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Protein

Phosphoheptose isomerase

Gene

gmhA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate.2 Publications

Catalytic activityi

D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate.1 Publication

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi61 – 611ZincBy similarity
Binding sitei61 – 611Substrate
Metal bindingi65 – 651ZincBy similarity
Binding sitei65 – 651SubstrateBy similarity
Binding sitei120 – 1201Substrate
Binding sitei124 – 1241SubstrateBy similarity
Binding sitei169 – 1691Substrate
Metal bindingi172 – 1721ZincBy similarity
Binding sitei172 – 1721Substrate
Metal bindingi180 – 1801ZincBy similarity
Binding sitei180 – 1801Substrate

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. D-sedoheptulose 7-phosphate isomerase activity Source: EcoCyc
  3. zinc ion binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-glycero-D-manno-heptose 7-phosphate biosynthetic process Source: UniProtKB-UniPathway
  2. lipopolysaccharide core region biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Lipopolysaccharide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:G6106-MONOMER.
ECOL316407:JW0212-MONOMER.
MetaCyc:G6106-MONOMER.
BRENDAi5.3.1.28. 2026.
UniPathwayiUPA00041; UER00436.
UPA00958.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoheptose isomerase (EC:5.3.1.28)
Alternative name(s):
Sedoheptulose 7-phosphate isomerase
Gene namesi
Name:gmhA
Synonyms:lpcA, tfrA, yafI
Ordered Locus Names:b0222, JW0212
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13146. gmhA.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611H → Q: Almost no effect. 1 Publication
Mutagenesisi65 – 651E → N or Q: No activity. 1 Publication
Mutagenesisi69 – 691R → Q: Almost no effect. 1 Publication
Mutagenesisi94 – 941D → N: No activity. 1 Publication
Mutagenesisi120 – 1201T → A: No activity. 1 Publication
Mutagenesisi169 – 1691D → N: No activity. 1 Publication
Mutagenesisi172 – 1721Q → E: No activity. 1 Publication
Mutagenesisi180 – 1801H → Q: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192Phosphoheptose isomerasePRO_0000136526Add
BLAST

Proteomic databases

PaxDbiP63224.
PRIDEiP63224.

Expressioni

Gene expression databases

GenevestigatoriP63224.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-48179N.
STRINGi511145.b0222.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 2220Combined sources
Helixi24 – 4219Combined sources
Beta strandi47 – 526Combined sources
Helixi54 – 7017Combined sources
Beta strandi74 – 763Combined sources
Beta strandi78 – 814Combined sources
Helixi88 – 914Combined sources
Helixi100 – 1089Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi120 – 1223Combined sources
Helixi125 – 13713Combined sources
Beta strandi140 – 1467Combined sources
Helixi150 – 1523Combined sources
Beta strandi156 – 1627Combined sources
Helixi168 – 19124Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I22X-ray2.80A/B/C/D1-192[»]
2I2WX-ray1.95A/B/C/D1-192[»]
ProteinModelPortaliP63224.
SMRiP63224. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63224.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 192156SISAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni54 – 552Substrate binding
Regioni93 – 942Substrate bindingBy similarity
Regioni119 – 1213Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the SIS family. GmhA subfamily.Curated
Contains 1 SIS domain.Curated

Phylogenomic databases

eggNOGiCOG0279.
HOGENOMiHOG000237571.
InParanoidiP63224.
KOiK03271.
OMAiGVKNDVL.
OrthoDBiEOG6384PC.
PhylomeDBiP63224.

Family and domain databases

HAMAPiMF_00067. GmhA.
InterProiIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamiPF13580. SIS_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00441. gmhA. 1 hit.
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63224-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC
60 70 80 90 100
GNGGSHCDAM HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI
110 120 130 140 150
FSRYVEAVGR EGDVLLGIST SGNSANVIKA IAAAREKGMK VITLTGKDGG
160 170 180 190
KMAGTADIEI RVPHFGYADR IQEIHIKVIH ILIQLIEKEM VK
Length:192
Mass (Da):20,815
Last modified:September 27, 2004 - v1
Checksum:i7A2C05E1079108B4
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG64746.
RefSeqiNP_414757.1. NC_000913.3.
YP_488519.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC73326; AAC73326; b0222.
BAA77892; BAA77892; BAA77892.
GeneIDi12934376.
949134.
KEGGiecj:Y75_p0213.
eco:b0222.
PATRICi32115559. VBIEscCol129921_0224.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiG64746.
RefSeqiNP_414757.1. NC_000913.3.
YP_488519.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2I22X-ray2.80A/B/C/D1-192[»]
2I2WX-ray1.95A/B/C/D1-192[»]
ProteinModelPortaliP63224.
SMRiP63224. Positions 1-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-48179N.
STRINGi511145.b0222.

Proteomic databases

PaxDbiP63224.
PRIDEiP63224.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73326; AAC73326; b0222.
BAA77892; BAA77892; BAA77892.
GeneIDi12934376.
949134.
KEGGiecj:Y75_p0213.
eco:b0222.
PATRICi32115559. VBIEscCol129921_0224.

Organism-specific databases

EchoBASEiEB2940.
EcoGeneiEG13146. gmhA.

Phylogenomic databases

eggNOGiCOG0279.
HOGENOMiHOG000237571.
InParanoidiP63224.
KOiK03271.
OMAiGVKNDVL.
OrthoDBiEOG6384PC.
PhylomeDBiP63224.

Enzyme and pathway databases

UniPathwayiUPA00041; UER00436.
UPA00958.
BioCyciEcoCyc:G6106-MONOMER.
ECOL316407:JW0212-MONOMER.
MetaCyc:G6106-MONOMER.
BRENDAi5.3.1.28. 2026.

Miscellaneous databases

EvolutionaryTraceiP63224.
PROiP63224.

Gene expression databases

GenevestigatoriP63224.

Family and domain databases

HAMAPiMF_00067. GmhA.
InterProiIPR004515. Phosphoheptose_Isoase.
IPR001347. SIS.
[Graphical view]
PfamiPF13580. SIS_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00441. gmhA. 1 hit.
PROSITEiPS51464. SIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiGMHA_ECOLI
AccessioniPrimary (citable) accession number: P63224
Secondary accession number(s): P51001
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: April 1, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.