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Pyridoxal phosphate phosphatase YbhA (PLP phosphatase) (EC 3.1.3.74)

 YBHA_ECOLI              Reviewed;         272 AA.
P21829;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 3.
28-MAR-2018, entry version 145.
RecName: Full=Pyridoxal phosphate phosphatase YbhA;
Short=PLP phosphatase;
EC=3.1.3.74;
Name=ybhA; OrderedLocusNames=b0766, JW0749;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=7665460; DOI=10.1128/jb.177.17.4851-4856.1995;
Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U.,
Gunsalus R.P., Shanmugam K.T.;
"Genetic analysis of the modABCD (molybdate transport) operon of
Escherichia coli.";
J. Bacteriol. 177:4851-4856(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12 / MC1000 / ATCC 39531;
PubMed=8564363;
Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R.;
"Molecular analysis of the molybdate uptake operon, modABCD, of
Escherichia coli and modR, a regulatory gene.";
Microbiol. Res. 150:347-361(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=8905232; DOI=10.1093/dnares/3.3.137;
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome
corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
FUNCTION AS A PHOSPHATASE.
PubMed=15808744; DOI=10.1016/j.fmrre.2004.12.006;
Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A.,
Arrowsmith C.H., Edwards A.M., Yakunin A.F.;
"Enzyme genomics: application of general enzymatic screens to discover
new enzymes.";
FEMS Microbiol. Rev. 29:263-279(2005).
[7]
FUNCTION AS A PHOSPHATASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, SUBSTRATE SPECIFICITY, AND COFACTOR.
PubMed=16990279; DOI=10.1074/jbc.M605449200;
Kuznetsova E., Proudfoot M., Gonzalez C.F., Brown G., Omelchenko M.V.,
Borozan I., Carmel L., Wolf Y.I., Mori H., Savchenko A.V.,
Arrowsmith C.H., Koonin E.V., Edwards A.M., Yakunin A.F.;
"Genome-wide analysis of substrate specificities of the Escherichia
coli haloacid dehalogenase-like phosphatase family.";
J. Biol. Chem. 281:36149-36161(2006).
-!- FUNCTION: Catalyzes the dephosphorylation of pyridoxal-phosphate
(PLP). Can also hydrolyze erythrose-4-phosphate (Ery4P) and
fructose-1,6-bis-phosphate (Fru1,6bisP).
{ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16990279}.
-!- CATALYTIC ACTIVITY: Pyridoxal 5'-phosphate + H(2)O = pyridoxal +
phosphate. {ECO:0000269|PubMed:16990279}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:16990279};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:16990279};
Name=Co(2+); Xref=ChEBI:CHEBI:48828;
Evidence={ECO:0000269|PubMed:16990279};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:16990279};
Note=Magnesium. Can also use other divalent metal cations as
manganese, cobalt or zinc. {ECO:0000269|PubMed:16990279};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.37 mM for PLP (in the presence of magnesium ion as cofactor
and at pH 9) {ECO:0000269|PubMed:16990279};
KM=1.3 mM for Fru1,6bisP (in the presence of magnesium ion as
cofactor and at pH 9) {ECO:0000269|PubMed:16990279};
pH dependence:
Optimum pH is between 6 and 7.5. {ECO:0000269|PubMed:16990279};
-!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CbbY/CbbZ/Gph/YieH family. {ECO:0000305}.
-!- CAUTION: This ORF is coded on the other strand of an ORF which has
been called modD (by PubMed:7665460 and PubMed:8564363), but which
seems to be wrong. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=U07867; Type=Frameshift; Positions=217; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U27192; AAB60177.1; -; Genomic_DNA.
EMBL; U07867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U00096; AAC73853.1; -; Genomic_DNA.
EMBL; AP009048; BAA35430.1; -; Genomic_DNA.
PIR; F64812; F64812.
RefSeq; NP_415287.1; NC_000913.3.
RefSeq; WP_001300666.1; NZ_LN832404.1.
ProteinModelPortal; P21829; -.
SMR; P21829; -.
BioGrid; 4261146; 12.
IntAct; P21829; 3.
STRING; 316385.ECDH10B_0834; -.
PaxDb; P21829; -.
PRIDE; P21829; -.
DNASU; 945372; -.
EnsemblBacteria; AAC73853; AAC73853; b0766.
EnsemblBacteria; BAA35430; BAA35430; BAA35430.
GeneID; 945372; -.
KEGG; ecj:JW0749; -.
KEGG; eco:b0766; -.
PATRIC; fig|1411691.4.peg.1512; -.
EchoBASE; EB1221; -.
EcoGene; EG11239; ybhA.
eggNOG; ENOG4108K4B; Bacteria.
eggNOG; COG0561; LUCA.
HOGENOM; HOG000184780; -.
InParanoid; P21829; -.
OMA; FSCEWSW; -.
PhylomeDB; P21829; -.
BioCyc; EcoCyc:EG11239-MONOMER; -.
BioCyc; MetaCyc:EG11239-MONOMER; -.
PRO; PR:P21829; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005829; C:cytosol; IDA:EcoCyc.
GO; GO:0000287; F:magnesium ion binding; IDA:EcoliWiki.
GO; GO:0016791; F:phosphatase activity; IDA:EcoliWiki.
GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:EcoliWiki.
GO; GO:0033883; F:pyridoxal phosphatase activity; IDA:EcoliWiki.
GO; GO:0050308; F:sugar-phosphatase activity; IDA:EcoliWiki.
Gene3D; 3.40.50.1000; -; 2.
InterPro; IPR000150; Cof.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR006379; HAD-SF_hydro_IIB.
InterPro; IPR023214; HAD_sf.
SUPFAM; SSF56784; SSF56784; 1.
TIGRFAMs; TIGR00099; Cof-subfamily; 1.
TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
PROSITE; PS01228; COF_1; 1.
PROSITE; PS01229; COF_2; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Magnesium; Metal-binding;
Reference proteome.
CHAIN 1 272 Pyridoxal phosphate phosphatase YbhA.
/FTId=PRO_0000054420.
REGION 43 44 Phosphate binding. {ECO:0000250}.
ACT_SITE 9 9 Nucleophile. {ECO:0000250}.
METAL 9 9 Magnesium. {ECO:0000250}.
METAL 11 11 Magnesium; via carbonyl oxygen.
{ECO:0000250}.
METAL 223 223 Magnesium. {ECO:0000250}.
BINDING 10 10 Phosphate; via amide nitrogen.
{ECO:0000250}.
BINDING 200 200 Phosphate. {ECO:0000250}.
BINDING 226 226 Phosphate. {ECO:0000250}.
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


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