GMHA1_CAMJE
ID GMHA1_CAMJE Reviewed; 186 AA.
AC Q9PNE6; Q0P9A7; Q6TG10; Q7BPS4;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Phosphoheptose isomerase 1;
DE EC=5.3.1.28;
DE AltName: Full=Sedoheptulose 7-phosphate isomerase 1;
GN Name=gmhA1; Synonyms=gmhA; OrderedLocusNames=Cj1149c;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43446 / MK104 / Serotype O:19;
RA Gilbert M.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GB11;
RX PubMed=14742567; DOI=10.1128/iai.72.2.1162-1165.2004;
RA Gilbert M., Godschalk P.C., Karwaski M.-F., Ang C.W., Van Belkum A., Li J.,
RA Wakarchuk W.W., Endtz H.P.;
RT "Evidence for acquisition of the lipooligosaccharide biosynthesis locus in
RT Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-
RT Barre syndrome, by horizontal exchange.";
RL Infect. Immun. 72:1162-1165(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [4]
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 [5]
RP CELL SURFACE.
RX PubMed=11173031; DOI=10.1016/s1369-5274(00)00161-2;
RA Linton D., Karlyshev A.V., Wren B.W.;
RT "Deciphering Campylobacter jejuni cell surface interactions from the genome
RT sequence.";
RL Curr. Opin. Microbiol. 4:35-40(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-186.
RX PubMed=16477602; DOI=10.1002/prot.20908;
RA Seetharaman J., Rajashankar K.R., Solorzano V., Kniewel R., Lima C.D.,
RA Bonanno J.B., Burley S.K., Swaminathan S.;
RT "Crystal structures of two putative phosphoheptose isomerases.";
RL Proteins 63:1092-1096(2006).
CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC D-glycero-D-manno-heptose 7-phosphate. {ECO:0000250}.
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 -!- 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; LOS core biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. {ECO:0000305}.
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DR EMBL; AF167344; AAR99164.1; -; Genomic_DNA.
DR EMBL; AY422197; AAR82882.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35264.1; -; Genomic_DNA.
DR PIR; G81319; G81319.
DR RefSeq; WP_002858021.1; NC_002163.1.
DR RefSeq; YP_002344540.1; NC_002163.1.
DR PDB; 1TK9; X-ray; 2.10 A; A/B/C/D=2-186.
DR PDBsum; 1TK9; -.
DR AlphaFoldDB; Q9PNE6; -.
DR SMR; Q9PNE6; -.
DR IntAct; Q9PNE6; 103.
DR STRING; 192222.Cj1149c; -.
DR PaxDb; Q9PNE6; -.
DR PRIDE; Q9PNE6; -.
DR EnsemblBacteria; CAL35264; CAL35264; Cj1149c.
DR GeneID; 905439; -.
DR KEGG; cje:Cj1149c; -.
DR PATRIC; fig|192222.6.peg.1130; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_4_0_7; -.
DR OMA; FLAHKEA; -.
DR BRENDA; 5.3.1.28; 1087.
DR UniPathway; UPA00041; UER00436.
DR UniPathway; UPA00976; -.
DR EvolutionaryTrace; Q9PNE6; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; Metal-binding;
KW Reference proteome; Zinc.
FT CHAIN 1..186
FT /note="Phosphoheptose isomerase 1"
FT /id="PRO_0000136522"
FT DOMAIN 33..186
FT /note="SIS"
FT BINDING 48..50
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 90..91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 116..118
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 16
FT /note="V -> A (in Ref. 2; AAR82882)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="A -> E (in Ref. 1; AAR99164 and 2; AAR82882)"
FT /evidence="ECO:0000305"
FT CONFLICT 31
FT /note="E -> D (in Ref. 1; AAR99164)"
FT /evidence="ECO:0000305"
FT CONFLICT 109
FT /note="K -> N (in Ref. 1; AAR99164 and 2; AAR82882)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="L -> F (in Ref. 1; AAR99164 and 2; AAR82882)"
FT /evidence="ECO:0000305"
FT HELIX 2..18
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 19..22
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:1TK9"
FT STRAND 43..48
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 50..63
FT /evidence="ECO:0007829|PDB:1TK9"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1TK9"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:1TK9"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:1TK9"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 122..133
FT /evidence="ECO:0007829|PDB:1TK9"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 149..152
FT /evidence="ECO:0007829|PDB:1TK9"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:1TK9"
FT HELIX 164..185
FT /evidence="ECO:0007829|PDB:1TK9"
SQ SEQUENCE 186 AA; 20085 MW; D7759471EC88924D CRC64;
MINLVEKEWQ EHQKIVQASE ILKGQIAKVG ELLCECLKKG GKILICGNGG SAADAQHFAA
ELSGRYKKER KALAGIALTT DTSALSAIGN DYGFEFVFSR QVEALGNEKD VLIGISTSGK
SPNVLEALKK AKELNMLCLG LSGKGGGMMN KLCDHNLVVP SDDTARIQEM HILIIHTLCQ
IIDESF
