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 24-JAN-2024, entry version 78.
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; Pseudomonadota; 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; 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:SF1; ARABINOSE 5-PHOSPHATE ISOMERASE KDSD; 1.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF01380; SIS; 1.
DR PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR SUPFAM; SSF53697; SIS domain; 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
//
