ID   KPSF1_ECOLX             Reviewed;         317 AA.
AC   P42502;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Arabinose 5-phosphate isomerase KpsF;
DE            Short=API;
DE            EC=5.3.1.13;
DE   AltName: Full=K-antigen-specific arabinose 5-phosphate isomerase;
DE            Short=K-API;
DE   AltName: Full=Polysialic acid capsule expression protein kpsF;
GN   Name=kpsF;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K1;
RX   PubMed=8253690; DOI=10.1128/jb.175.24.8018-8023.1993;
RA   Cieslewicz M.J., Steenbergen S.M., Vimr E.R.;
RT   "Cloning, sequencing, expression, and complementation analysis of the
RT   Escherichia coli K1 kps region 1 gene, kpsE, and identification of an
RT   upstream open reading frame encoding a protein with homology to GutQ.";
RL   J. Bacteriol. 175:8018-8023(1993).
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) (By similarity).
CC       {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}.
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DR   EMBL; L19929; AAB51623.1; -; Genomic_DNA.
DR   PIR; A49915; A49915.
DR   AlphaFoldDB; P42502; -.
DR   SMR; P42502; -.
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: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; 1.
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   3: Inferred from homology;
KW   ATP-binding; CBS domain; Isomerase; Lipopolysaccharide biosynthesis;
KW   Metal-binding; Nucleotide-binding; Repeat; Zinc.
FT   CHAIN           1..317
FT                   /note="Arabinose 5-phosphate isomerase KpsF"
FT                   /id="PRO_0000136573"
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..317
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   317 AA;  34474 MW;  EF4A4EC40C283368 CRC64;
     MSERHLPDDQ SSTIDPYLIT SVRQTLAEEG ARLQNLSKQL DSGQYQRVLN LIMNCKGHVI
     LSGMGKSGHV GRKMSATLAS TGTPSFFIHP AEAFHGDLGM ITPYDLLILI SASGETDEIL
     KLVPSLKNFG NRIIAITNNG NSTLAKNADA VLELHMANET CPNNLAPTTS TTLTMAIGDA
     LAIAMIRQRK FMPNDFARYH PGGSLGRRLL TRVADVMQHD VPAVQLDASF KTVIQRITSG
     CQGMVMVEDA EGGLAGIITD GDLRRFMEKE DSLTSATAAQ MMTREPLTLP EDTMIIEAEE
     KMQKDKCLNV IGDQQGK