ID   PLPHP_MYCTO             Reviewed;         258 AA.
AC   P9WFQ6; L0T8S0; O06228; P67083;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 34.
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=MT2207;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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=AAK46491.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46491.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70578; H70578.
DR   RefSeq; WP_003411137.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFQ6; -.
DR   SMR; P9WFQ6; -.
DR   EnsemblBacteria; AAK46491; AAK46491; MT2207.
DR   KEGG; mtc:MT2207; -.
DR   PATRIC; fig|83331.31.peg.2380; -.
DR   HOGENOM; CLU_059988_0_0_11; -.
DR   Proteomes; UP000001020; 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_0000428495"
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