KDSD_YERPE
ID KDSD_YERPE Reviewed; 328 AA.
AC Q8D1Q8; Q0WB74; Q8ZB48;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Arabinose 5-phosphate isomerase KdsD;
DE Short=API;
DE Short=L-API;
DE EC=5.3.1.13;
GN Name=kdsD; OrderedLocusNames=YPO3577, y0149, YP_3832;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate
CC (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs).
CC Catalyzes the reversible aldol-ketol isomerization between D-ribulose
CC 5-phosphate (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 -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC step 1/3.
CC -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC biosynthesis.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SIS family. GutQ/KpsF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM83742.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAS63979.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL22165.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM83742.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS63979.1; ALT_INIT; Genomic_DNA.
DR PIR; AB0435; AB0435.
DR RefSeq; WP_002210119.1; NZ_WUCM01000032.1.
DR RefSeq; YP_002348464.1; NC_003143.1.
DR AlphaFoldDB; Q8D1Q8; -.
DR SMR; Q8D1Q8; -.
DR STRING; 214092.YPO3577; -.
DR PaxDb; Q8D1Q8; -.
DR DNASU; 1145095; -.
DR EnsemblBacteria; AAM83742; AAM83742; y0149.
DR EnsemblBacteria; AAS63979; AAS63979; YP_3832.
DR GeneID; 66844060; -.
DR KEGG; ype:YPO3577; -.
DR KEGG; ypk:y0149; -.
DR KEGG; ypm:YP_3832; -.
DR PATRIC; fig|214092.21.peg.4071; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0794; Bacteria.
DR HOGENOM; CLU_040681_13_1_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00473.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
DR GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
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 SMART; SM00116; CBS; 2.
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 Carbohydrate metabolism; CBS domain; Isomerase;
KW Lipopolysaccharide biosynthesis; Metal-binding; Reference proteome; Repeat;
KW Zinc.
FT CHAIN 1..328
FT /note="Arabinose 5-phosphate isomerase KdsD"
FT /id="PRO_0000136581"
FT DOMAIN 41..184
FT /note="SIS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 210..268
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 277..328
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT BINDING 75..76
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 114..123
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148..150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 111
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 152
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
FT SITE 193
FT /note="Catalytically relevant"
FT /evidence="ECO:0000250"
SQ SEQUENCE 328 AA; 35062 MW; AE9A2411E9CC2020 CRC64;
MSTFDLQPGV DFQQAGKQVL QIEREGLAQL DQYINEDFSR ACEAIFRCHG KVVVMGMGKS
GHIGCKIAAT FASTGTPAFF VHPGEASHGD LGMITPQDIV LAISNSGESN EILTLIPVLK
RQKILLICMS SNPESTMGKA ADIHLCINVP QEACPLGLAP TTSTTATLVM GDALAVALLK
ARGFTQEDFA LSHPGGALGR KLLLRISDIM HTGTEIPTVS PDASLRDALL EITRKSLGLT
VICDDSMRIK GIFTDGDLRR VFDMGIDLNN AKIADVMTRG GIRVPPNILA VDALNLMESR
HITALLVADG DQLLGVVHMH DMLRAGVV
