ID   PLPHP_MYCLE             Reviewed;         257 AA.
AC   Q9CCE2;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-AUG-2001, sequence version 2.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000255|HAMAP-Rule:MF_02087};
DE            Short=PLP homeostasis protein {ECO:0000255|HAMAP-Rule:MF_02087};
GN   OrderedLocusNames=ML0919;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC       involved in PLP homeostasis. {ECO:0000255|HAMAP-Rule:MF_02087}.
CC   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000255|HAMAP-Rule:MF_02087}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC31300.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL583920; CAC31300.1; ALT_INIT; Genomic_DNA.
DR   PIR; A87024; A87024.
DR   RefSeq; WP_010908026.1; NC_002677.1.
DR   AlphaFoldDB; Q9CCE2; -.
DR   SMR; Q9CCE2; -.
DR   STRING; 272631.ML0919; -.
DR   PRIDE; Q9CCE2; -.
DR   EnsemblBacteria; CAC31300; CAC31300; CAC31300.
DR   KEGG; mle:ML0919; -.
DR   Leproma; ML0919; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_0_0_11; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.10; -; 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   PANTHER; PTHR10146; PTHR10146; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00044; TIGR00044; 1.
DR   PROSITE; PS01211; UPF0001; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..257
FT                   /note="Pyridoxal phosphate homeostasis protein"
FT                   /id="PRO_0000163202"
FT   MOD_RES         47
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02087"
SQ   SEQUENCE   257 AA;  27547 MW;  F2380FE9B7AE303C CRC64;
     MAADIDLQGD RESELMHALA TVRSRLAAAS QAAGRNVGEI ELLPISKFFP ATDVAILSRL
     GCRSVGESRA QEASTKAAEF AELLGVSREE KSSIHWHMVG QIQRNKVRSL AQWAHTAHSI
     DSLQLVAALD RAVAAALAGG RREQPLQVYV QISLDGDISR GGVNVTAPGA VDRVCAQVEE
     SKSLELVGLM GIPPLGWNPD QAFEQLRLEH RRVLRSHPDA IGLSAGMSND FEIAVKHGST
     CVRVGTALLG PSRLRSP