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Database: UniProt
Entry: K2JZF9_9GAMM
LinkDB: K2JZF9_9GAMM
Original site: K2JZF9_9GAMM 
ID   K2JZF9_9GAMM            Unreviewed;       226 AA.
AC   K2JZF9;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=B3C1_06453 {ECO:0000313|EMBL:EKE75699.1};
OS   Gallaecimonas xiamenensis 3-C-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Gallaecimonas.
OX   NCBI_TaxID=745411 {ECO:0000313|EMBL:EKE75699.1, ECO:0000313|Proteomes:UP000006755};
RN   [1] {ECO:0000313|EMBL:EKE75699.1, ECO:0000313|Proteomes:UP000006755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3-C-1 {ECO:0000313|EMBL:EKE75699.1,
RC   ECO:0000313|Proteomes:UP000006755};
RX   PubMed=23209203; DOI=10.1128/JB.01854-12;
RA   Lai Q., Wang L., Wang W., Shao Z.;
RT   "Genome Sequence of Gallaecimonas xiamenensis Type Strain 3-C-1.";
RL   J. Bacteriol. 194:6937-6937(2012).
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:EKE75699.1}.
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DR   EMBL; AMRI01000007; EKE75699.1; -; Genomic_DNA.
DR   RefSeq; WP_008483698.1; NZ_AMRI01000007.1.
DR   AlphaFoldDB; K2JZF9; -.
DR   STRING; 745411.B3C1_06453; -.
DR   PATRIC; fig|745411.4.peg.1281; -.
DR   eggNOG; COG0325; Bacteria.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000006755; 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.
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:UP000006755}.
FT   DOMAIN          30..224
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   226 AA;  24127 MW;  8870BBA96DAA8AAE CRC64;
     MTTIAERLGA AAGRIAKAAQ VAGRDPDSIT LLAVSKRKPL EDVVAALAQG QQAFGENYVQ
     EGVEKIQALA QQQPGAQVQW HLIGPLQSNK TAQVAQYFDW VQSIDRAKIA KRLSEQRPGH
     LKPIQICIQV NISGEESKSG VTPDAVLALA ADIAGLPNVR LRGLMAIGSG AQQEFHSMKA
     LFDQLKDSFP QVDTLSMGMS DDLEAAIMEG ATLVRLGTAI FGARTN
//
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