Entry sw:YBHA_ECOLI

ID   YBHA_ECOLI              Reviewed;         272 AA.
AC   P21829;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   02-NOV-2016, entry version 139.
DE   RecName: Full=Pyridoxal phosphate phosphatase YbhA;
DE            Short=PLP phosphatase;
DE            EC=3.1.3.74;
GN   Name=ybhA; OrderedLocusNames=b0766, JW0749;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7665460;
RA   Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U.,
RA   Gunsalus R.P., Shanmugam K.T.;
RT   "Genetic analysis of the modABCD (molybdate transport) operon of
RT   Escherichia coli.";
RL   J. Bacteriol. 177:4851-4856(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / MC1000 / ATCC 39531;
RX   PubMed=8564363;
RA   Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.;
RT   "Molecular analysis of the molybdate uptake operon, modABCD, of
RT   Escherichia coli and modR, a regulatory gene.";
RL   Microbiol. Res. 150:347-361(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   FUNCTION AS A PHOSPHATASE.
RX   PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
RA   Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
RA   Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
RT   "Enzyme genomics: application of general enzymatic screens to discover
RT   new enzymes.";
RL   FEMS Microbiol. Rev. 29:263-279(2005).
RN   [7]
RP   FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBSTRATE SPECIFICITY, AND COFACTOR.
RX   PubMed=16990279; DOI=10.1074/jbc.M605449200;
RA   Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
RA   Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V.,
RA   Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.;
RT   "Genome-wide analysis of substrate specificities of the Escherichia
RT   coli haloacid dehalogenase-like phosphatase family.";
RL   J. Biol. Chem. 281:36149-36161(2006).
CC   -!- FUNCTION: Catalyzes the dephosphorylation of pyridoxal-phosphate
CC       (PLP). Can also hydrolyze erythrose-4-phosphate (Ery4P) and
CC       fructose-1,6-bis-phosphate (Fru1,6bisP).
CC       {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16990279}.
CC   -!- CATALYTIC ACTIVITY: Pyridoxal 5'-phosphate + H(2)O = pyridoxal +
CC       phosphate. {ECO:0000269|PubMed:16990279}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:16990279};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:16990279};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:16990279};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:16990279};
CC       Note=Magnesium. Can also use other divalent metal cations as
CC       manganese, cobalt or zinc. {ECO:0000269|PubMed:16990279};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.37 mM for PLP (in the presence of magnesium ion as cofactor
CC         and at pH 9) {ECO:0000269|PubMed:16990279};
CC         KM=1.3 mM for Fru1,6bisP (in the presence of magnesium ion as
CC         cofactor and at pH 9) {ECO:0000269|PubMed:16990279};
CC       pH dependence:
CC         Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
CC   -!- CAUTION: This ORF is coded on the other strand of an ORF which has
CC       been called modD (by PubMed:7665460 and PubMed:8564363), but which
CC       seems to be wrong. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=U07867; Type=Frameshift; Positions=217; Evidence={ECO:0000305};
DR   EMBL; U27192; AAB60177.1; -; Genomic_DNA.
DR   EMBL; U07867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; U00096; AAC73853.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35430.1; -; Genomic_DNA.
DR   PIR; F64812; F64812.
DR   RefSeq; NP_415287.1; NC_000913.3.
DR   RefSeq; WP_001300666.1; NZ_LN832404.1.
DR   ProteinModelPortal; P21829; -.
DR   SMR; P21829; -.
DR   BioGrid; 4261146; 12.
DR   IntAct; P21829; 3.
DR   STRING; 511145.b0766; -.
DR   PaxDb; P21829; -.
DR   PRIDE; P21829; -.
DR   DNASU; 945372; -.
DR   EnsemblBacteria; AAC73853; AAC73853; b0766.
DR   EnsemblBacteria; BAA35430; BAA35430; BAA35430.
DR   GeneID; 945372; -.
DR   KEGG; ecj:JW0749; -.
DR   KEGG; eco:b0766; -.
DR   PATRIC; 32116733; VBIEscCol129921_0792.
DR   EchoBASE; EB1221; -.
DR   EcoGene; EG11239; ybhA.
DR   eggNOG; ENOG4108K4B; Bacteria.
DR   eggNOG; COG0561; LUCA.
DR   HOGENOM; HOG000184780; -.
DR   InParanoid; P21829; -.
DR   OMA; MTYRVIA; -.
DR   PhylomeDB; P21829; -.
DR   BioCyc; EcoCyc:EG11239-MONOMER; -.
DR   BioCyc; ECOL316407:JW0749-MONOMER; -.
DR   BioCyc; MetaCyc:EG11239-MONOMER; -.
DR   PRO; PR:P21829; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
DR   GO; GO:0016791; F:phosphatase activity; IDA:EcoliWiki.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:EcoliWiki.
DR   GO; GO:0033883; F:pyridoxal phosphatase activity; IDA:EcoliWiki.
DR   GO; GO:0050308; F:sugar-phosphatase activity; IDA:EcoliWiki.
DR   GO; GO:0044283; P:small molecule biosynthetic process; IBA:GO_Central.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR023214; HAD-like_dom.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR000150; Hypothet_cof.
DR   Pfam; PF08282; Hydrolase_3; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   TIGRFAMs; TIGR00099; Cof-subfamily; 1.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   PROSITE; PS01228; COF_1; 1.
DR   PROSITE; PS01229; COF_2; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    272       Pyridoxal phosphate phosphatase YbhA.
FT                                /FTId=PRO_0000054420.
FT   REGION       43     44       Phosphate binding. {ECO:0000250}.
FT   ACT_SITE      9      9       Nucleophile. {ECO:0000250}.
FT   METAL         9      9       Magnesium. {ECO:0000250}.
FT   METAL        11     11       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       223    223       Magnesium. {ECO:0000250}.
FT   BINDING      10     10       Phosphate; via amide nitrogen.
FT                                {ECO:0000250}.
FT   BINDING     200    200       Phosphate. {ECO:0000250}.
FT   BINDING     226    226       Phosphate. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         6    267       ipfam:Hydrolase_3 [T]
SQ   SEQUENCE   272 AA;  30201 MW;  BB4602AB4D26ACD2 CRC64;
     MTTRVIALDL DGTLLTPKKT LLPSSIEALA RAREAGYQLI IVTGRHHVAI HPFYQALALD
     TPAICCNGTY LYDYHAKTVL EADPMPVIKA LQLIEMLNEH HIHGLMYVDD AMVYEHPTGH
     VIRTSNWAQT LPPEQRPTFT QVASLAETAQ QVNAVWKFAL THDDLPQLQH FGKHVEHELG
     LECEWSWHDQ VDIARGGNSK GKRLTKWVEA QGWSMENVVA FGDNFNDISM LEAAGTGVAM
     GNADDAVKAR ANIVIGDNTT DSIAQFIYSH LI
//