P21829 (YBHA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyridoxal phosphate phosphatase YbhA
EC=3.1.3.74

Gene names

Name:	ybhA
Ordered Locus Names:	b0766, JW0749

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	272 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the dephosphorylation of pyridoxal-phosphate (PLP). Can also hydrolyze erythrose-4-phosphate (Ery4P) and fructose-1,6-bis-phosphate (Fru1,6bisP). Ref.6 Ref.7
Catalytic activity	Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.
Cofactor	Magnesium. Can also use other divalent metal cations as manganese, cobalt and zinc. Ref.7
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. CbbY/CbbZ/Gph/YieH family.
Caution	This ORF is coded on the other strand of an ORF which has been called modD (by Ref.1 and Ref.2), but which seems to be wrong.
Biophysicochemical properties	Kinetic parameters: KM=0.37 mM for PLP (with magnesium ions as cofactor and at pH 9) Ref.7 KM=1.3 mM for Fru1,6bisP (with magnesium ions as cofactor and at pH 9) pH dependence: Optimum pH is between 6 and 7.5.
Sequence caution	The sequence U07867 differs from that shown. Reason: Frameshift at position 217.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	magnesium ion binding Inferred from direct assay Ref.7. Source: EcoliWiki phosphotransferase activity, alcohol group as acceptor Inferred from direct assay PubMed 16889420. Source: EcoliWiki pyridoxal phosphatase activity Inferred from direct assay Ref.7. Source: EcoliWiki sugar-phosphatase activity Inferred from direct assay PubMed 16889420Ref.7. Source: EcoliWiki
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 272	272	Pyridoxal phosphate phosphatase YbhA		PRO_0000054420
Regions
	Region	9 – 11	3	Substrate By similarity
Sites
	Active site	9	1	Nucleophile By similarity
	Metal binding	9	1	Magnesium By similarity
	Metal binding	11	1	Magnesium By similarity
	Metal binding	223	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P21829 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: BB4602AB4D26ACD2	FASTA	272	30,201
	10 20 30 40 50 60 MTTRVIALDL DGTLLTPKKT LLPSSIEALA RAREAGYQLI IVTGRHHVAI HPFYQALALD 70 80 90 100 110 120 TPAICCNGTY LYDYHAKTVL EADPMPVIKA LQLIEMLNEH HIHGLMYVDD AMVYEHPTGH 130 140 150 160 170 180 VIRTSNWAQT LPPEQRPTFT QVASLAETAQ QVNAVWKFAL THDDLPQLQH FGKHVEHELG 190 200 210 220 230 240 LECEWSWHDQ VDIARGGNSK GKRLTKWVEA QGWSMENVVA FGDNFNDISM LEAAGTGVAM 250 260 270 GNADDAVKAR ANIVIGDNTT DSIAQFIYSH LI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli." Maupin-Furlow J.A., Rosentel J.K., Lee J.H., Deppenmeier U., Gunsalus R.P., Shanmugam K.T. J. Bacteriol. 177:4851-4856(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene." Walkenhorst H.M., Hemschemeier S.K., Eichenlaub R. Microbiol. Res. 150:347-361(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / MC1000 / ATCC 39531.
[3]	"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." 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. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." 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. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Enzyme genomics: application of general enzymatic screens to discover new enzymes." Kuznetsova E., Proudfoot M., Sanders S.A., Reinking J., Savchenko A., Arrowsmith C.H., Edwards A.M., Yakunin A.F. FEMS Microbiol. Rev. 29:263-279(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A PHOSPHATASE.
[7]	"Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family." 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. J. Biol. Chem. 281:36149-36161(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS A PHOSPHATASE, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, COFACTOR.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U27192 Genomic DNA. Translation: AAB60177.1. U07867 Genomic DNA. No translation available. U00096 Genomic DNA. Translation: AAC73853.1. AP009048 Genomic DNA. Translation: BAA35430.1.
PIR	F64812.
RefSeq	NP_415287.1. NC_000913.2. YP_489039.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P21829.
SMR	P21829. Positions 2-267.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21829. 3 interactions.
STRING	511145.b0766.
Protocols and materials databases
DNASU	945372.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73853; AAC73853; b0766. BAA35430; BAA35430; BAA35430.
GeneID	12932152. 945372.
KEGG	ecj:Y75_p0739. eco:b0766.
PATRIC	32116733. VBIEscCol129921_0792.
Organism-specific databases
EchoBASE	EB1221.
EcoGene	EG11239. ybhA.
Phylogenomic databases
eggNOG	COG0561.
HOGENOM	HOG000184780.
KO	K07024.
OMA	SHENTTE.
ProtClustDB	PRK10530.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11239-MONOMER. ECOL316407:JW0749-MONOMER. MetaCyc:EG11239-MONOMER.
Gene expression databases
Genevestigator	P21829.
Family and domain databases
Gene3D	3.40.50.1000. 2 hits.
InterPro	IPR023214. HAD-like_dom. IPR006379. HAD-SF_hydro_IIB. IPR000150. Hypothet_cof. [Graphical view]
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR00099. Cof-subfamily. 1 hit. TIGR01484. HAD-SF-IIB. 1 hit.
PROSITE	PS01228. COF_1. 1 hit. PS01229. COF_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

YBHA_ECOLI

Accession

Primary (citable) accession number: P21829

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program