ID X5EMK8_NEIME Unreviewed; 197 AA.
AC X5EMK8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Phosphoheptose isomerase {ECO:0000256|HAMAP-Rule:MF_00067};
DE EC=5.3.1.28 {ECO:0000256|HAMAP-Rule:MF_00067};
DE AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000256|HAMAP-Rule:MF_00067};
GN Name=lpcA {ECO:0000313|EMBL:AHW74671.1};
GN Synonyms=gmhA {ECO:0000256|HAMAP-Rule:MF_00067};
GN ORFNames=NMA510612_0357 {ECO:0000313|EMBL:AHW74671.1};
OS Neisseria meningitidis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487 {ECO:0000313|EMBL:AHW74671.1, ECO:0000313|Proteomes:UP000023582};
RN [1] {ECO:0000313|EMBL:AHW74671.1, ECO:0000313|Proteomes:UP000023582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RX PubMed=24812217;
RA Zhang Y., Yang J., Xu L., Zhu Y., Liu B., Shao Z., Zhang X., Jin Q.;
RT "Complete Genome Sequence of Neisseria meningitidis Serogroup A Strain
RT NMA510612, Isolated from a Patient with Bacterial Meningitis in China.";
RL Genome Announc. 2:e00360-14(2014).
RN [2] {ECO:0000313|Proteomes:UP000023582}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NMA510612 {ECO:0000313|Proteomes:UP000023582};
RA Zhang X., Zhang Y., Yang J., Zhu Y., Jin Q.;
RT "Complete Genome Sequence of Neisseria meningitides, serogroup A strain
RT 510612.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in
CC D-glycero-D-manno-heptose 7-phosphate. {ECO:0000256|ARBA:ARBA00003172,
CC ECO:0000256|HAMAP-Rule:MF_00067}.
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:0000256|ARBA:ARBA00000348, ECO:0000256|HAMAP-
CC Rule:MF_00067};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00067};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00067};
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:0000256|HAMAP-Rule:MF_00067}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00067}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_00067}.
CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily.
CC {ECO:0000256|ARBA:ARBA00009894, ECO:0000256|HAMAP-Rule:MF_00067}.
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DR EMBL; CP007524; AHW74671.1; -; Genomic_DNA.
DR RefSeq; WP_002219976.1; NZ_WSOQ01000034.1.
DR GeneID; 61282479; -.
DR KEGG; nmx:NMA510612_0357; -.
DR PATRIC; fig|487.1144.peg.2356; -.
DR OMA; TDVHICV; -.
DR UniPathway; UPA00041; UER00436.
DR Proteomes; UP000023582; 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 NCBIfam; TIGR00441; gmhA; 1.
DR PANTHER; PTHR30390:SF6; DNAA INITIATOR-ASSOCIATING PROTEIN DIAA; 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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00067};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00067};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00067};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00067}.
FT BINDING 52..54
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 94..95
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 120..122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 183
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
SQ SEQUENCE 197 AA; 20989 MW; FAE0DA549A085280 CRC64;
MTTLQERVAA HFAESIRAKQ EAGKVLVEPT VQAAELMLQC LMNDGKILAC GNGGSAADAQ
HFAAEMTGRF EKERMELAAV ALTTDTSALT AIGNDYGFDH VFSKQVRALG RAGDVLVGIS
TSGNSANVIE AVKAAHERDM HVIALTGRDG GKIAAILKDT DVLLNVPHPR TARIQENHIL
LIHAMCDCID SVLLEGM
//
