GUTQ_SHIFL
ID GUTQ_SHIFL Reviewed; 321 AA.
AC Q83MK2; Q7UBU1;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 5.
DT 03-AUG-2022, entry version 122.
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=SF2731, S2922;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN44222.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP18048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN44222.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP18048.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_708515.4; NC_004337.2.
DR RefSeq; WP_001287442.1; NZ_WPGW01000014.1.
DR AlphaFoldDB; Q83MK2; -.
DR SMR; Q83MK2; -.
DR STRING; 198214.SF2731; -.
DR EnsemblBacteria; AAN44222; AAN44222; SF2731.
DR EnsemblBacteria; AAP18048; AAP18048; S2922.
DR GeneID; 1025715; -.
DR KEGG; sfl:SF2731; -.
DR KEGG; sft:NCTC1_03006; -.
DR KEGG; sfx:S2922; -.
DR PATRIC; fig|198214.7.peg.3252; -.
DR HOGENOM; CLU_040681_13_1_6; -.
DR OrthoDB; 571638at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000410941"
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; 34033 MW; 89A8D35B4C21990C CRC64;
MSEALLNTGR 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 TGGTTLQAQS RAIDAKEVLM KRKITAAPVV
DENGKLTGAI NLQDFYQAGI I
