ID A0A1H5SWT4_9RHOO Unreviewed; 350 AA.
AC A0A1H5SWT4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=SAMN05216242_10288 {ECO:0000313|EMBL:SEF54965.1}, Tchl_1200
GN {ECO:0000313|EMBL:APR04059.1};
OS Thauera chlorobenzoica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=96773 {ECO:0000313|EMBL:APR04059.1, ECO:0000313|Proteomes:UP000185739};
RN [1] {ECO:0000313|EMBL:SEF54965.1, ECO:0000313|Proteomes:UP000236741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB-1 {ECO:0000313|EMBL:SEF54965.1,
RC ECO:0000313|Proteomes:UP000236741};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:APR04059.1, ECO:0000313|Proteomes:UP000185739}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3CB1 {ECO:0000313|EMBL:APR04059.1,
RC ECO:0000313|Proteomes:UP000185739};
RA Goris T., Mergelsberg M., Boll M.;
RT "Complete genome sequence of Thauera chlorobenzoica, a Betaproteobacterium
RT degrading haloaromatics anaerobically to CO2 and halides.";
RL Submitted (DEC-2016) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glycero-beta-D-manno-heptose 1-phosphate + H(+) = ADP-
CC D-glycero-beta-D-manno-heptose + diphosphate; Xref=Rhea:RHEA:27465,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59967, ChEBI:CHEBI:61593; EC=2.7.7.70;
CC Evidence={ECO:0000256|ARBA:ARBA00000534};
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}.
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; CP018839; APR04059.1; -; Genomic_DNA.
DR EMBL; FNVJ01000002; SEF54965.1; -; Genomic_DNA.
DR RefSeq; WP_075147595.1; NZ_FNVJ01000002.1.
DR AlphaFoldDB; A0A1H5SWT4; -.
DR STRING; 96773.Tchl_1200; -.
DR KEGG; tcl:Tchl_1200; -.
DR OrthoDB; 9795543at2; -.
DR UniPathway; UPA00041; UER00436.
DR Proteomes; UP000185739; Chromosome.
DR Proteomes; UP000236741; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033786; F:heptose-1-phosphate adenylyltransferase activity; IEA:RHEA.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; 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; cd05006; SIS_GmhA; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00067; GmhA; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR035461; GmhA/DiaA.
DR InterPro; IPR004515; Phosphoheptose_Isoase.
DR InterPro; IPR011914; RfaE_dom_II.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR NCBIfam; TIGR00125; cyt_tran_rel; 1.
DR NCBIfam; TIGR02199; rfaE_dom_II; 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; PF01467; CTP_transf_like; 1.
DR Pfam; PF13580; SIS_2; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00067}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..350
FT /note="Phosphoheptose isomerase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030027893"
FT DOMAIN 32..194
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT BINDING 47..49
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 89..90
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 115..117
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00067"
FT BINDING 167
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"
SQ SEQUENCE 350 AA; 36525 MW; 0202B626101EDE1A CRC64;
MTFIAQYIDK HLAAVAALRA VAPAVAAAAQ CISAAINRGN KLLLCGNGGS AADAQHIAAE
LVGRFVAERR GLPGIALSTD TSILTAVGND YGFDSVFARQ VEALAQPGDV LVGISTSGNS
GNVIAAVGAA RQRGCAVIGL LGRDGGKLRD LVDVAVTIGV AETAHIQECH IMVGHIWCAQ
IDADLAESIP ARGDSRSGVL DEAEAIAAVR AARQAGERVV MTNGCFDILH PGHIEYLEQA
RALGDRLVVA VNDDDSVRRL KGARRPVNAL DHRLRMLAAL GCVDWVVPFA EDTPERLICA
VLPDVLVKGG DYTPEQIAGG DCVRRAGGAV KVLGFVEGHS TSGLIEKIRR
//
