ID GUTQ_ECOLI Reviewed; 321 AA.
AC P17115; Q2MAC1; Q46874;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 3.
DT 27-MAR-2024, entry version 169.
DE RecName: Full=Arabinose 5-phosphate isomerase GutQ;
DE Short=API;
DE Short=G-API;
DE EC=5.3.1.13 {ECO:0000269|PubMed:16199563};
DE AltName: Full=Phosphosugar aldol-ketol isomerase;
GN Name=gutQ; Synonyms=srlQ; OrderedLocusNames=b2708, JW5431;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-313.
RC STRAIN=K12;
RX PubMed=2134185; DOI=10.3109/10425179009016042;
RA Yamada M., Yamada Y., Saier M.H. Jr.;
RT "Nucleotide sequence and expression of the gutQ gene within the glucitol
RT operon of Escherichia coli.";
RL DNA Seq. 1:141-145(1990).
RN [4]
RP PROTEIN SEQUENCE OF 2-6.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=17366475; DOI=10.1002/pmic.200600599;
RA Maillet I., Berndt P., Malo C., Rodriguez S., Brunisholz R.A., Pragai Z.,
RA Arnold S., Langen H., Wyss M.;
RT "From the genome sequence to the proteome and back: evaluation of E. coli
RT genome annotation with a 2-D gel-based proteomics approach.";
RL Proteomics 7:1097-1106(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP NOMENCLATURE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16199563; DOI=10.1128/jb.187.20.6936-6942.2005;
RA Meredith T.C., Woodard R.W.;
RT "Identification of GutQ from Escherichia coli as a D-arabinose 5-phosphate
RT isomerase.";
RL J. Bacteriol. 187:6936-6942(2005).
CC -!- FUNCTION: Catalyzes the reversible aldol-ketol isomerization between D-
CC ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It
CC appears that the physiological function of G-API may be to synthesize
CC the regulatory molecule A5P, which in turn participates in the
CC induction of the gut operon through an unknown mechanism. It is also
CC able of sustaining the biosynthetic pathway of 3-deoxy-D-manno-
CC octulosonate (KDO), a unique 8-carbon sugar component of
CC lipopolysaccharides (LPSs). {ECO:0000269|PubMed:16199563}.
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; Evidence={ECO:0000269|PubMed:16199563};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23105;
CC Evidence={ECO:0000269|PubMed:16199563};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23106;
CC Evidence={ECO:0000269|PubMed:16199563};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.64 mM for Ru5P (at pH 8.25 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:16199563};
CC KM=1.2 mM for A5P (at pH 8.25 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:16199563};
CC pH dependence:
CC Optimum pH is 8.25. {ECO:0000269|PubMed:16199563};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16199563}.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69217.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA35745.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA35745.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U29579; AAA69217.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75750.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76785.1; -; Genomic_DNA.
DR EMBL; X51361; CAA35745.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_417188.4; NC_000913.3.
DR RefSeq; WP_001287420.1; NZ_LN832404.1.
DR AlphaFoldDB; P17115; -.
DR SMR; P17115; -.
DR BioGRID; 4263273; 290.
DR IntAct; P17115; 2.
DR STRING; 511145.b2708; -.
DR jPOST; P17115; -.
DR PaxDb; 511145-b2708; -.
DR EnsemblBacteria; AAC75750; AAC75750; b2708.
DR GeneID; 947587; -.
DR KEGG; ecj:JW5431; -.
DR KEGG; eco:b2708; -.
DR PATRIC; fig|511145.12.peg.2799; -.
DR EchoBASE; EB0966; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_6; -.
DR InParanoid; P17115; -.
DR OMA; KDQYAAN; -.
DR OrthoDB; 9762536at2; -.
DR PhylomeDB; P17115; -.
DR BioCyc; EcoCyc:EG10973-MONOMER; -.
DR BioCyc; MetaCyc:EG10973-MONOMER; -.
DR PRO; PR:P17115; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
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; IMP:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:EcoCyc.
DR GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR CDD; cd04604; CBS_pair_SIS_assoc; 1.
DR CDD; cd05014; SIS_Kpsf; 1.
DR Gene3D; 3.10.580.10; CBS-domain; 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 NCBIfam; TIGR00393; kpsF; 1.
DR PANTHER; PTHR42745; -; 1.
DR PANTHER; PTHR42745:SF2; ARABINOSE 5-PHOSPHATE ISOMERASE GUTQ; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; CBS domain; Direct protein sequencing; Isomerase;
KW Lipopolysaccharide biosynthesis; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:17366475"
FT CHAIN 2..321
FT /note="Arabinose 5-phosphate isomerase GutQ"
FT /id="PRO_0000136572"
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 215
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; 34031 MW; 85C31DFBD92F7B7C CRC64;
MSEALLNAGR QTLMLELQEA SRLPERLGDD FVRAANIILH CEGKVVVSGI GKSGHIGKKI
AATLASTGTP AFFVHPAEAL HGDLGMIESR DVMLFISYSG GAKELDLIIP RLEDKSIALL
AMTGKPTSPL GLAAKAVLDI SVEREACPMH LAPTSSTVNT LMMGDALAMA VMQARGFNEE
DFARSHPAGA LGARLLNKVH HLMRRDDAIP QVALTASVMD AMLELSRTGL GLVAVCDAQQ
QVQGVFTDGD LRRWLVGGGA LTTPVNEAMT VGGTTLQSQS RAIDAKEILM KRKITAAPVV
DENGKLTGAI NLQDFYQAGI I
//
