ID   PLPHP_DEIRA             Reviewed;         209 AA.
AC   Q9RUL6;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=DR_1368;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
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; AE000513; AAF10940.1; -; Genomic_DNA.
DR   PIR; A75403; A75403.
DR   RefSeq; NP_295091.1; NC_001263.1.
DR   RefSeq; WP_010888009.1; NZ_CP015081.1.
DR   AlphaFoldDB; Q9RUL6; -.
DR   SMR; Q9RUL6; -.
DR   STRING; 243230.DR_1368; -.
DR   EnsemblBacteria; AAF10940; AAF10940; DR_1368.
DR   KEGG; dra:DR_1368; -.
DR   PATRIC; fig|243230.17.peg.1565; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_1_0_0; -.
DR   InParanoid; Q9RUL6; -.
DR   OMA; PLEWHMI; -.
DR   OrthoDB; 1423012at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
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   PROSITE; PS01211; UPF0001; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..209
FT                   /note="Pyridoxal phosphate homeostasis protein"
FT                   /id="PRO_0000163195"
FT   MOD_RES         31
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02087"
SQ   SEQUENCE   209 AA;  22235 MW;  E7B42D23D9E82B2B CRC64;
     MSVPAVLAGI REAEAQAGRA AGTVRLVAVT KGHSLDEIRG QVLAHGDFPL AENRGQELRD
     KVAGLPGAEW HFIGPLQRNK IKYLRGVTLV HSIEEPWQAQ AIADAAAEWG QAPAVLLQRH
     NGEGQKHGVL PDDLPAVLRE VRATGLEVRG LMAMAPYDDE ARAAQVFADT ARQAQDLGLV
     ELSMGMSGDY PLAVAAGATL VRVGRSLFA