D,D-heptose 1,7-bisphosphate phosphatase - Escherichia coli (strain K12)

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P63228 (GMHB_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
D,D-heptose 1,7-bisphosphate phosphatase
EC=3.1.3.-

Alternative name(s):
D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase

Gene names

Name:	gmhB
Synonyms:	yaeD
Ordered Locus Names:	b0200, JW0196

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	191 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position.
Catalytic activity	D-glycero-beta-D-manno-heptose 1,7-bisphosphate + H₂O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate.
Pathway	Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 2/4. Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	This enzyme is insensitive to the anomeric configuration of the D-glycero-D-manno-heptose 1,7-bisphosphate. Phosphatase activity is essential for nucleotide activation (fourth step).
Sequence similarities	Belongs to the gmhB family.
Sequence caution	The sequence BAA03661.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Lipopolysaccharide biosynthesis
Cellular component	Cytoplasm
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lipopolysaccharide core region biosynthetic process Inferred from mutant phenotype Ref.6. Source: EcoCyc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	D,D-heptose 1,7-bisphosphate phosphatase activity Inferred from direct assay. Source: EcoCyc zinc ion binding Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 191

191

D,D-heptose 1,7-bisphosphate phosphatase

PRO_0000209389

Secondary structure

191

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P63228 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: E7814B34A23128FA
Show »

FASTA

191

21,294

        10         20         30         40         50         60 
MAKSVPAIFL DRDGTINVDH GYVHEIDNFE FIDGVIDAMR ELKKMGFALV VVTNQSGIAR 

        70         80         90        100        110        120 
GKFTEAQFET LTEWMDWSLA DRDVDLDGIY YCPHHPQGSV EEFRQVCDCR KPHPGMLLSA 

       130        140        150        160        170        180 
RDYLHIDMAA SYMVGDKLED MQAAVAANVG TKVLVRTGKP ITPEAENAAD WVLNSLADLP 

       190 
QAIKKQQKPA Q

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of 5'flanking region of the ribosomal RNA gene (rrnH) in E. coli." Miyamoto K., Inokuchi H. Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia coli." Kneidinger B., Marolda C., Graninger M., Zamyatina A., McArthur F., Kosma P., Valvano M.A., Messner P. J. Bacteriol. 184:363-369(2002) [PubMed: 11751812] [Abstract] Cited for: CHARACTERIZATION. Strain: K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D15061 Genomic DNA. Translation: BAA03661.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73311.1.
AP009048 Genomic DNA. Translation: BAA77877.1.
U70214 Genomic DNA. Translation: AAB08628.1.

PIR

H64744.

RefSeq

NP_414742.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GMW	X-ray	1.50	A/B	1-191	[»]
3ESQ	X-ray	1.70	A	1-191	[»]
3ESR	X-ray	1.95	A	1-191	[»]
3L1U	X-ray	1.95	A/B	1-191	[»]
3L1V	X-ray	1.95	A/B	1-191	[»]
3L8E	X-ray	1.64	A/B	1-187	[»]
3L8F	X-ray	1.79	A	1-187	[»]
3L8G	X-ray	2.18	A	1-187	[»]

ProteinModelPortal

P63228.

SMR

P63228. Positions 4-187.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47998N.

IntAct

P63228. 7 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001312; EBESCP00000001312; EBESCG00000001087.
EBESCT00000017958; EBESCP00000017249; EBESCG00000017014.

GeneID

944879.

GenomeReviews

Gene locus JW0196 in contig AP009048_GR.
Gene locus b0200 in contig U00096_GR.

KEGG

ecj:JW0196.
eco:b0200.

PATRIC

32115513. VBIEscCol129921_0208.

Organism-specific databases

EchoBASE

EB1687.

EcoGene

EG11736. gmhB.

Phylogenomic databases

eggNOG

COG0241.

GeneTree

EBGT00050000010149.

HOGENOM

HBG613347.

OMA

INIDHGY.

PhylomeDB

P63228.

ProtClustDB

PRK08942.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11736-MONOMER.
MetaCyc:EG11736-MONOMER.

Gene expression databases

Genevestigator

P63228.

Family and domain databases

InterPro

IPR023214. HAD-like_dom.
IPR006549. HAD-SF_hydro_IIIA.
IPR004446. Heptose_bisP_phosphatase.
IPR006543. Histidinol-phos.
IPR013954. PNK3P.
[Graphical view]

Gene3D

G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.

K03273.

Pfam

PF08645. PNK3P. 1 hit.
[Graphical view]

PIRSF

PIRSF004682. GmhB. 1 hit.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR00213. GmhB_yaeD. 1 hit.
TIGR01662. HAD-SF-IIIA. 1 hit.
TIGR01656. Histidinol-ppas. 1 hit.

ProtoNet

Search...

Entry information

Entry name

GMHB_ECOLI

Accession

Primary (citable) accession number: P63228
Secondary accession number(s): P31546

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	September 27, 2004
Last modified:	January 25, 2012
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents