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P63224 (GMHA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoheptose isomerase

EC=5.3.1.28
Alternative name(s):
Sedoheptulose 7-phosphate isomerase
Gene names
Name:gmhA
Synonyms:lpcA, tfrA, yafI
Ordered Locus Names:b0222, JW0212
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length192 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. Ref.7 Ref.10

Catalytic activity

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. Ref.10

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00067

Pathway

Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. Ref.7

Bacterial outer membrane biogenesis; LPS core biosynthesis. Ref.7

Subunit structure

Homotetramer. Ref.10

Subcellular location

Cytoplasm HAMAP-Rule MF_00067.

Miscellaneous

The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate.

Sequence similarities

Belongs to the SIS family. GmhA subfamily.

Contains 1 SIS domain.

Sequence caution

The sequence AAB08644.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192Phosphoheptose isomerase HAMAP-Rule MF_00067
PRO_0000136526

Regions

Domain37 – 192156SIS
Region54 – 552Substrate binding HAMAP-Rule MF_00067
Region93 – 942Substrate binding By similarity
Region119 – 1213Substrate binding By similarity

Sites

Metal binding611Zinc By similarity
Metal binding651Zinc By similarity
Metal binding1721Zinc By similarity
Metal binding1801Zinc By similarity
Binding site611Substrate
Binding site651Substrate By similarity
Binding site1201Substrate
Binding site1241Substrate By similarity
Binding site1691Substrate
Binding site1721Substrate
Binding site1801Substrate

Experimental info

Mutagenesis611H → Q: Almost no effect. Ref.10
Mutagenesis651E → N or Q: No activity. Ref.10
Mutagenesis691R → Q: Almost no effect. Ref.10
Mutagenesis941D → N: No activity. Ref.10
Mutagenesis1201T → A: No activity. Ref.10
Mutagenesis1691D → N: No activity. Ref.10
Mutagenesis1721Q → E: No activity. Ref.10
Mutagenesis1801H → Q: No activity. Ref.10

Secondary structure

............................... 192
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63224 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: 7A2C05E1079108B4

FASTA19220,815
        10         20         30         40         50         60 
MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC GNGGSHCDAM 

        70         80         90        100        110        120 
HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI FSRYVEAVGR EGDVLLGIST 

       130        140        150        160        170        180 
SGNSANVIKA IAAAREKGMK VITLTGKDGG KMAGTADIEI RVPHFGYADR IQEIHIKVIH 

       190 
ILIQLIEKEM VK 

« Hide

References

« Hide 'large scale' references
[1]"Biosynthesis of inner core lipopolysaccharide in enteric bacteria identification and characterization of a conserved phosphoheptose isomerase."
Brooke J.S., Valvano M.A.
J. Biol. Chem. 271:3608-3614(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]"dinP, a new gene in Escherichia coli, whose product shows similarities to UmuC and its homologues."
Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.
Mutat. Res. 347:1-7(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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.
[4]"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.
[5]"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 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[6]"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.
[7]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, ADP-L-GLYCERO-BETA-D-MANNO-HEPTOSE BIOSYNTHESIS PATHWAY.
Strain: K12 / DH5-alpha and K12 / MG1655 / ATCC 47076.
[8]"Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides."
Valvano M.A., Messner P., Kosma P.
Microbiology 148:1979-1989(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
[9]"Lipopolysaccharide endotoxins."
Raetz C.R.H., Whitfield C.
Annu. Rev. Biochem. 71:635-700(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: LIPOPOLYSACCHARIDE REVIEW.
[10]"Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antibiotic adjuvants."
Taylor P.L., Blakely K.M., de Leon G.P., Walker J.R., McArthur F., Evdokimova E., Zhang K., Valvano M.A., Wright G.D., Junop M.S.
J. Biol. Chem. 283:2835-2845(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH SEDOHEPTULOSE-7-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF HIS-61; GLU-65; ARG-69; ASP-94; THR-120; ASP-169; GLN-172 AND HIS-180.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32590 Genomic DNA. Translation: AAC43630.1.
D38582 Genomic DNA. Translation: BAA07584.1.
U70214 Genomic DNA. Translation: AAB08644.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73326.1.
AP009048 Genomic DNA. Translation: BAA77892.1.
PIRG64746.
RefSeqNP_414757.1. NC_000913.3.
YP_488519.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I22X-ray2.80A/B/C/D1-192[»]
2I2WX-ray1.95A/B/C/D1-192[»]
ProteinModelPortalP63224.
SMRP63224. Positions 1-192.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48179N.
STRING511145.b0222.

Proteomic databases

PaxDbP63224.
PRIDEP63224.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73326; AAC73326; b0222.
BAA77892; BAA77892; BAA77892.
GeneID12934376.
949134.
KEGGecj:Y75_p0213.
eco:b0222.
PATRIC32115559. VBIEscCol129921_0224.

Organism-specific databases

EchoBASEEB2940.
EcoGeneEG13146. gmhA.

Phylogenomic databases

eggNOGCOG0279.
HOGENOMHOG000237571.
KOK03271.
OMAHVFSRYV.
OrthoDBEOG6384PC.
PhylomeDBP63224.

Enzyme and pathway databases

BioCycEcoCyc:G6106-MONOMER.
ECOL316407:JW0212-MONOMER.
MetaCyc:G6106-MONOMER.
UniPathwayUPA00041; UER00436.
UPA00958.

Gene expression databases

GenevestigatorP63224.

Family and domain databases

HAMAPMF_00067. GmhA.
InterProIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamPF13580. SIS_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00441. gmhA. 1 hit.
PROSITEPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63224.
PROP63224.

Entry information

Entry nameGMHA_ECOLI
AccessionPrimary (citable) accession number: P63224
Secondary accession number(s): P51001
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: July 9, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

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