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Database: UniProt
Entry: A0A0B8ZV21_9SPHN
LinkDB: A0A0B8ZV21_9SPHN
Original site: A0A0B8ZV21_9SPHN 
ID   A0A0B8ZV21_9SPHN        Unreviewed;       221 AA.
AC   A0A0B8ZV21;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=NJ75_01846 {ECO:0000313|EMBL:KHS47010.1};
OS   Novosphingobium subterraneum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=48936 {ECO:0000313|EMBL:KHS47010.1, ECO:0000313|Proteomes:UP000031338};
RN   [1] {ECO:0000313|EMBL:KHS47010.1, ECO:0000313|Proteomes:UP000031338}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12447 {ECO:0000313|EMBL:KHS47010.1,
RC   ECO:0000313|Proteomes:UP000031338};
RA   Gan H.M., Gan H.Y., Savka M.A.;
RT   "Draft genome sequence of Novosphingobium subterraneum DSM 12447.";
RL   Submitted (OCT-2014) 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:KHS47010.1}.
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DR   EMBL; JRVC01000007; KHS47010.1; -; Genomic_DNA.
DR   RefSeq; WP_039333619.1; NZ_JRVC01000007.1.
DR   AlphaFoldDB; A0A0B8ZV21; -.
DR   STRING; 48936.NJ75_01846; -.
DR   PATRIC; fig|48936.3.peg.1861; -.
DR   Proteomes; UP000031338; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd00635; PLPDE_III_YBL036c_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}.
FT   DOMAIN          17..220
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   221 AA;  23510 MW;  A63E30185F09C1E7 CRC64;
     MEQAVPSSPL EQVHSRIATA ARIAGRKADD VTLIAISKTK PAEAILDLIA QGQRVFGENR
     VQESQDKWPA IRAAHPDVQL HLVGQLQSNK AEDAIALFDC IHSVDRPSLV TALAKAQDKL
     GRKVPCFIQV NIGNEEQKGG CAVAELPALL TQACEAGLEV VGLMCVPPAG IEAAPFFALL
     DKLADDNGLS RLSMGMSDDF ETAVQLGATH VRIGSALFGK R
//
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