ID A0A0S2JHI8_9GAMM Unreviewed; 239 AA.
AC A0A0S2JHI8;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
DE Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
GN ORFNames=CMT41_12665 {ECO:0000313|EMBL:ALO35474.1};
OS Colwellia sp. MT41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=58049 {ECO:0000313|EMBL:ALO35474.1, ECO:0000313|Proteomes:UP000065319};
RN [1] {ECO:0000313|EMBL:ALO35474.1, ECO:0000313|Proteomes:UP000065319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MT41 {ECO:0000313|EMBL:ALO35474.1,
RC ECO:0000313|Proteomes:UP000065319};
RA Kyaw T.S., Ugalde J., Peoples L., Narasingarao P., Chastain R.A.,
RA Yayanos A., Methe B.A., Bartlett D.H.;
RT "Distinctive Gene and Protein Characteristics of Extremely Piezophilic
RT Colwellia.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC involved in PLP homeostasis. {ECO:0000256|HAMAP-Rule:MF_02087}.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|PIRSR:PIRSR004848-1};
CC -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC YggS/PROSC family. {ECO:0000256|HAMAP-Rule:MF_02087,
CC ECO:0000256|RuleBase:RU004514}.
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DR EMBL; CP013145; ALO35474.1; -; Genomic_DNA.
DR RefSeq; WP_057181636.1; NZ_CP013145.1.
DR AlphaFoldDB; A0A0S2JHI8; -.
DR STRING; 58049.CMT41_12665; -.
DR KEGG; com:CMT41_12665; -.
DR OrthoDB; 9804072at2; -.
DR Proteomes; UP000065319; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR CDD; cd06824; PLPDE_III_Yggs_like; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_02087; PLP_homeostasis; 1.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR029066; PLP-binding_barrel.
DR InterPro; IPR011078; PyrdxlP_homeostasis.
DR NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR PANTHER; PTHR10146; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1.
DR PANTHER; PTHR10146:SF14; PYRIDOXAL PHOSPHATE HOMEOSTASIS PROTEIN; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS01211; UPF0001; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_02087,
KW ECO:0000256|PIRSR:PIRSR004848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000065319}.
FT DOMAIN 30..235
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 45
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 239 AA; 26792 MW; 7C95AEBD36F8D814 CRC64;
MINIKDNLDK IKAQIQQACQ QSGRLIPYTE QVKQSLPVSL LAVSKTKPAA LIEQAYLAGQ
HDFGENYLQE AVEKITQLAH LPELNWHFIG PIQANKTKQI ARYFSWVHSV DREKIARRLN
QHIQDDNCHN TPLNICLQVN ISNEESKSGV AIDDILSLAD IVNNCDKLTL RGLMAVPEKN
AGNDCYEKMQ QLFIQLQKHY PSVDTLSLGM SNDLPQAVAH GSTMVRIGSA IFGARTYKN
//
