GenomeNet

Database: UniProt
Entry: B4S3M4_PROA2
LinkDB: B4S3M4_PROA2
Original site: B4S3M4_PROA2 
ID   B4S3M4_PROA2            Unreviewed;       199 AA.
AC   B4S3M4;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 90.
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   OrderedLocusNames=Paes_1745 {ECO:0000313|EMBL:ACF46763.1};
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF46763.1, ECO:0000313|Proteomes:UP000002725};
RN   [1] {ECO:0000313|EMBL:ACF46763.1, ECO:0000313|Proteomes:UP000002725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001108; ACF46763.1; -; Genomic_DNA.
DR   RefSeq; WP_012506296.1; NC_011059.1.
DR   AlphaFoldDB; B4S3M4; -.
DR   STRING; 290512.Paes_1745; -.
DR   KEGG; paa:Paes_1745; -.
DR   eggNOG; COG0279; Bacteria.
DR   HOGENOM; CLU_080999_4_0_10; -.
DR   OMA; DVHICVP; -.
DR   UniPathway; UPA00041; UER00436.
DR   Proteomes; UP000002725; 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   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}; Reference proteome {ECO:0000313|Proteomes:UP000002725};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00067}.
FT   DOMAIN          38..196
FT                   /note="SIS"
FT                   /evidence="ECO:0000259|PROSITE:PS51464"
FT   BINDING         53..55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         95..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         121..123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         172
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         172
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT   BINDING         180
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
SQ   SEQUENCE   199 AA;  21499 MW;  9D155A99BA12834D CRC64;
     MGILETIKKA ISHSIEVKQD ILEDKELIGE IIKVIDDLIK ALNCGNRIIF AGNGGSAADA
     QHLAAEFVSR FQFDRPGLPA LSLATDTSMI TAIGNDYGYE KLFVRQLEAQ SRKGDVFVGL
     TTSGKSPNIL AAFDACNLLG VTSVALCGLG GDLEDKVDYL IRVPSIHTPR IQESHILIGH
     IICAEVEQQI FSHLAPSQK
//
DBGET integrated database retrieval system