ID   Q8X927_ECO57            Unreviewed;       272 AA.
AC   Q8X927; A0A0H3JGJ7; A0A6M0JPS6; Q7AGH9;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   27-NOV-2024, entry version 134.
DE   SubName: Full=Pyridoxal phosphate phosphatase {ECO:0000313|EMBL:BAB34217.1};
GN   Name=ybhA {ECO:0000313|EMBL:BAB34217.1};
GN   ORFNames=ECs_0794 {ECO:0000313|EMBL:BAB34217.1};
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334 {ECO:0000313|EMBL:BAB34217.1, ECO:0000313|Proteomes:UP000000558};
RN   [1] {ECO:0000313|EMBL:BAB34217.1, ECO:0000313|Proteomes:UP000000558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC
RC   {ECO:0000313|Proteomes:UP000000558};
RX   PubMed=11258796; DOI=.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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DR   EMBL; BA000007; BAB34217.1; -; Genomic_DNA.
DR   RefSeq; NP_308821.1; NC_002695.1.
DR   RefSeq; WP_001303848.1; NZ_VOAI01000019.1.
DR   AlphaFoldDB; Q8X927; -.
DR   STRING; 155864.Z0936; -.
DR   GeneID; 917532; -.
DR   KEGG; ecs:ECs_0794; -.
DR   PATRIC; fig|386585.9.peg.914; -.
DR   eggNOG; COG0561; Bacteria.
DR   HOGENOM; CLU_044146_1_0_6; -.
DR   Proteomes; UP000000558; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter.
DR   GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR   CDD; cd07516; HAD_Pase; 1.
DR   FunFam; 3.30.1240.10:FF:000005; Cof family hydrolase; 1.
DR   Gene3D; 3.30.1240.10; -; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR000150; Cof.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   NCBIfam; TIGR00099; Cof-subfamily; 1.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   PANTHER; PTHR10000:SF58; MANNOSYL-3-PHOSPHOGLYCERATE PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR10000; PHOSPHOSERINE PHOSPHATASE; 1.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS01228; COF_1; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000558}.
SQ   SEQUENCE   272 AA;  30260 MW;  5D46BCC7665B6CD3 CRC64;
     MTTRVIALDL DGTLLTPKKT LLPSSIEALA RAREAGYQLI IVTGRHHVAI HPFYQALALD
     TPAICCNGTY LYDYHAKTVL EADPMPVNKA LQLIEMLNEH HIHGLMYVDD EMVYEHPTGH
     VIRTSNWAQT LPPEQRPTFT QVASLAETAQ QVNAVWKFAL THDDLPQLQH FGKHVEHELG
     LECEWSWHDQ VDIARGGNSK GKRLTKWVEA QGWSMENVVA FGDNFNDISM LEAAGTGVAM
     GNADDAVKAR ANIVIGDNTT DSIAQFIYSH LI
//