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   27-MAR-2024, entry version 140.
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; Pseudomonadota; 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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 511145-b0222; -.
DR   EnsemblBacteria; AAC73326; AAC73326; b0222.
DR   GeneID; 75205744; -.
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; KDEANIH; -.
DR   OrthoDB; 9810929at2; -.
DR   PhylomeDB; P63224; -.
DR   BioCyc; EcoCyc:G6106-MONOMER; -.
DR   BioCyc; MetaCyc:G6106-MONOMER; -.
DR   BRENDA; 5.3.1.28; 2026.
DR   SABIO-RK; P63224; -.
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:0042802; F:identical protein binding; 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   GO; GO:0051289; P:protein homotetramerization; IDA: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   NCBIfam; TIGR00441; gmhA; 1.
DR   PANTHER; PTHR30390:SF7; PHOSPHOHEPTOSE ISOMERASE; 1.
DR   PANTHER; PTHR30390; SEDOHEPTULOSE 7-PHOSPHATE ISOMERASE / DNAA INITIATOR-ASSOCIATING FACTOR FOR REPLICATION INITIATION; 1.
DR   Pfam; PF13580; SIS_2; 1.
DR   SUPFAM; SSF53697; SIS domain; 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
//