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P63224

- GMHA_ECOLI

UniProt

P63224 - GMHA_ECOLI

Protein

Phosphoheptose isomerase

Gene

gmhA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 85 (01 Oct 2014)
      Sequence version 1 (27 Sep 2004)
      Previous versions | rss
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    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

    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

    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.
    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG13146. gmhA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: EcoCyc

    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 – 2220
    Helixi24 – 4219
    Beta strandi47 – 526
    Helixi54 – 7017
    Beta strandi74 – 763
    Beta strandi78 – 814
    Helixi88 – 914
    Helixi100 – 1089
    Beta strandi114 – 1185
    Beta strandi120 – 1223
    Helixi125 – 13713
    Beta strandi140 – 1467
    Helixi150 – 1523
    Beta strandi156 – 1627
    Helixi168 – 19124

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK03271.
    OMAiHVFSRYV.
    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

    MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC    50
    GNGGSHCDAM HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI 100
    FSRYVEAVGR EGDVLLGIST SGNSANVIKA IAAAREKGMK VITLTGKDGG 150
    KMAGTADIEI RVPHFGYADR IQEIHIKVIH ILIQLIEKEM VK 192
    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.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    PIRi G64746.
    RefSeqi NP_414757.1. NC_000913.3.
    YP_488519.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I22 X-ray 2.80 A/B/C/D 1-192 [» ]
    2I2W X-ray 1.95 A/B/C/D 1-192 [» ]
    ProteinModelPortali P63224.
    SMRi P63224. Positions 1-192.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-48179N.
    STRINGi 511145.b0222.

    Proteomic databases

    PaxDbi P63224.
    PRIDEi P63224.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73326 ; AAC73326 ; b0222 .
    BAA77892 ; BAA77892 ; BAA77892 .
    GeneIDi 12934376.
    949134.
    KEGGi ecj:Y75_p0213.
    eco:b0222.
    PATRICi 32115559. VBIEscCol129921_0224.

    Organism-specific databases

    EchoBASEi EB2940.
    EcoGenei EG13146. gmhA.

    Phylogenomic databases

    eggNOGi COG0279.
    HOGENOMi HOG000237571.
    KOi K03271.
    OMAi HVFSRYV.
    OrthoDBi EOG6384PC.
    PhylomeDBi P63224.

    Enzyme and pathway databases

    UniPathwayi UPA00041 ; UER00436 .
    UPA00958 .
    BioCyci EcoCyc:G6106-MONOMER.
    ECOL316407:JW0212-MONOMER.
    MetaCyc:G6106-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P63224.
    PROi P63224.

    Gene expression databases

    Genevestigatori P63224.

    Family and domain databases

    HAMAPi MF_00067. GmhA.
    InterProi IPR004515. Phosphoheptose_Isoase.
    IPR001347. SIS.
    [Graphical view ]
    Pfami PF13580. SIS_2. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00441. gmhA. 1 hit.
    PROSITEi PS51464. SIS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 85 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