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Database: UniProt
Entry: A4I0L9_LEIIN
LinkDB: A4I0L9_LEIIN
Original site: A4I0L9_LEIIN 
ID   A4I0L9_LEIIN            Unreviewed;       245 AA.
AC   A4I0L9; A0A2K4YUX5; A0A381MIN1;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
DE            Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_03225};
GN   ORFNames=LINJ_23_1880 {ECO:0000313|EMBL:CAM68291.1};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM68291.1, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM68291.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM68291.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM68291.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM68291.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which may be
CC       involved in intracellular homeostatic regulation of pyridoxal 5'-
CC       phosphate (PLP), the active form of vitamin B6. {ECO:0000256|HAMAP-
CC       Rule:MF_03225}.
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_03225,
CC       ECO:0000256|RuleBase:RU004514}.
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DR   EMBL; FR796455; CAM68291.1; -; Genomic_DNA.
DR   RefSeq; XP_001465860.1; XM_001465823.1.
DR   AlphaFoldDB; A4I0L9; -.
DR   SMR; A4I0L9; -.
DR   STRING; 5671.A4I0L9; -.
DR   GeneID; 5069287; -.
DR   KEGG; lif:LINJ_23_1880; -.
DR   VEuPathDB; TriTrypDB:LINF_230025500; -.
DR   eggNOG; KOG3157; Eukaryota.
DR   InParanoid; A4I0L9; -.
DR   OMA; PLEWHMI; -.
DR   OrthoDB; 21261at2759; -.
DR   Proteomes; UP000008153; Chromosome 23.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   CDD; cd06822; PLPDE_III_YBL036c_euk; 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   Isomerase {ECO:0000313|EMBL:CAM68291.1};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_03225,
KW   ECO:0000256|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008153}.
FT   DOMAIN          15..238
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         42
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03225,
FT                   ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   245 AA;  27228 MW;  A80DAF267254927F CRC64;
     MSRYDIASEP TAETLALNYK AVRDTVAQES GNRRVTLIAV SKTKSPACLL NLYNLGQRVF
     GENYVQELGE KAKVLPEDTV WHFIGHLQSN KVKELLEGVP NLRVIQTIDS ENLASKVNEG
     CRKYRGGRPL EVYIQVNTSG EETKSGTEPG EATVALAKYI VDECPLLRLK GLMTIGMPDY
     TSRPENFECL TKCREDVAQA VQMAPEDLEL SMGMSGDYVN AIRMGSTTVR VGTSIFGQRY
     YPHKQ
//
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