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Conserved domains on  [gi|518676475|ref|WP_019838168|]
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MULTISPECIES: hypothetical protein [Gammaproteobacteria]

Protein Classification

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 ...
1-64 4.33e-23

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 cd06826:

Pssm-ID: 469695 [Multi-domain]  Cd Length: 365  Bit Score: 88.94  E-value: 4.33e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518676475   1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSAGMSRNGLEMGTEQGRKDSLALA 64
Cdd:cd06826   87 IEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSGGMSRNGLELSTAQGKEDAVAIA 150
 
Name Accession Description Interval E-value
PLPDE_III_AR2 cd06826
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ...
1-64 4.33e-23

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is composed of bacterial alanine racemases (EC 5.1.1.1) with similarity to Yersinia pestis and Vibrio cholerae alanine racemase (AR) 2. ARs catalyze the interconversion between L- and D-alanine, an essential component of the peptidoglycan layer of bacterial cell walls. These proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains 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. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.


Pssm-ID: 143499 [Multi-domain]  Cd Length: 365  Bit Score: 88.94  E-value: 4.33e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518676475   1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSAGMSRNGLEMGTEQGRKDSLALA 64
Cdd:cd06826   87 IEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSGGMSRNGLELSTAQGKEDAVAIA 150
PRK13340 PRK13340
alanine racemase; Reviewed
1-64 1.51e-21

alanine racemase; Reviewed


Pssm-ID: 183984 [Multi-domain]  Cd Length: 406  Bit Score: 85.06  E-value: 1.51e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518676475   1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSAGMSRNGLEMGTEQGRKDSLALA 64
Cdd:PRK13340 126 IEQALRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSGGMSRNGLDMSTARGKWEALRIA 189
Alr COG0787
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ...
2-51 6.85e-07

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: 43.94  E-value: 6.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 518676475   2 ETALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSaGMSRNGLEM 51
Cdd:COG0787   90 ELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDT-GMNRLGFRP 138
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
1-50 5.32e-05

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 38.36  E-value: 5.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 518676475    1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSaGMSRNGLE 50
Cdd:pfam01168  82 LALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDT-GMGRLGFR 130
 
Name Accession Description Interval E-value
PLPDE_III_AR2 cd06826
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is ...
1-64 4.33e-23

Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme, Alanine Racemase 2; This subfamily is composed of bacterial alanine racemases (EC 5.1.1.1) with similarity to Yersinia pestis and Vibrio cholerae alanine racemase (AR) 2. ARs catalyze the interconversion between L- and D-alanine, an essential component of the peptidoglycan layer of bacterial cell walls. These proteins are similar to other bacterial ARs and are fold type III PLP-dependent enzymes containing contains 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. Homodimer formation and the presence of the PLP cofactor are required for catalytic activity.


Pssm-ID: 143499 [Multi-domain]  Cd Length: 365  Bit Score: 88.94  E-value: 4.33e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518676475   1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSAGMSRNGLEMGTEQGRKDSLALA 64
Cdd:cd06826   87 IEDALAYNIEELIGSLDQAEQIDSLAKRHGKTLPVHLALNSGGMSRNGLELSTAQGKEDAVAIA 150
PRK13340 PRK13340
alanine racemase; Reviewed
1-64 1.51e-21

alanine racemase; Reviewed


Pssm-ID: 183984 [Multi-domain]  Cd Length: 406  Bit Score: 85.06  E-value: 1.51e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518676475   1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSAGMSRNGLEMGTEQGRKDSLALA 64
Cdd:PRK13340 126 IEQALRYDLEELIGDDEQAKLLAAIAKKNGKPIDIHLALNSGGMSRNGLDMSTARGKWEALRIA 189
Alr COG0787
Alanine racemase [Cell wall/membrane/envelope biogenesis]; Alanine racemase is part of the ...
2-51 6.85e-07

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: 43.94  E-value: 6.85e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 518676475   2 ETALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSaGMSRNGLEM 51
Cdd:COG0787   90 ELAIEYDLEPVVHSLEQLEALAAAARRLGKPLPVHLKVDT-GMNRLGFRP 138
PLPDE_III_AR cd00430
Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Alanine Racemase; This family includes ...
1-49 1.77e-05

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: 39.79  E-value: 1.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 518676475   1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSaGMSRNGL 49
Cdd:cd00430   87 AEEAIEYDLTPTVSSLEQAEALSAAAARLGKTLKVHLKIDT-GMGRLGF 134
Ala_racemase_N pfam01168
Alanine racemase, N-terminal domain;
1-50 5.32e-05

Alanine racemase, N-terminal domain;


Pssm-ID: 460095 [Multi-domain]  Cd Length: 220  Bit Score: 38.36  E-value: 5.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 518676475    1 METALTYDVEELMGGLDFARMAGEIATRHGKILRVHLGLNSaGMSRNGLE 50
Cdd:pfam01168  82 LALAAEYDLTPTVDSLEQLEALAAAARRLGKPLRVHLKIDT-GMGRLGFR 130
 
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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