GMHA_ECOLI
ID GMHA_ECOLI Reviewed; 192 AA.
AC P63224; P51001;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Phosphoheptose isomerase;
DE EC=5.3.1.28;
DE AltName: Full=Sedoheptulose 7-phosphate isomerase;
GN Name=gmhA; Synonyms=lpcA, tfrA, yafI; OrderedLocusNames=b0222, JW0212;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8631969; DOI=10.1074/jbc.271.7.3608;
RA Brooke J.S., Valvano M.A.;
RT "Biosynthesis of inner core lipopolysaccharide in enteric bacteria
RT identification and characterization of a conserved phosphoheptose
RT isomerase.";
RL J. Biol. Chem. 271:3608-3614(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=7596361; DOI=10.1016/0165-7992(95)90024-1;
RA Ohmori H., Hatada E., Qiao Y., Tsuji M., Fukuda R.;
RT "dinP, a new gene in Escherichia coli, whose product shows similarities to
RT UmuC and its homologues.";
RL Mutat. Res. 347:1-7(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T.,
RA Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S.,
RA Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0
RT - 6.0 min (189,987 - 281,416bp) region.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP FUNCTION, AND ADP-L-GLYCERO-BETA-D-MANNO-HEPTOSE BIOSYNTHESIS PATHWAY.
RC STRAIN=K12 / DH5-alpha, and K12 / MG1655 / ATCC 47076;
RX PubMed=11751812; DOI=10.1128/jb.184.2.363-369.2002;
RA Kneidinger B., Marolda C., Graninger M., Zamyatina A., McArthur F.,
RA Kosma P., Valvano M.A., Messner P.;
RT "Biosynthesis pathway of ADP-L-glycero-beta-D-manno-heptose in Escherichia
RT coli.";
RL J. Bacteriol. 184:363-369(2002).
RN [8]
RP BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE.
RX PubMed=12101286; DOI=10.1099/00221287-148-7-1979;
RA Valvano M.A., Messner P., Kosma P.;
RT "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-
RT heptose precursors of bacterial glycoproteins and cell surface
RT polysaccharides.";
RL Microbiology 148:1979-1989(2002).
RN [9]
RP LIPOPOLYSACCHARIDE REVIEW.
RX PubMed=12045108; DOI=10.1146/annurev.biochem.71.110601.135414;
RA Raetz C.R.H., Whitfield C.;
RT "Lipopolysaccharide endotoxins.";
RL Annu. Rev. Biochem. 71:635-700(2002).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP SEDOHEPTULOSE-7-PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP MUTAGENESIS OF HIS-61; GLU-65; ARG-69; ASP-94; THR-120; ASP-169; GLN-172
RP AND HIS-180.
RX PubMed=18056714; DOI=10.1074/jbc.m706163200;
RA Taylor P.L., Blakely K.M., de Leon G.P., Walker J.R., McArthur F.,
RA Evdokimova E., Zhang K., Valvano M.A., Wright G.D., Junop M.S.;
RT "Structure and function of sedoheptulose-7-phosphate isomerase, a critical
RT enzyme for lipopolysaccharide biosynthesis and a target for antibiotic
RT adjuvants.";
RL J. Biol. Chem. 283:2835-2845(2008).
CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC D-glycero-D-manno-heptose 7-phosphate. {ECO:0000269|PubMed:11751812,
CC ECO:0000269|PubMed:18056714}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-
CC heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate;
CC Xref=Rhea:RHEA:27489, ChEBI:CHEBI:57483, ChEBI:CHEBI:60203,
CC ChEBI:CHEBI:60204; EC=5.3.1.28;
CC Evidence={ECO:0000269|PubMed:18056714};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-
CC phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and
CC D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-
CC phosphate: step 1/1.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; LPS core biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:18056714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: The reaction produces a racemic mixture of D-glycero-
CC alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-
CC phosphate.
CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB08644.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U32590; AAC43630.1; -; Genomic_DNA.
DR EMBL; D38582; BAA07584.1; -; Genomic_DNA.
DR EMBL; U70214; AAB08644.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73326.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA77892.1; -; Genomic_DNA.
DR PIR; G64746; G64746.
DR RefSeq; NP_414757.1; NC_000913.3.
DR RefSeq; WP_000284050.1; NZ_STEB01000020.1.
DR PDB; 2I22; X-ray; 2.80 A; A/B/C/D=1-192.
DR PDB; 2I2W; X-ray; 1.95 A; A/B/C/D=1-192.
DR PDBsum; 2I22; -.
DR PDBsum; 2I2W; -.
DR AlphaFoldDB; P63224; -.
DR SMR; P63224; -.
DR BioGRID; 4263370; 277.
DR DIP; DIP-48179N; -.
DR STRING; 511145.b0222; -.
DR jPOST; P63224; -.
DR PaxDb; P63224; -.
DR PRIDE; P63224; -.
DR EnsemblBacteria; AAC73326; AAC73326; b0222.
DR EnsemblBacteria; BAA77892; BAA77892; BAA77892.
DR GeneID; 66671459; -.
DR GeneID; 949134; -.
DR KEGG; ecj:JW0212; -.
DR KEGG; eco:b0222; -.
DR PATRIC; fig|1411691.4.peg.2061; -.
DR EchoBASE; EB2940; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_4_0_6; -.
DR InParanoid; P63224; -.
DR OMA; FLAHKEA; -.
DR PhylomeDB; P63224; -.
DR BioCyc; EcoCyc:G6106-MON; -.
DR BioCyc; MetaCyc:G6106-MON; -.
DR BRENDA; 5.3.1.28; 2026.
DR UniPathway; UPA00041; UER00436.
DR UniPathway; UPA00958; -.
DR EvolutionaryTrace; P63224; -.
DR PRO; PR:P63224; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; ISS:EcoCyc.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IDA:EcoCyc.
DR GO; GO:0009244; P:lipopolysaccharide core region biosynthetic process; IMP:EcoCyc.
DR CDD; cd05006; SIS_GmhA; 1.
DR HAMAP; MF_00067; GmhA; 1.
DR InterPro; IPR035461; GmhA/DiaA.
DR InterPro; IPR004515; Phosphoheptose_Isoase.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR TIGRFAMs; TIGR00441; gmhA; 1.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Isomerase;
KW Lipopolysaccharide biosynthesis; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..192
FT /note="Phosphoheptose isomerase"
FT /id="PRO_0000136526"
FT DOMAIN 37..192
FT /note="SIS"
FT BINDING 54..55
FT /ligand="substrate"
FT BINDING 61
FT /ligand="substrate"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 93..94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119..121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="substrate"
FT BINDING 172
FT /ligand="substrate"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MUTAGEN 61
FT /note="H->Q: Almost no effect."
FT /evidence="ECO:0000269|PubMed:18056714"
FT MUTAGEN 65
FT /note="E->N,Q: No activity."
FT /evidence="ECO:0000269|PubMed:18056714"
FT MUTAGEN 69
FT /note="R->Q: Almost no effect."
FT /evidence="ECO:0000269|PubMed:18056714"
FT MUTAGEN 94
FT /note="D->N: No activity."
FT /evidence="ECO:0000269|PubMed:18056714"
FT MUTAGEN 120
FT /note="T->A: No activity."
FT /evidence="ECO:0000269|PubMed:18056714"
FT MUTAGEN 169
FT /note="D->N: No activity."
FT /evidence="ECO:0000269|PubMed:18056714"
FT MUTAGEN 172
FT /note="Q->E: No activity."
FT /evidence="ECO:0000269|PubMed:18056714"
FT MUTAGEN 180
FT /note="H->Q: No activity."
FT /evidence="ECO:0000269|PubMed:18056714"
FT HELIX 3..22
FT /evidence="ECO:0007829|PDB:2I2W"
FT HELIX 24..42
FT /evidence="ECO:0007829|PDB:2I2W"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:2I2W"
FT HELIX 54..70
FT /evidence="ECO:0007829|PDB:2I2W"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2I2W"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:2I2W"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2I2W"
FT HELIX 100..108
FT /evidence="ECO:0007829|PDB:2I2W"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2I2W"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:2I2W"
FT HELIX 125..137
FT /evidence="ECO:0007829|PDB:2I2W"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:2I2W"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2I2W"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2I2W"
FT HELIX 168..191
FT /evidence="ECO:0007829|PDB:2I2W"
SQ SEQUENCE 192 AA; 20815 MW; 7A2C05E1079108B4 CRC64;
MYQDLIRNEL NEAAETLANF LKDDANIHAI QRAAVLLADS FKAGGKVLSC GNGGSHCDAM
HFAEELTGRY RENRPGYPAI AISDVSHISC VGNDFGFNDI FSRYVEAVGR EGDVLLGIST
SGNSANVIKA IAAAREKGMK VITLTGKDGG KMAGTADIEI RVPHFGYADR IQEIHIKVIH
ILIQLIEKEM VK
