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Conserved domains on  [gi|29126929|gb|AAH47992|]
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Proline synthetase co-transcribed [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 ...
17-141 7.09e-72

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: 214.76  E-value: 7.09e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929  17 LRAVNERVQQSVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScpEIKWHFIGHLQK 87
Cdd:cd06822   1 LIANLKRIRQAVKRASKKLPASKPRLVAVSKTKPAELIKEAYDAGQRHFGENYVqeliekapdLPI--DIKWHFIGHLQS 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 29126929  88 QNVNKLMAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSK 141
Cdd:cd06822  79 NKVKKLLKVPNLYMVETVDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESK 132
 
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, ...
17-141 7.09e-72

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: 214.76  E-value: 7.09e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929  17 LRAVNERVQQSVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScpEIKWHFIGHLQK 87
Cdd:cd06822   1 LIANLKRIRQAVKRASKKLPASKPRLVAVSKTKPAELIKEAYDAGQRHFGENYVqeliekapdLPI--DIKWHFIGHLQS 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 29126929  88 QNVNKLMAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSK 141
Cdd:cd06822  79 NKVKKLLKVPNLYMVETVDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESK 132
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
17-141 6.03e-41

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


Pssm-ID: 440094  Cd Length: 227  Bit Score: 135.94  E-value: 6.03e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929  17 LRAVNERVQQSVARRPRDLPAIqpRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPeIKWHFIGHLQK 87
Cdd:COG0325   8 LAAVRERIAAAAARAGRDPEEV--TLVAVSKTVPAEAIREAYAAGQRDFGENRVqealekieaLADLD-IEWHFIGHLQS 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 29126929  88 QNVNKlmAVPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSK 141
Cdd:COG0325  85 NKVKY--VAELFDLIHSVDRLKLAEELNKRAAKAGR--PLDVLLQVNISGEESK 134
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
41-141 5.74e-29

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: 105.31  E-value: 5.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929    41 RLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPEIKWHFIGHLQKqNVNKLMaVPNLSMLETVDSVKLA 111
Cdd:TIGR00044  30 KLLAVSKTKPASAIQEAYDAGQRAFGENYVqelvekirhLEELGLLEWHFIGPLQS-NKSRLV-VENFDWCHTIDSLKIA 107
                          90       100       110
                  ....*....|....*....|....*....|
gi 29126929   112 DKVNSSWQKKGPtePLKVMVQINTSGEDSK 141
Cdd:TIGR00044 108 TKLNEQREALLP--PLNVLLQINISDEESK 135
 
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, ...
17-141 7.09e-72

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: 214.76  E-value: 7.09e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929  17 LRAVNERVQQSVARRPRDLPAIQPRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScpEIKWHFIGHLQK 87
Cdd:cd06822   1 LIANLKRIRQAVKRASKKLPASKPRLVAVSKTKPAELIKEAYDAGQRHFGENYVqeliekapdLPI--DIKWHFIGHLQS 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 29126929  88 QNVNKLMAVPNLSMLETVDSVKLADKVNSSWQKKGPTEPLKVMVQINTSGEDSK 141
Cdd:cd06822  79 NKVKKLLKVPNLYMVETVDSEKLADKLNKAWEKLGEREPLKVMVQVNTSGEESK 132
YggS COG0325
Pyridoxal 5'-phosphate homeostasis protein YggS, UPF0001 family [Coenzyme transport and ...
17-141 6.03e-41

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


Pssm-ID: 440094  Cd Length: 227  Bit Score: 135.94  E-value: 6.03e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929  17 LRAVNERVQQSVARRPRDLPAIqpRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPeIKWHFIGHLQK 87
Cdd:COG0325   8 LAAVRERIAAAAARAGRDPEEV--TLVAVSKTVPAEAIREAYAAGQRDFGENRVqealekieaLADLD-IEWHFIGHLQS 84
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 29126929  88 QNVNKlmAVPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSK 141
Cdd:COG0325  85 NKVKY--VAELFDLIHSVDRLKLAEELNKRAAKAGR--PLDVLLQVNISGEESK 134
PLPDE_III_YBL036c_like cd00635
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes, YBL036c-like proteins; This family ...
17-141 5.68e-40

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: 133.36  E-value: 5.68e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929  17 LRAVNERVQQSVARRPRDLPAIqpRLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSScPEIKWHFIGHLQK 87
Cdd:cd00635   5 LEEVRERIAAAAERAGRDPDEV--TLVAVSKTVPAEAIREAIEAGQRDFGENRVqealdkaeeLPD-PDIEWHFIGHLQT 81
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 29126929  88 qnvNKL-MAVPNLSMLETVDSVKLADKVNSSWQKKGPtePLKVMVQINTSGEDSK 141
Cdd:cd00635  82 ---NKVkYAVRLFDLIHSVDSLKLAEELNKRAEKEGR--VLDVLVQVNIGGEESK 131
TIGR00044 TIGR00044
pyridoxal phosphate enzyme, YggS family; Members of this protein family include YggS from ...
41-141 5.74e-29

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: 105.31  E-value: 5.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929    41 RLVAVSKTKPADMVIEAYGHGQRTFGENYI---------LSSCPEIKWHFIGHLQKqNVNKLMaVPNLSMLETVDSVKLA 111
Cdd:TIGR00044  30 KLLAVSKTKPASAIQEAYDAGQRAFGENYVqelvekirhLEELGLLEWHFIGPLQS-NKSRLV-VENFDWCHTIDSLKIA 107
                          90       100       110
                  ....*....|....*....|....*....|
gi 29126929   112 DKVNSSWQKKGPtePLKVMVQINTSGEDSK 141
Cdd:TIGR00044 108 TKLNEQREALLP--PLNVLLQINISDEESK 135
PLPDE_III cd06808
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzymes; The fold type III PLP-dependent enzyme ...
41-141 6.46e-06

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: 43.85  E-value: 6.46e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29126929  41 RLVAVSKTKPADMVIEAYGHGQRTFGENYI-------LSSCPEIKWHFIGHLQKQNVNKLMAVPNLSMLeTVDSVKLADK 113
Cdd:cd06808  17 TLFAVVKANANPEVARTLAALGTGFDVASLgealllrAAGIPPEPILFLGPCKQVSELEDAAEQGVIVV-TVDSLEELEK 95
                        90       100
                ....*....|....*....|....*...
gi 29126929 114 VNSSWQKKGPtePLKVMVQINTSGEDSK 141
Cdd:cd06808  96 LEEAALKAGP--PARVLLRIDTGDENGK 121
 
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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