KPSF5_ECOLX
ID KPSF5_ECOLX Reviewed; 327 AA.
AC Q47334;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=K5;
RX PubMed=8932302; DOI=10.1128/jb.178.22.6466-6474.1996;
RA Simpson D.A., Hammarton T.C., Roberts I.S.;
RT "Transcriptional organization and regulation of expression of region 1 of
RT the Escherichia coli K5 capsule gene cluster.";
RL J. Bacteriol. 178:6466-6474(1996).
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; X95264; CAA64561.1; -; Genomic_DNA.
DR RefSeq; WP_001296394.1; NZ_WVTZ01000026.1.
DR AlphaFoldDB; Q47334; -.
DR SMR; Q47334; -.
DR OMA; EREVCPN; -.
DR OrthoDB; 571638at2; -.
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; 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 3: Inferred from homology;
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_0000136574"
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; 35563 MW; D0C9A38DFB1E02C4 CRC64;
MSERHLPDDQ SSTIDPYLIT SVRQTLAEQS AALQNLSKQL DSGQYQRVLN LIMNCKGHVI
LSGMGKSGHV GRKMSATLAS TGTPSFFIHP AEAFHGDLGM ITPYDLLILI SASGETDEIL
KLVPSLKNFG NRIIAITNNG NSTLAKNADA VLELHMANET CPNNLAPTTS TTLTMAIGDA
LAIAMIHQRK FMPNDFARYH PGGSLGRRLL TRVADVMQHD VPAVQLDASF KTVIQRITSG
CQGMVMVEDA EGGLAGIITD GDLRRFMEKE DSLTSATAAQ MMTREPLTLP EDTMIIEAEE
KMQKHRVSTL LVTNKANKVT GLVRIFD
