KPSF_ECOL6
ID KPSF_ECOL6 Reviewed; 327 AA.
AC Q8FDQ2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Arabinose 5-phosphate isomerase KpsF {ECO:0000303|PubMed:16390329};
DE Short=API {ECO:0000303|PubMed:16390329};
DE EC=5.3.1.13 {ECO:0000269|PubMed:16390329};
DE AltName: Full=K-antigen-specific arabinose 5-phosphate isomerase;
DE Short=K-API;
GN Name=kpsF {ECO:0000303|PubMed:16390329}; OrderedLocusNames=c3686;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION AS AN ARABINOSE 5-PHOSPHATE ISOMERASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, ACTIVITY REGULATION,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=16390329; DOI=10.1042/bj20051828;
RA Meredith T.C., Woodard R.W.;
RT "Characterization of Escherichia coli D-arabinose 5-phosphate isomerase
RT encoded by kpsF: implications for group 2 capsule biosynthesis.";
RL Biochem. J. 395:427-432(2006).
CC -!- FUNCTION: Involved in the biosynthesis of K-antigen capsules. Catalyzes
CC the reversible aldol-ketol isomerization between D-ribulose 5-phosphate
CC (Ru5P) and D-arabinose 5-phosphate (A5P).
CC {ECO:0000269|PubMed:16390329}.
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:16390329};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23105;
CC Evidence={ECO:0000269|PubMed:16390329};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23106;
CC Evidence={ECO:0000269|PubMed:16390329};
CC -!- ACTIVITY REGULATION: Inhibited by 10 uM zinc, cadmium or mercury ions.
CC {ECO:0000269|PubMed:16390329}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.30 mM for Ru5P (at pH 7.8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:16390329};
CC KM=0.57 mM for A5P (at pH 7.8 and at 37 degrees Celsius)
CC {ECO:0000269|PubMed:16390329};
CC pH dependence:
CC Optimum pH is 7.8. {ECO:0000269|PubMed:16390329};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16390329}.
CC -!- MASS SPECTROMETRY: Mass=35323; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16390329};
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN82134.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000269|PubMed:16390329};
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DR EMBL; AE014075; AAN82134.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8FDQ2; -.
DR SMR; Q8FDQ2; -.
DR STRING; 199310.c3686; -.
DR EnsemblBacteria; AAN82134; AAN82134; c3686.
DR KEGG; ecc:c3686; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_6; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-KW.
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 TIGRFAMs; TIGR00393; kpsF; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51464; SIS; 1.
PE 1: Evidence at protein level;
KW ATP-binding; CBS domain; Isomerase; Lipopolysaccharide biosynthesis;
KW Metal-binding; Nucleotide-binding; Repeat; Zinc.
FT CHAIN 1..327
FT /note="Arabinose 5-phosphate isomerase KpsF"
FT /id="PRO_0000410942"
FT DOMAIN 48..191
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 217..273
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 282..327
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 63..68
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 82..83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 121..130
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 155..157
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 66
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 118
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 159
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 200
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
SQ SEQUENCE 327 AA; 35487 MW; D3C9778EF81F16C4 CRC64;
MSERHLPDDQ SSTIDPYLIT SVRQTLAEQS AALQNLSKQL DSGQYQRVLN LIMNCKGHVI
LSGMGKSGHV GRKISATLAS TGTPSFFIHP AEAFHGDLGM ITPYDLLILI SASGETDEIL
KLVPSLKNFG NRIIAITNNG NSTLAKNADA VLELHMANET CPNNLAPTTS TTLTMAIGDA
LAIAMIHQRK FMPNDFARYH PGGSLGRRLL TRVADVMQHD VPAVQLDASF KTVIQRITSG
CQGMVMVEDA EGGLAGIITD GDLRRFMEKE GSLTSATAAQ MMTREPLTLP EDTMIIEAEE
KMQKHRVSTL LVTNKANKVT GLVRIFD
