GUTQ_ECO57
ID GUTQ_ECO57 Reviewed; 321 AA.
AC Q8X4S5; Q7ABC5;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 114.
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=Z4015, ECs3564;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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=AAG57815.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB36987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57815.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36987.1; ALT_INIT; Genomic_DNA.
DR PIR; C85919; C85919.
DR PIR; D91074; D91074.
DR PIR; H65050; H65050.
DR RefSeq; NP_311591.2; NC_002695.1.
DR RefSeq; WP_001287420.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X4S5; -.
DR SMR; Q8X4S5; -.
DR STRING; 155864.EDL933_3875; -.
DR EnsemblBacteria; AAG57815; AAG57815; Z4015.
DR EnsemblBacteria; BAB36987; BAB36987; ECs_3564.
DR GeneID; 914714; -.
DR KEGG; ece:Z4015; -.
DR KEGG; ecs:ECs_3564; -.
DR PATRIC; fig|386585.9.peg.3724; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_6; -.
DR OMA; VHHLMRT; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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; 1.
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_0000410937"
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
