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Conserved domains on  [gi|1720426181|ref|XP_030099103|]
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pyridoxal phosphate homeostasis protein isoform X5 [Mus musculus]

Protein Classification

type III PLP-dependent enzyme domain-containing protein( domain architecture ID 469)

type III PLP (pyridoxal 5-phosphate)-dependent enzyme domain-containing protein, similar to alanine racemase which catalyzes the interconversion of L-alanine and D-alanine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLPDE_III super family cl00261
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 1-143 6.60e-92

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.


The actual alignment was detected with superfamily member cd06822:

Pssm-ID: 469695  Cd Length: 227  Bit Score: 266.76  E-value: 6.60e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   1 MAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGS 80
Cdd:cd06822    85 LKVPNLYMVETVDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESKSGLEPSEAVELVKHIIEECPNLKFSGLMTIGS 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720426181  81 FGHDLSQGPNPDFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFG 143
Cdd:cd06822   165 FGYSLSSGPNPDFLCLVDCRKKVCEKLGINPDDLELSMGMSADFEHAIEMGSTNVRVGSAIFG 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, ...
 1-143 6.60e-92

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: 266.76  E-value: 6.60e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   1 MAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGS 80
Cdd:cd06822    85 LKVPNLYMVETVDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESKSGLEPSEAVELVKHIIEECPNLKFSGLMTIGS 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720426181  81 FGHDLSQGPNPDFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFG 143
Cdd:cd06822   165 FGYSLSSGPNPDFLCLVDCRKKVCEKLGINPDDLELSMGMSADFEHAIEMGSTNVRVGSAIFG 227
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
 2-146 6.42e-48

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


Pssm-ID: 440094  Cd Length: 227  Bit Score: 154.81  E-value: 6.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   2 AVPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSF 81
Cdd:COG0325    90 VAELFDLIHSVDRLKLAEELNKRAAKAGR--PLDVLLQVNISGEESKSGVAPEELPALAEAIAA-LPNLRLRGLMTIAPL 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426181  82 GHDLSQgPNPDFQRLLTLRRELcEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFGERD 146
Cdd:COG0325   167 TEDPEE-VRPAFARLRELFDRL-RAQGPGLD--ELSMGMSGDYEIAIEEGATMVRVGTAIFGARP 227
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
 3-145 1.45e-30

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: 110.70  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   3 VPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSfg 82
Cdd:TIGR00044  92 VENFDWCHTIDSLKIATKLNEQREALLP--PLNVLLQINISDEESKSGIQPEELLELAAQL-EELKHLKLRGLMTIGA-- 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426181  83 hdlsqgPNPDFQRLLTLRRELCE-----KLGIPVEQV-ELSMGMSMDFQHAIEVGSTNVRIGSTIFGER 145
Cdd:TIGR00044 167 ------PTDSYVDQEEVFRQMKVlfaqiKQRSPHGTIdTLSMGMSDDFEEAIAAGATMVRIGTAIFGAR 229
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
11-146 6.96e-14

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 66.48  E-value: 6.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  11 TVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGedSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQGPN 90
Cdd:pfam01168  93 TVDSLEQLEALAAAARRLGK--PLRVHLKIDTGM--GRLGFRPEEALALLARLAA-LPGLRLEGLMTHFACADEPDDPYT 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  91 P-DFQRLLTLRRELcEKLGIPVEqvELSMGMSmdfqHAIEVGSTN---VRIGSTIFGERD 146
Cdd:pfam01168 168 NaQLARFREAAAAL-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, ...
 1-143 6.60e-92

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: 266.76  E-value: 6.60e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   1 MAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIKASCPSLEFVGLMTIGS 80
Cdd:cd06822    85 LKVPNLYMVETVDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESKSGLEPSEAVELVKHIIEECPNLKFSGLMTIGS 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720426181  81 FGHDLSQGPNPDFQRLLTLRRELCEKLGIPVEQVELSMGMSMDFQHAIEVGSTNVRIGSTIFG 143
Cdd:cd06822   165 FGYSLSSGPNPDFLCLVDCRKKVCEKLGINPDDLELSMGMSADFEHAIEMGSTNVRVGSAIFG 227
PLPDE_III_YBL036c_like cd00635
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins; This family ...
 2-143 3.69e-48

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: 155.32  E-value: 3.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   2 AVPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSF 81
Cdd:cd00635    87 AVRLFDLIHSVDSLKLAEELNKRAEKEGR--VLDVLVQVNIGGEESKSGVAPEELEELLEEI-AALPNLRIRGLMTIAPL 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426181  82 GHDLSQgPNPDFQRLLTLRRELCEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFG 143
Cdd:cd00635   164 TEDPEE-VRPYFRELRELRDELGAKGGVNLK--ELSMGMSGDFEIAIEEGATLVRIGTAIFG 222
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
 2-146 6.42e-48

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


Pssm-ID: 440094  Cd Length: 227  Bit Score: 154.81  E-value: 6.42e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   2 AVPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSF 81
Cdd:COG0325    90 VAELFDLIHSVDRLKLAEELNKRAAKAGR--PLDVLLQVNISGEESKSGVAPEELPALAEAIAA-LPNLRLRGLMTIAPL 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426181  82 GHDLSQgPNPDFQRLLTLRRELcEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFGERD 146
Cdd:COG0325   167 TEDPEE-VRPAFARLRELFDRL-RAQGPGLD--ELSMGMSGDYEIAIEEGATMVRVGTAIFGARP 227
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
 3-145 1.45e-30

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: 110.70  E-value: 1.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181   3 VPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSfg 82
Cdd:TIGR00044  92 VENFDWCHTIDSLKIATKLNEQREALLP--PLNVLLQINISDEESKSGIQPEELLELAAQL-EELKHLKLRGLMTIGA-- 166

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426181  83 hdlsqgPNPDFQRLLTLRRELCE-----KLGIPVEQV-ELSMGMSMDFQHAIEVGSTNVRIGSTIFGER 145
Cdd:TIGR00044 167 ------PTDSYVDQEEVFRQMKVlfaqiKQRSPHGTIdTLSMGMSDDFEEAIAAGATMVRIGTAIFGAR 229
PLPDE_III_Yggs_like cd06824
Pyridoxal 5-phosphate (PLP)-binding TIM barrel domain of Type III PLP-Dependent Enzymes, ...
 10-144 5.54e-30

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: 108.82  E-value: 5.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  10 ETVDSVKLADKVNSswQKKGPTEPLKVMVQINTSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGSFGHDLSQgP 89
Cdd:cd06824    97 HSVDRLKIAKRLND--QRPAGLPPLNVCIQVNISGEDSKSGVAPEDAAELAEAI-SQLPNLRLRGLMAIPAPTDDEAA-Q 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720426181  90 NPDFQRLLTLRRELcEKLGIPVEqvELSMGMSMDFQHAIEVGSTNVRIGSTIFGE 144
Cdd:cd06824   173 RAAFKRLRQLFDQL-KKQYPDLD--TLSMGMSGDLEAAIAAGSTMVRIGTAIFGA 224
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
 11-138 1.76e-14

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: 68.11  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  11 TVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQGPN 90
Cdd:cd06808    86 TVDSLEELEKLEEAALKAGP--PARVLLRIDTGDENGKFGVRPEELKALLERAKE-LPHLRLVGLHTHFGSADEDYSPFV 162

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720426181  91 PDFQRLLTLRRELcEKLGIPVEQVELSMGMSMD-FQHAIEVGSTNVRIG 138
Cdd:cd06808   163 EALSRFVAALDQL-GELGIDLEQLSIGGSFAILyLQELPLGTFIIVEPG 210
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
11-146 6.96e-14

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 66.48  E-value: 6.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  11 TVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGedSKHGLLPSETIAVVEHIKAsCPSLEFVGLMTIGSFGHDLSQGPN 90
Cdd:pfam01168  93 TVDSLEQLEALAAAARRLGK--PLRVHLKIDTGM--GRLGFRPEEALALLARLAA-LPGLRLEGLMTHFACADEPDDPYT 167

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  91 P-DFQRLLTLRRELcEKLGIPVEqvELSMGMSmdfqHAIEVGSTN---VRIGSTIFGERD 146
Cdd:pfam01168 168 NaQLARFREAAAAL-EAAGLRPP--VVHLANS----AAILLHPLHfdmVRPGIALYGLSP 220
LysA COG0019
Diaminopimelate decarboxylase [Amino acid transport and metabolism]; Diaminopimelate ...
 40-119 1.05e-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: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  40 INTSGEDSKHGLLPSETIAVVEHIKAScPSLEFVGLMTigsfgHDLSQGPNPD-----FQRLLTLRRELcEKLGIPVEqv 114
Cdd:COG0019   161 ISTGGKDSKFGIPLEDALEAYRRAAAL-PGLRLVGLHF-----HIGSQILDLEpfeeaLERLLELAEEL-RELGIDLE-- 231


                  ....*
gi 1720426181 115 ELSMG 119
Cdd:COG0019   232 WLDLG 236
PLPDE_III_LS_D-TA_like cd06820
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, Low Specificity D-Threonine ...
 11-145 1.27e-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: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  11 TVDSVKLADKVNSSWQKKGptEPLKVMVQINtSGEDSKHGLLPSETIAVVEHIkASCPSLEFVGLMTIGsfGHDLSQGPN 90
Cdd:cd06820   101 GVDSAEVARGLAEVAEGAG--RPLEVLVEVD-SGMNRCGVQTPEDAVALARAI-ASAPGLRFRGIFTYP--GHSYAPGAL 174

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426181  91 P-----DFQRLLTLRRELcEKLGIPVEQVelSMGMSMDFQHAIEV-GSTNVRIGSTIFGER 145
Cdd:cd06820   175 EeaaadEAEALLAAAGIL-EEAGLEPPVV--SGGSTPTLWRSHEVpGITEIRPGTYIFNDA 232
PLPDE_III_DapDC cd06828
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Diaminopimelate Decarboxylase; ...
 40-119 3.20e-04

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: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426181  40 INTSGEDSKHGLLPSETIAVVEHIKAScPSLEFVGL-MTIGsfghdlSQGPNPD-----FQRLLTLRRELcEKLGIPVEq 113
Cdd:cd06828   138 ISTGGKDSKFGIPLEQALEAYRRAKEL-PGLKLVGLhCHIG------SQILDLEpfveaAEKLLDLAAEL-RELGIDLE- 208


                  ....*.
gi 1720426181 114 vELSMG 119
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.
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