PLPHP_ECOL6
ID PLPHP_ECOL6 Reviewed; 234 AA.
AC P67081; P52054;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
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 Name=yggS; OrderedLocusNames=c3537;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC involved in PLP homeostasis. {ECO:0000255|HAMAP-Rule:MF_02087}.
CC -!- SUBUNIT: Monomer. {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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN81985.1; -; Genomic_DNA.
DR RefSeq; WP_000997795.1; NC_004431.1.
DR AlphaFoldDB; P67081; -.
DR SMR; P67081; -.
DR STRING; 199310.c3537; -.
DR EnsemblBacteria; AAN81985; AAN81985; c3537.
DR GeneID; 66673167; -.
DR KEGG; ecc:c3537; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_0_1_6; -.
DR OMA; IEWHMIG; -.
DR BioCyc; ECOL199310:C3537-MON; -.
DR Proteomes; UP000001410; 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..234
FT /note="Pyridoxal phosphate homeostasis protein"
FT /id="PRO_0000163197"
FT MOD_RES 36
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02087"
SQ SEQUENCE 234 AA; 25787 MW; 2AA431E2D75BCA59 CRC64;
MNDIAHNLAQ VRDKISAAAT RCGRSPEEIT LLAVSKTKPA SAIAEAIDAG QRQFGENYVQ
EGVDKIRHFQ ELGVTGLEWH FIGPLQSNKS RLVAEHFDWC HTIDRLRIAT RLNDQRPAEL
PPLNVLIQIN ISDENSKSGI QLAELDELAA AVAELPRLRL RGLMAIPAPE SEYVRQFEVA
RQMAVAFAGL KTRYPHIDTL SLGMSDDMEA AIAAGSTMVR IGTAIFGARD YSKK