GUTQ_SALTI
ID GUTQ_SALTI Reviewed; 321 AA.
AC Q8Z4C7; Q7C7R3;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Arabinose 5-phosphate isomerase GutQ;
DE Short=API;
DE Short=G-API;
DE EC=5.3.1.13;
DE AltName: Full=Phosphosugar aldol-ketol isomerase;
GN Name=gutQ; OrderedLocusNames=STY2960, t2740;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Catalyzes the reversible aldol-ketol isomerization between D-
CC ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It is
CC also able of sustaining the biosynthetic pathway of 3-deoxy-D-manno-
CC octulosonate (KDO), a unique 8-carbon sugar component of
CC lipopolysaccharides (LPSs) (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-arabinose 5-phosphate = D-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:23104, ChEBI:CHEBI:57693, ChEBI:CHEBI:58121;
CC EC=5.3.1.13;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
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DR EMBL; AE014613; AAO70301.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD05945.1; -; Genomic_DNA.
DR RefSeq; NP_457232.1; NC_003198.1.
DR RefSeq; WP_001278206.1; NZ_WSUR01000005.1.
DR AlphaFoldDB; Q8Z4C7; -.
DR SMR; Q8Z4C7; -.
DR STRING; 220341.16503916; -.
DR EnsemblBacteria; AAO70301; AAO70301; t2740.
DR KEGG; stt:t2740; -.
DR KEGG; sty:STY2960; -.
DR PATRIC; fig|220341.7.peg.3014; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_6; -.
DR OMA; MPRVITP; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; Chromosome.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; ISS:UniProtKB.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR004800; KdsD/KpsF-type.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR035474; SIS_Kpsf.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR TIGRFAMs; TIGR00393; kpsF; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW ATP-binding; CBS domain; Isomerase; Lipopolysaccharide biosynthesis;
KW Metal-binding; Nucleotide-binding; Repeat; Zinc.
FT CHAIN 1..321
FT /note="Arabinose 5-phosphate isomerase GutQ"
FT /id="PRO_0000410939"
FT DOMAIN 34..177
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 203..261
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 269..321
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 49..54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 68..69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 107..116
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141..143
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 52
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 104
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 145
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 186
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
SQ SEQUENCE 321 AA; 34119 MW; 55E1097D3E28A068 CRC64;
MSDALLNAGR QTLMLELQEA SRLPERLGDD FVRAANIIIH CEGKVIVSGI GKSGHIGKKI
AATLASTGTP AFFVHPAEAL HGDLGMIESR DVMLFISYSG GAKELDLIIP RLEDKSVALL
AMTGKPHSPL GRAAKAVLDI SVEREACPMH LAPTSSTVNT LMMGDALAMA VMQARGFNEE
DFARSHPAGA LGARLLNNVH HLMRQGDAIP QVMLATSVMD AMLELSRTGL GLVAVCDEQH
VVKGVFTDGD LRRWLVGGGA LTTPVSEAMT PNGITLQAQS RAIDAKELLM KRKITAAPVV
DENGKLTGAI NLQDFYQAGI I
