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Conserved domains on  [gi|568953808|ref|XP_006509045|]
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pyridoxal phosphate homeostasis protein isoform X2 [Mus musculus]

Protein Classification

YggS family pyridoxal phosphate enzyme( domain architecture ID 10160097)

YggS family pyridoxal phosphate enzyme is a pyridoxal 5-phosphate (PLP)-dependent enzyme; similar to human pyridoxal phosphate homeostasis protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'-phosphate (PLP), the active form of vitamin B6

Gene Ontology:  GO:0030170

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III_YBL036c_euk cd06822
Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, ...
 50-252 3.15e-132

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: 373.46  E-value: 3.15e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  50 DLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScpEIKWHFIGHLQKQNVNKLMAVPNLSMLET 120
Cdd:cd06822   18 KLPASKPRLVAVSKTKPAELIKEAYDAGQRHFGENYVqeliekapdLPI--DIKWHFIGHLQSNKVKKLLKVPNLYMVET 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 121 VDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGSFGHDLSQGPNP 200
Cdd:cd06822   96 VDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESKSGLEPSEAVELVKHIIEECPNLKFSGLMTIGSFGYSLSSGPNP 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568953808 201 DFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFG 252
Cdd:cd06822  176 DFLCLVDCRKKVCEKLGINPDDLELSMGMSADFEHAIEMGSTNVRVGSAIFG 227
 
Name Accession Description Interval E-value
PLPDE_III_YBL036c_euk cd06822
Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, ...
 50-252 3.15e-132

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: 373.46  E-value: 3.15e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  50 DLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScpEIKWHFIGHLQKQNVNKLMAVPNLSMLET 120
Cdd:cd06822   18 KLPASKPRLVAVSKTKPAELIKEAYDAGQRHFGENYVqeliekapdLPI--DIKWHFIGHLQSNKVKKLLKVPNLYMVET 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 121 VDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGSFGHDLSQGPNP 200
Cdd:cd06822   96 VDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESKSGLEPSEAVELVKHIIEECPNLKFSGLMTIGSFGYSLSSGPNP 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568953808 201 DFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFG 252
Cdd:cd06822  176 DFLCLVDCRKKVCEKLGINPDDLELSMGMSADFEHAIEMGSTNVRVGSAIFG 227
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
 57-255 4.67e-75

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


Pssm-ID: 440094  Cd Length: 227  Bit Score: 228.39  E-value: 4.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  57 RLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPeIKWHFIGHLQKqnvNKL-MAVPNLSMLETVDSVKL 126
Cdd:COG0325   30 TLVAVSKTVPAEAIREAYAAGQRDFGENRVqealekieaLADLD-IEWHFIGHLQS---NKVkYVAELFDLIHSVDRLKL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 127 ADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQgPNPDFQRLL 206
Cdd:COG0325  106 AEELNKRAAKAGR--PLDVLLQVNISGEESKSGVAPEELPALAEAIAA-LPNLRLRGLMTIAPLTEDPEE-VRPAFARLR 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568953808 207 TLRRELcEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFGERD 255
Cdd:COG0325  182 ELFDRL-RAQGPGLD--ELSMGMSGDYEIAIEEGATMVRVGTAIFGARP 227
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
 57-254 4.81e-52

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: 169.64  E-value: 4.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808   57 RLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPEIKWHFIGHLQKqNVNKLMaVPNLSMLETVDSVKLA 127
Cdd:TIGR00044  30 KLLAVSKTKPASAIQEAYDAGQRAFGENYVqelvekirhLEELGLLEWHFIGPLQS-NKSRLV-VENFDWCHTIDSLKIA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  128 DKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSfghdlsqgPNPDFQRLLT 207
Cdd:TIGR00044 108 TKLNEQREALLP--PLNVLLQINISDEESKSGIQPEELLELAAQL-EELKHLKLRGLMTIGA--------PTDSYVDQEE 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568953808  208 LRRELCE-----KLGIPVEQV-ELSMGMSMDFQHAIEVGSTNVRIGSTIFGER 254
Cdd:TIGR00044 177 VFRQMKVlfaqiKQRSPHGTIdTLSMGMSDDFEEAIAAGATMVRIGTAIFGAR 229
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
57-255 3.92e-15

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 72.64  E-value: 3.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808   57 RLVAVSKtkpADmvieAYGHG------------QRTFGENYI-----L-SSCPEIKWHFIGHLQKQNVnKLMAVPNLSMl 118
Cdd:pfam01168  22 KLMAVVK---AN----AYGHGavevaralleggADGFAVATLdealeLrEAGITAPILVLGGFPPEEL-ALAAEYDLTP- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  119 eTVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGedSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQGP 198
Cdd:pfam01168  93 -TVDSLEQLEALAAAARRLGK--PLRVHLKIDTGM--GRLGFRPEEALALLARLAA-LPGLRLEGLMTHFACADEPDDPY 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953808  199 NP-DFQRLLTLRRELcEKLGIPVEqvELSMGMSmdfqHAIEVGSTN---VRIGSTIFGERD 255
Cdd:pfam01168 167 TNaQLARFREAAAAL-EAAGLRPP--VVHLANS----AAILLHPLHfdmVRPGIALYGLSP 220
 
Name Accession Description Interval E-value
PLPDE_III_YBL036c_euk cd06822
Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, ...
 50-252 3.15e-132

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: 373.46  E-value: 3.15e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  50 DLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScpEIKWHFIGHLQKQNVNKLMAVPNLSMLET 120
Cdd:cd06822   18 KLPASKPRLVAVSKTKPAELIKEAYDAGQRHFGENYVqeliekapdLPI--DIKWHFIGHLQSNKVKKLLKVPNLYMVET 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 121 VDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGSFGHDLSQGPNP 200
Cdd:cd06822   96 VDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESKSGLEPSEAVELVKHIIEECPNLKFSGLMTIGSFGYSLSSGPNP 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568953808 201 DFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFG 252
Cdd:cd06822  176 DFLCLVDCRKKVCEKLGINPDDLELSMGMSADFEHAIEMGSTNVRVGSAIFG 227
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
 57-255 4.67e-75

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


Pssm-ID: 440094  Cd Length: 227  Bit Score: 228.39  E-value: 4.67e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  57 RLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPeIKWHFIGHLQKqnvNKL-MAVPNLSMLETVDSVKL 126
Cdd:COG0325   30 TLVAVSKTVPAEAIREAYAAGQRDFGENRVqealekieaLADLD-IEWHFIGHLQS---NKVkYVAELFDLIHSVDRLKL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 127 ADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQgPNPDFQRLL 206
Cdd:COG0325  106 AEELNKRAAKAGR--PLDVLLQVNISGEESKSGVAPEELPALAEAIAA-LPNLRLRGLMTIAPLTEDPEE-VRPAFARLR 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 568953808 207 TLRRELcEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFGERD 255
Cdd:COG0325  182 ELFDRL-RAQGPGLD--ELSMGMSGDYEIAIEEGATMVRVGTAIFGARP 227
PLPDE_III_YBL036c_like cd00635
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins; This family ...
 56-252 4.98e-74

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: 225.43  E-value: 4.98e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  56 PRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScPEIKWHFIGHLQKqnvNKL-MAVPNLSMLETVDSVK 125
Cdd:cd00635   26 VTLVAVSKTVPAEAIREAIEAGQRDFGENRVqealdkaeeLPD-PDIEWHFIGHLQT---NKVkYAVRLFDLIHSVDSLK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 126 LADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSFGHDLSQgPNPDFQRL 205
Cdd:cd00635  102 LAEELNKRAEKEGR--VLDVLVQVNIGGEESKSGVAPEELEELLEEI-AALPNLRIRGLMTIAPLTEDPEE-VRPYFREL 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568953808 206 LTLRRELCEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFG 252
Cdd:cd00635  178 RELRDELGAKGGVNLK--ELSMGMSGDFEIAIEEGATLVRIGTAIFG 222
PLPDE_III_Yggs_like cd06824
Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, ...
 57-253 2.15e-54

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: 175.46  E-value: 2.15e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  57 RLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPEIKWHFIGHLQKqNVNKLMAvPNLSMLETVDSVKLA 127
Cdd:cd06824   28 QLLAVSKTKPADAIREAYAAGQRHFGENYVqealekieaLRDLQDIEWHFIGPIQS-NKTKLIA-ENFDWVHSVDRLKIA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 128 DKVNSswQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSFGHDLSQgPNPDFQRLLT 207
Cdd:cd06824  106 KRLND--QRPAGLPPLNVCIQVNISGEDSKSGVAPEDAAELAEAI-SQLPNLRLRGLMAIPAPTDDEAA-QRAAFKRLRQ 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 568953808 208 LRRELcEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFGE 253
Cdd:cd06824  182 LFDQL-KKQYPDLD--TLSMGMSGDLEAAIAAGSTMVRIGTAIFGA 224
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
 57-254 4.81e-52

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: 169.64  E-value: 4.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808   57 RLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPEIKWHFIGHLQKqNVNKLMaVPNLSMLETVDSVKLA 127
Cdd:TIGR00044  30 KLLAVSKTKPASAIQEAYDAGQRAFGENYVqelvekirhLEELGLLEWHFIGPLQS-NKSRLV-VENFDWCHTIDSLKIA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  128 DKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSfghdlsqgPNPDFQRLLT 207
Cdd:TIGR00044 108 TKLNEQREALLP--PLNVLLQINISDEESKSGIQPEELLELAAQL-EELKHLKLRGLMTIGA--------PTDSYVDQEE 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568953808  208 LRRELCE-----KLGIPVEQV-ELSMGMSMDFQHAIEVGSTNVRIGSTIFGER 254
Cdd:TIGR00044 177 VFRQMKVlfaqiKQRSPHGTIdTLSMGMSDDFEEAIAAGATMVRIGTAIFGAR 229
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 57-247 1.21e-17

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: 79.29  E-value: 1.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  57 RLVAVSKTKPADMVIEAYGHGQRTFGENYI-------LSSCPEIKWHFIGHLQKQNVNKLMAVPNLSMLeTVDSVKLADK 129
Cdd:cd06808   17 TLFAVVKANANPEVARTLAALGTGFDVASLgealllrAAGIPPEPILFLGPCKQVSELEDAAEQGVIVV-TVDSLEELEK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 130 VNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQGPNPDFQRLLTLR 209
Cdd:cd06808   96 LEEAALKAGP--PARVLLRIDTGDENGKFGVRPEELKALLERAKE-LPHLRLVGLHTHFGSADEDYSPFVEALSRFVAAL 172

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 568953808 210 RELcEKLGIPVEQVELSMGMSMD-FQHAIEVGSTNVRIG 247
Cdd:cd06808  173 DQL-GELGIDLEQLSIGGSFAILyLQELPLGTFIIVEPG 210
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
57-255 3.92e-15

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 72.64  E-value: 3.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808   57 RLVAVSKtkpADmvieAYGHG------------QRTFGENYI-----L-SSCPEIKWHFIGHLQKQNVnKLMAVPNLSMl 118
Cdd:pfam01168  22 KLMAVVK---AN----AYGHGavevaralleggADGFAVATLdealeLrEAGITAPILVLGGFPPEEL-ALAAEYDLTP- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808  119 eTVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGedSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQGP 198
Cdd:pfam01168  93 -TVDSLEQLEALAAAARRLGK--PLRVHLKIDTGM--GRLGFRPEEALALLARLAA-LPGLRLEGLMTHFACADEPDDPY 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568953808  199 NP-DFQRLLTLRRELcEKLGIPVEqvELSMGMSmdfqHAIEVGSTN---VRIGSTIFGERD 255
Cdd:pfam01168 167 TNaQLARFREAAAAL-EAAGLRPP--VVHLANS----AAILLHPLHfdmVRPGIALYGLSP 220
PLPDE_III_LS_D-TA_like cd06820
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ...
 101-254 3.90e-05

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine Aldolase-like; This subfamily is composed of uncharacterized bacterial proteins with similarity to low specificity D-threonine aldolase (D-TA), which is a fold type III PLP-dependent enzyme that catalyzes the interconversion between D-threonine/D-allo-threonine and glycine plus acetaldehyde. Both PLP and divalent cations (eg. Mn2+) are required for catalytic activity. Low specificity D-TAs show similarity to bacterial alanine racemase (AR), which contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain. AR exists as homodimers with active sites that lie at the interface between the TIM barrel domain of one subunit and the beta-sandwich domain of the other subunit. Based on its similarity to AR, it is possible that low specificity D-TAs also form dimers in solution. Experimental data show that the monomeric form of low specificity D-TAs exhibit full catalytic activity.


Pssm-ID: 143494 [Multi-domain]  Cd Length: 353  Bit Score: 44.23  E-value: 3.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 101 LQKQNVNKLMAVP---NLSMleTVDSVKLADKVNSSWQKKGptEPLKVMVQINtSGEDSKHGLLPSETIAVVEHIkASCP 177
Cdd:cd06820   81 VGRQKLERLRALAervTLSV--GVDSAEVARGLAEVAEGAG--RPLEVLVEVD-SGMNRCGVQTPEDAVALARAI-ASAP 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 178 SLEFVGLMTIGsfGHDLSQGPNP-----DFQRLLTLRRELcEKLGIPVEQVelSMGMSMDFQHAIEV-GSTNVRIGSTIF 251
Cdd:cd06820  155 GLRFRGIFTYP--GHSYAPGALEeaaadEAEALLAAAGIL-EEAGLEPPVV--SGGSTPTLWRSHEVpGITEIRPGTYIF 229


                 ...
gi 568953808 252 GER 254
Cdd:cd06820  230 NDA 232
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 149-228 4.40e-05

Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate decarboxylase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439790 [Multi-domain]  Cd Length: 417  Bit Score: 44.37  E-value: 4.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 149 INTSGEDSKHGLLPSETIAVVEHIKAScPSLEFVGLMTigsfgHDLSQGPNPD-----FQRLLTLRRELcEKLGIPVEqv 223
Cdd:COG0019  161 ISTGGKDSKFGIPLEDALEAYRRAAAL-PGLRLVGLHF-----HIGSQILDLEpfeeaLERLLELAEEL-RELGIDLE-- 231


                 ....*
gi 568953808 224 ELSMG 228
Cdd:COG0019  232 WLDLG 236
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 149-228 1.11e-03

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; Diaminopimelate decarboxylase (DapDC, EC 4.1.1.20) participates in the last step of lysine biosynthesis. It converts meso-2,6-diaminoheptanedioate to L-lysine. It is a fold type III PLP-dependent enzyme that contains an N-terminal PLP-binding TIM-barrel domain and a C-terminal beta-sandwich domain, similar to bacterial alanine racemases. DapDC 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. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.


Pssm-ID: 143501 [Multi-domain]  Cd Length: 373  Bit Score: 39.77  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568953808 149 INTSGEDSKHGLLPSETIAVVEHIKAScPSLEFVGL-MTIGsfghdlSQGPNPD-----FQRLLTLRRELcEKLGIPVEq 222
Cdd:cd06828  138 ISTGGKDSKFGIPLEQALEAYRRAKEL-PGLKLVGLhCHIG------SQILDLEpfveaAEKLLDLAAEL-RELGIDLE- 208


                 ....*.
gi 568953808 223 vELSMG 228
Cdd:cd06828  209 -FLDLG 213
 
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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