Entry sw: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   18-JAN-2017, entry version 96.
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.,
RA   Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V.,
RA   Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M.,
RA   Simmonds M., Skelton J., 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.,
RA   Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
RA   Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
RA   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.,
RA   Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
RA   Yang H., 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-
CC       octulosonate (KDO), a unique 8-carbon sugar component of
CC       lipopolysaccharides (LPSs). Catalyzes the reversible aldol-ketol
CC       isomerization between D-ribulose 5-phosphate (Ru5P) and D-
CC       arabinose 5-phosphate (A5P) (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: D-arabinose 5-phosphate = D-ribulose 5-
CC       phosphate.
CC   -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC       biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-
CC       phosphate: 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   -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00703}.
CC   -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00797}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM83742.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAS63979.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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_LT605018.1.
DR   RefSeq; YP_002348464.1; NC_003143.1.
DR   ProteinModelPortal; Q8D1Q8; -.
DR   STRING; 187410.y0149; -.
DR   PRIDE; Q8D1Q8; -.
DR   DNASU; 1145095; -.
DR   EnsemblBacteria; AAM83742; AAM83742; y0149.
DR   EnsemblBacteria; AAS63979; AAS63979; YP_3832.
DR   GeneID; 1176397; -.
DR   KEGG; ype:YPO3577; -.
DR   KEGG; ypk:y0149; -.
DR   KEGG; ypm:YP_3832; -.
DR   eggNOG; ENOG4105C2X; Bacteria.
DR   eggNOG; COG0517; LUCA.
DR   eggNOG; COG0794; LUCA.
DR   HOGENOM; HOG000264729; -.
DR   KO; K06041; -.
DR   OMA; LMACLMR; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00473.
DR   Proteomes; UP000000815; Chromosome.
DR   Proteomes; UP000001019; Chromosome.
DR   Proteomes; UP000002490; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0019146; F:arabinose-5-phosphate isomerase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR004800; KdsD/KpsF-type.
DR   InterPro; IPR001347; SIS.
DR   Pfam; PF00571; CBS; 2.
DR   Pfam; PF01380; SIS; 1.
DR   PIRSF; PIRSF004692; KdsD_KpsF; 1.
DR   SMART; SM00116; CBS; 2.
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; Complete proteome; Isomerase;
KW   Lipopolysaccharide biosynthesis; Metal-binding; Reference proteome;
KW   Repeat; Zinc.
FT   CHAIN         1    328       Arabinose 5-phosphate isomerase KdsD.
FT                                /FTId=PRO_0000136581.
FT   DOMAIN       41    184       SIS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00797}.
FT   DOMAIN      210    268       CBS 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00703}.
FT   DOMAIN      277    328       CBS 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00703}.
FT   REGION       75     76       Substrate binding. {ECO:0000250}.
FT   REGION      114    123       Substrate binding. {ECO:0000250}.
FT   REGION      148    150       Substrate binding. {ECO:0000250}.
FT   METAL        82     82       Zinc. {ECO:0000250}.
FT   BINDING      82     82       Substrate. {ECO:0000250}.
FT   BINDING      88     88       Substrate. {ECO:0000250}.
FT   BINDING     275    275       Substrate. {ECO:0000250}.
FT   SITE         59     59       Catalytically relevant. {ECO:0000250}.
FT   SITE        111    111       Catalytically relevant. {ECO:0000250}.
FT   SITE        152    152       Catalytically relevant. {ECO:0000250}.
FT   SITE        193    193       Catalytically relevant. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       274    325       ipfam:CBS [T]
FT   MYHIT       210    268       iprf:CBS [T]
FT   MYHIT        46    177       ipfam:SIS [T]
FT   MYHIT       277    328       iprf:CBS [T]
FT   MYHIT       215    263       ismart:CBS [T]
FT   MYHIT        41    184       iprf:SIS [T]
FT   MYHIT       206    261       ipfam:CBS [T]
FT   MYHIT       280    327       ismart:CBS [T]
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
//