GMHA2_CAMJE
ID GMHA2_CAMJE Reviewed; 201 AA.
AC Q9PMN3; Q0P8J0;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Phosphoheptose isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00067};
DE EC=5.3.1.28 {ECO:0000255|HAMAP-Rule:MF_00067, ECO:0000269|PubMed:31449400};
DE AltName: Full=Sedoheptulose 7-phosphate isomerase 2 {ECO:0000255|HAMAP-Rule:MF_00067};
GN Name=gmhA2 {ECO:0000255|HAMAP-Rule:MF_00067}; OrderedLocusNames=Cj1424c;
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 [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 [2]
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 [3]
RP CAPSULAR POLYSACCHARIDE.
RX PubMed=10672176; DOI=10.1046/j.1365-2958.2000.01717.x;
RA Karlyshev A.V., Linton D., Gregson N.A., Lastovica A.J., Wren B.W.;
RT "Genetic and biochemical evidence of a Campylobacter jejuni capsular
RT polysaccharide that accounts for Penner serotype specificity.";
RL Mol. Microbiol. 35:529-541(2000).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:31449400};
RX PubMed=31449400; DOI=10.1021/acs.biochem.9b00548;
RA Huddleston J.P., Raushel F.M.;
RT "Biosynthesis of GDP-d-glycero-alpha-d-manno-heptose for the Capsular
RT Polysaccharide of Campylobacter jejuni.";
RL Biochemistry 58:3893-3902(2019).
CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC D-glycero-D-manno-heptose 7-phosphate. No activity with L-galacto-
CC heptulose, L-galacto-heptulose 7-phosphate or D-manno-heptulose.
CC {ECO:0000269|PubMed:31449400}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00067, ECO:0000269|PubMed:31449400};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00067};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00067};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=320 uM for D-sedoheptulose 7-phosphate (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:31449400};
CC Note=kcat is 0.14 sec(-1) for D-sedoheptulose 7-phosphate.
CC {ECO:0000269|PubMed:31449400};
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. {ECO:0000255|HAMAP-Rule:MF_00067,
CC ECO:0000269|PubMed:31449400}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000305|PubMed:31449400}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}.
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:0000255|HAMAP-Rule:MF_00067}.
CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00067}.
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DR EMBL; AL111168; CAL35533.1; -; Genomic_DNA.
DR PIR; H81287; H81287.
DR RefSeq; WP_002857991.1; NC_002163.1.
DR RefSeq; YP_002344807.1; NC_002163.1.
DR AlphaFoldDB; Q9PMN3; -.
DR SMR; Q9PMN3; -.
DR IntAct; Q9PMN3; 2.
DR STRING; 192222.Cj1424c; -.
DR PaxDb; Q9PMN3; -.
DR PRIDE; Q9PMN3; -.
DR EnsemblBacteria; CAL35533; CAL35533; Cj1424c.
DR GeneID; 905713; -.
DR KEGG; cje:Cj1424c; -.
DR PATRIC; fig|192222.6.peg.1405; -.
DR eggNOG; COG0279; Bacteria.
DR HOGENOM; CLU_080999_4_0_7; -.
DR OMA; TAHSNDY; -.
DR BRENDA; 5.3.1.28; 1087.
DR UniPathway; UPA00041; UER00436.
DR UniPathway; UPA00934; -.
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; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IC:UniProtKB.
DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IDA:UniProtKB.
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 PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Carbohydrate metabolism; Cytoplasm;
KW Isomerase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..201
FT /note="Phosphoheptose isomerase 2"
FT /id="PRO_0000136523"
FT DOMAIN 39..198
FT /note="SIS"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 54..56
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 96..97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 122..124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00067"
SQ SEQUENCE 201 AA; 21653 MW; E99EAD00B36DEF99 CRC64;
MENLNSYIKG HFADSILVKE QILKDENLIT LIKNASLEVI KAYKNGNKTL LAGNGGSAAD
AQHIAGEFVS RFYFDRPGIA SIALTTDTSI LTAIGNDYGY ENLFARQVQA QGVKGDVFIG
ISTSGNSKNI LKALEFCKQK EIISIGLSGA SGGAMNELCD YCIKVPSTCT PRIQEAHILI
GHIICAIVEE ELFGKGFSCK Q
