P75792 (SUPH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sugar phosphatase YbiV
EC=3.1.3.23

Gene names

Name:	ybiV
Synonyms:	supH
Ordered Locus Names:	b0822, JW0806

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	271 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the hydrolysis of sugar phosphate to sugar and inorganic phosphate. Has a wide substrate specificity catalyzing the hydrolysis of fructose-1-phosphate (Fru1P) most efficiently, but it remains uncertain if this is the real substrate in vivo. Appears to have a low level of phosphotransferase activity using monophosphates as the phosphate donor. Ref.4 Ref.5 Ref.6
Catalytic activity	Sugar phosphate + H2O = sugar + phosphate.
Cofactor	Magnesium. Can also use other divalent metal cations as manganese, cobalt and zinc. Ref.5
Subunit structure	Homodimer. Ref.6 Ref.7
Induction	Regulated by the cAMP receptor protein crp Potential.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. Cof family. SupH subfamily.
Biophysicochemical properties	Kinetic parameters: Glucose-6-phosphate is also a good substrate with a relative activity of 62.5% versus the activity with ribose-5-phosphate. KM=0.12 mM for imido-di-phosphate (with magnesium ions as cofactor and at pH 9) Ref.5 KM=1.4 mM for Fru1P (with magnesium ions as cofactor and at pH 9) KM=2.4 mM for ribose-5-phosphate (with magnesium ions as cofactor and at pH 9) KM=3.1 mM for glucose-6-phosphate (with magnesium ions as cofactor and at pH 9) KM=4.9 mM for acetyl-phosphate (with magnesium ions as cofactor and at pH 9) KM=6 mM for ribose-5-phosphate (at pH 5.4) KM=6 mM for glycerol-1-phosphate (at pH 5.4) KM=4.5 mM for glycerol-2-phosphate (at pH 5.4)

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	magnesium ion binding Inferred from direct assay Ref.5. Source: UniProtKB sugar-phosphatase activity Inferred from direct assay Ref.5. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 271

271

Sugar phosphatase YbiV

PRO_0000054421

Regions

Region

9 – 11

3

Substrate By similarity

Region

44 – 46

3

Substrate binding

Sites

Active site

9

1

Nucleophile

Metal binding

9

1

Magnesium

Metal binding

11

1

Magnesium

Metal binding

215

1

Magnesium

Metal binding

216

1

Magnesium

Binding site

192

1

Substrate

Secondary structure

1

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271

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Helix

10 – 14

5

Helix

23 – 36

14

Beta strand

39 – 43

5

Helix

48 – 51

4

Helix

52 – 54

3

Turn

56 – 61

6

Beta strand

62 – 66

5

Helix

67 – 69

3

Beta strand

71 – 74

4

Beta strand

77 – 81

5

Helix

86 – 97

12

Beta strand

103 – 110

8

Beta strand

112 – 115

4

Helix

120 – 127

8

Beta strand

131 – 137

7

Helix

139 – 141

3

Beta strand

146 – 152

7

Helix

155 – 157

3

Helix

158 – 168

11

Turn

169 – 171

3

Beta strand

172 – 177

6

Beta strand

182 – 186

5

Helix

192 – 203

12

Helix

207 – 209

3

Beta strand

210 – 214

5

Helix

217 – 219

3

Helix

220 – 225

6

Beta strand

227 – 231

5

Helix

237 – 242

6

Beta strand

244 – 246

3

Helix

250 – 252

3

Helix

254 – 264

11

Sequences

	Sequence		Length	Mass (Da)
	P75792 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: F8733636B422A9A9	FASTA	271	30,413
	10 20 30 40 50 60 MSVKVIVTDM DGTFLNDAKT YNQPRFMAQY QELKKRGIKF VVASGNQYYQ LISFFPELKD 70 80 90 100 110 120 EISFVAENGA LVYEHGKQLF HGELTRHESR IVIGELLKDK QLNFVACGLQ SAYVSENAPE 130 140 150 160 170 180 AFVALMAKHY HRLKPVKDYQ EIDDVLFKFS LNLPDEQIPL VIDKLHVALD GIMKPVTSGF 190 200 210 220 230 240 GFIDLIIPGL HKANGISRLL KRWDLSPQNV VAIGDSGNDA EMLKMARYSF AMGNAAENIK 250 260 270 QIARYATDDN NHEGALNVIQ AVLDNTSPFN S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"Ybiv from Escherichia coli K12 is a HAD phosphatase." Roberts A., Lee S.-Y., McCullagh E., Silversmith R.E., Wemmer D.E. Proteins 58:790-801(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND OF COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION AS A PHOSPHATASE, SUBUNIT. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Domain shifting confirms monomeric structure of Escherichia coli sugar phosphatase suph." New York structural genomix research consortium (NYSGXRC) Submitted (JUL-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-271, SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC73909.1.
AP009048 Genomic DNA. Translation: BAA35503.1.

PIR

F64819.

RefSeq

NP_415343.1. NC_000913.2.
YP_489095.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RLM	X-ray	1.90	A/B/C/D	3-271	[»]
1RLO	X-ray	2.00	A/B/C/D	3-271	[»]
1RLT	X-ray	2.20	A/B/C/D	3-271	[»]
2HF2	X-ray	1.90	A/B	2-271	[»]

ProteinModelPortal

P75792.

SMR

P75792. Positions 1-270.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-11441N.

IntAct

P75792. 10 interactions.

STRING

511145.b0822.

Proteomic databases

PaxDb

P75792.

PRIDE

P75792.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73909; AAC73909; b0822.
BAA35503; BAA35503; BAA35503.

GeneID

12934001.
945432.

KEGG

ecj:Y75_p0795.
eco:b0822.

PATRIC

32116847. VBIEscCol129921_0849.

Organism-specific databases

EchoBASE

EB3111.

EcoGene

EG13327. supH.

Phylogenomic databases

eggNOG

COG0561.

HOGENOM

HOG000184782.

KO

K07757.

OMA

SFFPEIR.

ProtClustDB

CLSK879776.

Enzyme and pathway databases

BioCyc

EcoCyc:G6425-MONOMER.
ECOL316407:JW0806-MONOMER.
MetaCyc:G6425-MONOMER.

Gene expression databases

Genevestigator

P75792.

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

PF08282. Hydrolase_3. 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. False negative.
PS01229. COF_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P75792.

Entry information

Entry name

SUPH_ECOLI

Accession

Primary (citable) accession number: P75792

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program