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Database: UniProt
Entry: A4BKC3_9GAMM
LinkDB: A4BKC3_9GAMM
Original site: A4BKC3_9GAMM 
ID   A4BKC3_9GAMM            Unreviewed;       235 AA.
AC   A4BKC3;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   13-SEP-2023, entry version 57.
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=MED297_19052 {ECO:0000313|EMBL:EAR07428.1};
OS   Reinekea blandensis MED297.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Saccharospirillaceae; Reinekea.
OX   NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR07428.1, ECO:0000313|Proteomes:UP000005953};
RN   [1] {ECO:0000313|EMBL:EAR07428.1, ECO:0000313|Proteomes:UP000005953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED297 {ECO:0000313|EMBL:EAR07428.1,
RC   ECO:0000313|Proteomes:UP000005953};
RA   Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA   Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA   Venter J.C.;
RL   Submitted (FEB-2006) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAR07428.1}.
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DR   EMBL; AAOE01000043; EAR07428.1; -; Genomic_DNA.
DR   RefSeq; WP_008044388.1; NZ_CH724151.1.
DR   AlphaFoldDB; A4BKC3; -.
DR   STRING; 314283.MED297_19052; -.
DR   HOGENOM; CLU_059988_0_1_6; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000005953; Unassembled WGS sequence.
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:UP000005953}.
FT   DOMAIN          30..228
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         38
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   235 AA;  25821 MW;  47C8D5AC014A982E CRC64;
     MSELSVTSRL AQVNAKIHAA CTKNDRPESE VTLVAVSKTK PAARVREAWE AGARHFGENY
     AQELAEKVQE LKLDKAQWHF IGPLQSNKTR LIAEHADWVH TIDRLKIARR LSDQRPPDRA
     PLNVLIQVNI SDDPAKAGVD LSQIAGLADR IATLPNLTLR GLMTITAANL DEATLAAQFR
     ELKNAQADLI THHPTCTEVS MGMSQDFELA IANGATMVRV GSDIFGHRAP KPDKE
//
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