ID A0A0C2Q5K0_9CYAN Unreviewed; 655 AA.
AC A0A0C2Q5K0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 41.
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=gmhA {ECO:0000256|HAMAP-Rule:MF_00067};
GN ORFNames=SD81_24495 {ECO:0000313|EMBL:KIJ75528.1};
OS Tolypothrix campylonemoides VB511288.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1245935 {ECO:0000313|EMBL:KIJ75528.1};
RN [1] {ECO:0000313|EMBL:KIJ75528.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VB511288 {ECO:0000313|EMBL:KIJ75528.1};
RA Tripathy S., Das S., Gupta A., Malar M.C., Adhikary S.P.;
RT "Draft whole genome shotgun sequence of Tolypothrix campylonemoides
RT VB511288.";
RL Submitted (JAN-2015) 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|HAMAP-
CC 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIJ75528.1}.
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DR EMBL; JXCB01000009; KIJ75528.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2Q5K0; -.
DR OrthoDB; 7847955at2; -.
DR UniPathway; UPA00041; UER00436.
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:0016757; F:glycosyltransferase activity; IEA:InterPro.
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; cd03800; GT4_sucrose_synthase; 1.
DR CDD; cd05006; SIS_GmhA; 1.
DR Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR HAMAP; MF_00067; GmhA; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR028098; Glyco_trans_4-like_N.
DR InterPro; IPR035461; GmhA/DiaA.
DR InterPro; IPR004515; Phosphoheptose_Isoase.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR PANTHER; PTHR30390; SEDOHEPTULOSE 7-PHOSPHATE ISOMERASE / DNAA INITIATOR-ASSOCIATING FACTOR FOR REPLICATION INITIATION; 1.
DR Pfam; PF13439; Glyco_transf_4; 1.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 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 DOMAIN 471..627
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT BINDING 486..488
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 499
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 529..530
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 555..557
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 560
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 607
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 607
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
SQ SEQUENCE 655 AA; 72799 MW; BCB17FA451FDAE78 CRC64;
MTKSIALISE HASPLGTFGG ADSGGQNVYV GQIAKHLAIA GYKVDVFTRR DSQELPEIIQ
WIDGVRIINV PAGLPTYIRK EDMLPYMEEF TAYVLNFCQN PWSFQSKAHK KYDLIHANFW
MSALVAAEIK QVLGIPFVVT FHALGRVRRF WQGEADEFPD ERFIIEDRIV AEADHIIAEC
PQDEEDLLRL YHAKKEKITI IPCGFDASEF WQVDKTKARK TLGLPPDERL ILQLGRLVPR
KGVDTVIRAF GRLLQQYDIQ ARLLIVGGES EEPDPHLTPE IARLQTIAIE EGVESQVTFV
GRRSREMVKY YYCAADVFVT TPWYEPFGIT PLEAMACGTP VIGSHVGGIK YTVKDSETGY
LVPPNQPEAI AERIAYLYKN PEVHKRLSHN AIQRVNHLFT WQKVTNSVAS LYEKVLKDKQ
KPIFLSPPAF PTPVVSSSLT FVDDSFAAAI AAMEKSRQTL KSAIVEAAEA LFTCFALGGK
VLVCGNGGSA ADAQHFAAEF VGKLRCSKRA GLPVMALSAD TAFLTAWAND AGYEYVFSRQ
VETFAQSGDL LLGISTSGRS PNMIEAFKTA RHCHINTIAL VGGDGGELLP LADLAVVVPA
TDTQRIQEVQ HLVLHLLCEL VEKRVGKKEE GERGRVGEWE RQRVPNGNHQ FYQLG
//
