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