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PLPHP_HAEIN
ID   PLPHP_HAEIN             Reviewed;         237 AA.
AC   P44506;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=HI_0090;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=10675023;
RX   DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA   Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA   Fountoulakis M.;
RT   "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL   Electrophoresis 21:411-429(2000).
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; L42023; AAC21768.1; -; Genomic_DNA.
DR   PIR; B64142; B64142.
DR   RefSeq; NP_438263.1; NC_000907.1.
DR   RefSeq; WP_005693829.1; NC_000907.1.
DR   AlphaFoldDB; P44506; -.
DR   SMR; P44506; -.
DR   STRING; 71421.HI_0090; -.
DR   EnsemblBacteria; AAC21768; AAC21768; HI_0090.
DR   KEGG; hin:HI_0090; -.
DR   PATRIC; fig|71421.8.peg.91; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_0_1_6; -.
DR   OMA; IEWHMIG; -.
DR   PhylomeDB; P44506; -.
DR   BioCyc; HINF71421:G1GJ1-95-MON; -.
DR   Proteomes; UP000000579; Chromosome.
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   TIGRFAMs; TIGR00044; TIGR00044; 1.
DR   PROSITE; PS01211; UPF0001; 1.
PE   1: Evidence at protein level;
KW   Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..237
FT                   /note="Pyridoxal phosphate homeostasis protein"
FT                   /id="PRO_0000163199"
FT   MOD_RES         35
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02087"
SQ   SEQUENCE   237 AA;  26767 MW;  804FA860AFCFF7BD CRC64;
     MNIQHNLNLI QQKIETACKE ENRNQNTVKL LAVSKTKPIS AILSAYQAGQ TAFGENYVQE
     GVEKIQYFES QGINLEWHFI GPLQSNKTRL VAEHFDWMQT LDRAKIADRL NEQRPTNKAP
     LNVLIQINIS DEESKSGIQP EEMLTLAKHI ENLPHLCLRG LMAIPAPTDN IAEQENAFRK
     MLELFEQLKQ VLPNQQIDTL SMGMTDDMPS AIKCGSTMVR IGTAIFGARN YSTSQNK
 
 
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