ID   PLPHP_MYCBO             Reviewed;         258 AA.
AC   P67084; A0A1R3Y0F2; O06228; X2BK84;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
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=BQ2027_MB2172C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
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}.
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DR   EMBL; LT708304; SIU00780.1; -; Genomic_DNA.
DR   RefSeq; NP_855821.1; NC_002945.3.
DR   RefSeq; WP_003411137.1; NC_002945.4.
DR   AlphaFoldDB; P67084; -.
DR   SMR; P67084; -.
DR   EnsemblBacteria; SIU00780; SIU00780; BQ2027_MB2172C.
DR   PATRIC; fig|233413.5.peg.2388; -.
DR   OMA; IEWHMIG; -.
DR   Proteomes; UP000001419; 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.
FT   CHAIN           1..258
FT                   /note="Pyridoxal phosphate homeostasis protein"
FT                   /id="PRO_0000163204"
FT   MOD_RES         47
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02087"
SQ   SEQUENCE   258 AA;  27693 MW;  6C534D96E9368BB2 CRC64;
     MAADLSAYPD RESELTHALA AMRSRLAAAA EAAGRNVGEI ELLPITKFFP ATDVAILFRL
     GCRSVGESRE QEASAKMAEL NRLLAAAELG HSGGVHWHMV GRIQRNKAGS LARWAHTAHS
     VDSSRLVTAL DRAVVAALAE HRRGERLRVY VQVSLDGDGS RGGVDSTTPG AVDRICAQVQ
     ESEGLELVGL MGIPPLDWDP DEAFDRLQSE HNRVRAMFPH AIGLSAGMSN DLEVAVKHGS
     TCVRVGTALL GPRRLRSP