound PLP cofactor, is similar to the N-terminal domain of the fold type III PLP-dependent enzymes, bacterial alanine racemase and eukaryotic ornithine decarboxylase, which are two-domain dimeric proteins. YggS has not been characterized extensively and its biological function is still unkonwn.


Pssm-ID: 143497  Cd Length: 224  Bit Score: 193.56  E-value: 3.43e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  16 PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD--DVEWHFIGPLQTNKVKYIVPFISMIQSVSSLK 93
Cdd:cd06824    24 PSSVQLLAVSKTKPADAIREAYAAGQRHFGENYVQEALEKIEALRDlqDIEWHFIGPIQSNKTKLIAENFDWVHSVDRLK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  94 LFDEISRQASKvgRTVP--VLLEVHIASEDTKSGFTPEELPQVLEAV--LARgsdtgVKIAGLMGMATFTDDREQIRREF 169
Cdd:cd06824   104 IAKRLNDQRPA--GLPPlnVCIQVNISGEDSKSGVAPEDAAELAEAIsqLPN-----LRLRGLMAIPAPTDDEAAQRAAF 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1274916373 170 RRLASLFREMKERFfsdsADFCELSMGMSGDFELAIEEGSTIVRIGTTIFGE 221
Cdd:cd06824   177 KRLRQLFDQLKKQY----PDLDTLSMGMSGDLEAAIAAGSTMVRIGTAIFGA 224
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
16-222 2.76e-57

pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from Escherichia coli and YBL036C, an uncharacterized pyridoxal protein of Saccharomyces cerevisiae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129155 [Multi-domain]  Cd Length: 229  Bit Score: 181.19  E-value: 2.76e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  16 PQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPD--DVEWHFIGPLQTNKVKYIVPFISMIQSVSSLK 93
Cdd:TIGR00044  26 PEEVKLLAVSKTKPASAIQEAYDAGQRAFGENYVQELVEKIRHLEElgLLEWHFIGPLQSNKSRLVVENFDWCHTIDSLK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  94 LFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELpqvLEAVLARGSDTGVKIAGLMGMATFTDDREQIRREFRRLA 173
Cdd:TIGR00044 106 IATKLNEQREALLPPLNVLLQINISDEESKSGIQPEEL---LELAAQLEELKHLKLRGLMTIGAPTDSYVDQEEVFRQMK 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1274916373 174 SLFREMKERFFSDSADfcELSMGMSGDFELAIEEGSTIVRIGTTIFGER 222
Cdd:TIGR00044 183 VLFAQIKQRSPHGTID--TLSMGMSDDFEEAIAAGATMVRIGTAIFGAR 229
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
15-216 9.54e-22

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: 88.92  E-value: 9.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  15 LPQGVRLAAVSKFHPVEELMEAYEAGQRVFAESRVQELMSKVEAMPDDVEWHFIGPL-QTNKVKYIV--PFISMIqsVSS 91
Cdd:cd06808    12 APAGITLFAVVKANANPEVARTLAALGTGFDVASLGEALLLRAAGIPPEPILFLGPCkQVSELEDAAeqGVIVVT--VDS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  92 LKLFDEISRQASKVGRTVPVLLEVHIASEDTKSGFTPEELPQVLEAVLARGsdtGVKIAGLMG-MATFTDDREQIRREFR 170
Cdd:cd06808    90 LEELEKLEEAALKAGPPARVLLRIDTGDENGKFGVRPEELKALLERAKELP---HLRLVGLHThFGSADEDYSPFVEALS 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1274916373 171 RLASLFREMKERFFsdsaDFCELSMGMSGDFELAIEE---GSTIVRIGT 216
Cdd:cd06808   167 RFVAALDQLGELGI----DLEQLSIGGSFAILYLQELplgTFIIVEPGR 211
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
11-222 4.61e-18

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 79.19  E-value: 4.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  11 ILRSLPQGVRLAAVSKF----HPVEE-LMEAYEAGQRVFAESRVQELMSKVEAMPDdVEWHFIGPLQTNKVKYIVPFiSM 85
Cdd:pfam01168  13 LRRRAGPGAKLMAVVKAnaygHGAVEvARALLEGGADGFAVATLDEALELREAGIT-APILVLGGFPPEELALAAEY-DL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  86 IQSVSSLKLFDEISRQASKVGRTVPVLLEVhiaseDT---KSGFTPEELPQVLEAVLARGsdtGVKIAGLMGMATFTDDR 162
Cdd:pfam01168  91 TPTVDSLEQLEALAAAARRLGKPLRVHLKI-----DTgmgRLGFRPEEALALLARLAALP---GLRLEGLMTHFACADEP 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274916373 163 EQ--IRREFRRlaslFREMKERFFSDSADFCELSMGMSGDFELAIEEgSTIVRIGTTIFGER 222
Cdd:pfam01168 163 DDpyTNAQLAR----FREAAAALEAAGLRPPVVHLANSAAILLHPLH-FDMVRPGIALYGLS 219
PLPDE_III_AR cd00430
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ...
85-220 3.53e-06

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: 46.72  E-value: 3.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  85 MIQSVSSLKLFDEISRQASKVGRTVPVLLEVhiaseDT---KSGFTPEELPQVLEAVLARGsdtGVKIAGLM------GM 155
Cdd:cd00430    95 LTPTVSSLEQAEALSAAAARLGKTLKVHLKI-----DTgmgRLGFRPEEAEELLEALKALP---GLELEGVFthfataDE 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1274916373 156 ATFTDDREQIRReFRRLASLFREMKERF----FSDSA---DFCELSMGMsgdfelaieegstiVRIGTTIFG 220
Cdd:cd00430   167 PDKAYTRRQLER-FLEALAELEEAGIPPplkhLANSAailRFPEAHFDM--------------VRPGIALYG 223
Alr COG0787
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ...
86-178 4.59e-06

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: 46.64  E-value: 4.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  86 IQSVSSLKLFDEISRQASKVGRTVPVLLEVhiaseDT---KSGFTPEELPQVLEAVLARGsdtGVKIAGLMG-MAT---- 157
Cdd:COG0787    98 EPVVHSLEQLEALAAAARRLGKPLPVHLKV-----DTgmnRLGFRPEEAPALAARLAALP---GLEVEGIMShFACadep 169
                          90       100
                  ....*....|....*....|....
gi 1274916373 158 ---FTddREQIRReFRRLASLFRE 178
Cdd:COG0787   170 dhpFT--AEQLER-FEEAVAALPA 190
PLPDE_III_yhfX_like cd06811
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the ...
73-152 2.43e-05

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme yhfX; This subfamily is composed of the uncharacterized protein yhfX from Escherichia coli K-12 and similar bacterial proteins. These proteins are homologous 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: 143486  Cd Length: 382  Bit Score: 44.19  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1274916373  73 TNKVKYIVPFISMIQSVSSLKLFDEISRQASKVGRTVPVLLEVhIASEDT-----KSGFTPEELPQVLEAVLARGsdtGV 147
Cdd:cd06811   110 RHQVPAVLAMRPEVITVYSLEKAREISDAAVELGRVQDVLLRV-YGDEDTlypgqEGGFPLEELPAVLAAIKALP---GI 185

                  ....*
gi 1274916373 148 KIAGL 152
Cdd:cd06811   186 RIAGL 190
 
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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