GUTQ_SALTY
ID GUTQ_SALTY Reviewed; 321 AA.
AC Q8ZMJ9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 98.
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=STM2838;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL21718.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE006468; AAL21718.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_461759.3; NC_003197.2.
DR AlphaFoldDB; Q8ZMJ9; -.
DR SMR; Q8ZMJ9; -.
DR STRING; 99287.STM2838; -.
DR PaxDb; Q8ZMJ9; -.
DR DNASU; 1254361; -.
DR EnsemblBacteria; AAL21718; AAL21718; STM2838.
DR GeneID; 1254361; -.
DR KEGG; stm:STM2838; -.
DR PATRIC; fig|99287.12.peg.2992; -.
DR HOGENOM; CLU_040681_13_1_6; -.
DR PhylomeDB; Q8ZMJ9; -.
DR Proteomes; UP000001014; 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; Reference proteome; Repeat; Zinc.
FT CHAIN 1..321
FT /note="Arabinose 5-phosphate isomerase GutQ"
FT /id="PRO_0000410940"
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; 34135 MW; 73CD121A0263970F CRC64;
MSDALLNAGR QTLMLELQEA SRLPERLGDD FVRAANIIIH CEGKVIVSGI GKSGHIGKKI
AATLASTGTP AFFVHPAEAL HGDLGMIESR DVMLFISYSG GAKELDLIIP RLEDKSVALL
AMTGKLHSPL GRAAKAVLDI SVEREACPMH LAPTSSTVNT LMMGDALAMA VMQARGFNEE
DFARSHPAGA LGARLLNNVH HLMRQGDAIP QVMLATSVMD AMLELSRTGL GLVAVCDEQH
VVKGVFTDGD LRRWLVGGGA LTTPVSEAMT PNGITLQAQS RAIDAKELLM KRKITAAPVV
DENGKLTGAI NLQDFYQAGI I
