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Database: UniProt
Entry: H3NUV2_9GAMM
LinkDB: H3NUV2_9GAMM
Original site: H3NUV2_9GAMM 
ID   H3NUV2_9GAMM            Unreviewed;       230 AA.
AC   H3NUV2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-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=OMB55_00022070 {ECO:0000313|EMBL:EHQ58459.1};
OS   gamma proteobacterium HIMB55.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ58459.1, ECO:0000313|Proteomes:UP000003408};
RN   [1] {ECO:0000313|EMBL:EHQ58459.1, ECO:0000313|Proteomes:UP000003408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ58459.1,
RC   ECO:0000313|Proteomes:UP000003408};
RX   PubMed=22493201; DOI=10.1128/JB.00171-12;
RA   Huggett M.J., Rappe M.S.;
RT   "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium of
RT   the OM60/NOR5 Clade.";
RL   J. Bacteriol. 194:2393-2394(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:EHQ58459.1}.
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DR   EMBL; AGIF02000001; EHQ58459.1; -; Genomic_DNA.
DR   AlphaFoldDB; H3NUV2; -.
DR   STRING; 745014.OMB55_00022070; -.
DR   PATRIC; fig|745014.4.peg.2237; -.
DR   eggNOG; COG0325; Bacteria.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000003408; 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:UP000003408}.
FT   DOMAIN          14..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   230 AA;  25199 MW;  F7A3F0740EF4FD48 CRC64;
     MNVPDLHQNI SRIRNRLSKA IDAAQRAPDS VKLIAVSKTK SAEAIKAVYD TGQRDFGENY
     VSEAIEKMSA LESLDICWHF LGPLQSNKTR LVAANFDWIH SVDRVKIAKR LNEQRPDALP
     PLNVCLQVNI PAEPTKSGVA SEAELLDLAL AISEMDRLAL RGIMAIPAPA SDFEQQCAQF
     NRIAQLLSIP DLPKQMNELS IGMSGDMDAA VAEGATMVRI GTDIFGARYN
//
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