GMHA_PSEAE
ID GMHA_PSEAE Reviewed; 197 AA.
AC Q9HVZ0;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Phosphoheptose isomerase;
DE EC=5.3.1.28;
DE AltName: Full=Sedoheptulose 7-phosphate isomerase;
GN Name=gmhA; OrderedLocusNames=PA4425;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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 X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP D-GLYCERO-ALPHA-D-MANNO-HEPTOSE 7-PHOSPHATE.
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: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; LPS 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; AE004091; AAG07813.1; -; Genomic_DNA.
DR PIR; A83092; A83092.
DR RefSeq; NP_253115.1; NC_002516.2.
DR RefSeq; WP_003094149.1; NZ_QZGE01000004.1.
DR PDB; 1X92; X-ray; 2.30 A; A/B=1-197.
DR PDB; 3BJZ; X-ray; 2.40 A; A/B/C/D=1-197.
DR PDBsum; 1X92; -.
DR PDBsum; 3BJZ; -.
DR AlphaFoldDB; Q9HVZ0; -.
DR SMR; Q9HVZ0; -.
DR STRING; 287.DR97_1603; -.
DR DrugBank; DB02470; D-Glycero-D-Mannopyranose-7-Phosphate.
DR PaxDb; Q9HVZ0; -.
DR PRIDE; Q9HVZ0; -.
DR DNASU; 881196; -.
DR EnsemblBacteria; AAG07813; AAG07813; PA4425.
DR GeneID; 881196; -.
DR KEGG; pae:PA4425; -.
DR PATRIC; fig|208964.12.peg.4634; -.
DR PseudoCAP; PA4425; -.
DR HOGENOM; CLU_080999_3_1_6; -.
DR InParanoid; Q9HVZ0; -.
DR OMA; DVHICVP; -.
DR PhylomeDB; Q9HVZ0; -.
DR BioCyc; PAER208964:G1FZ6-4513-MON; -.
DR BRENDA; 5.3.1.28; 5087.
DR UniPathway; UPA00041; UER00436.
DR UniPathway; UPA00958; -.
DR EvolutionaryTrace; Q9HVZ0; -.
DR Proteomes; UP000002438; 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:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009244; P:lipopolysaccharide core region 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 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..197
FT /note="Phosphoheptose isomerase"
FT /id="PRO_0000136542"
FT DOMAIN 36..197
FT /note="SIS"
FT BINDING 51..53
FT /ligand="substrate"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="substrate"
FT BINDING 64
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 BINDING 124
FT /ligand="substrate"
FT BINDING 174
FT /ligand="substrate"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:1X92"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:1X92"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1X92"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 85..94
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 102..108
FT /evidence="ECO:0007829|PDB:1X92"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:1X92"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 125..136
FT /evidence="ECO:0007829|PDB:1X92"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:1X92"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:1X92"
FT HELIX 170..193
FT /evidence="ECO:0007829|PDB:1X92"
SQ SEQUENCE 197 AA; 21413 MW; CF48D9DF28634BB4 CRC64;
MDMQHRIRQL FQASIETKQQ ALEVLPPYIE QASLVMVNAL LNEGKILSCG NGGSAGDAQH
FSSELLNRFE RERPSLPAVA LTTDSSTITS IANDYSYNEV FSKQIRALGQ PGDVLLAIST
SGNSANVIQA IQAAHDREML VVALTGRDGG GMASLLLPED VEIRVPSKIT ARIQEVHLLA
IHCLCDLIDR QLFGSEE
