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Database: UniProt
Entry: D4S5P3_9FIRM
LinkDB: D4S5P3_9FIRM
Original site: D4S5P3_9FIRM 
ID   D4S5P3_9FIRM            Unreviewed;       277 AA.
AC   D4S5P3;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   08-MAY-2019, entry version 44.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000256|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000256|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000256|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000256|HAMAP-Rule:MF_00056,
GN   ECO:0000313|EMBL:EFF66663.1};
GN   ORFNames=HMPREF7545_0858 {ECO:0000313|EMBL:EFF66663.1};
OS   Selenomonas noxia ATCC 43541.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales;
OC   Selenomonadaceae; Selenomonas.
OX   NCBI_TaxID=585503 {ECO:0000313|EMBL:EFF66663.1, ECO:0000313|Proteomes:UP000003701};
RN   [1] {ECO:0000313|EMBL:EFF66663.1, ECO:0000313|Proteomes:UP000003701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43541 {ECO:0000313|EMBL:EFF66663.1,
RC   ECO:0000313|Proteomes:UP000003701};
RA   Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C.,
RA   Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L.,
RA   Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y.,
RA   Hemphill L., Highlander S.K., Hirani K., Hogues M., Jackson L.,
RA   Jakkamsetti A., Javaid M., Jiang H., Korchina V., Kovar C., Lara F.,
RA   Lee S., Mata R., Mathew T., Moen C., Morales K., Munidasa M.,
RA   Nazareth L., Ngo R., Nguyen L., Okwuonu G., Ongeri F., Patil S.,
RA   Petrosino J., Pham C., Pham P., Pu L.-L., Puazo M., Raj R., Reid J.,
RA   Rouhana J., Saada N., Shang Y., Simmons D., Thornton R., Warren J.,
RA   Weissenberger G., Zhang J., Zhang L., Zhou C., Zhu D., Muzny D.,
RA   Worley K., Gibbs R.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-
CC         deoxy-alpha-D-manno-2-octulosonate-8-phosphate + phosphate;
CC         Xref=Rhea:RHEA:14053, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57693, ChEBI:CHEBI:58702, ChEBI:CHEBI:85985;
CC         EC=2.5.1.55; Evidence={ECO:0000256|HAMAP-Rule:MF_00056,
CC         ECO:0000256|SAAS:SAAS01123735};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|SAAS:SAAS00700395}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC       biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-
CC       phosphate: step 2/3. {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|SAAS:SAAS00700401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056,
CC       ECO:0000256|SAAS:SAAS00700398}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00056, ECO:0000256|SAAS:SAAS00700400}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EFF66663.1}.
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DR   EMBL; ACKT01000016; EFF66663.1; -; Genomic_DNA.
DR   STRING; 585503.HMPREF7545_0858; -.
DR   EnsemblBacteria; EFF66663; EFF66663; HMPREF7545_0858.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000003701; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008676; F:3-deoxy-8-phosphooctulonate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019294; P:keto-3-deoxy-D-manno-octulosonic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00056; KDO8P_synth; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006269; KDO8P_synthase.
DR   PANTHER; PTHR21057; PTHR21057; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   TIGRFAMs; TIGR01362; KDO8P_synth; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000003701};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00700406};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003701};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:EFF66663.1}.
FT   DOMAIN        9    263       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
FT   COILED      255    275       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   277 AA;  30381 MW;  0B0D6A63723FFCA9 CRC64;
     MKMNKVKLAN FEIGGGEPLV LIAGPCVLEG LERSLMIGRG IKEITNRLGI PYVFKASFDK
     ANRSAYHSFR GPGMEDGLKM LKKIRRELNV PVVTDIHETC QAEPAAKAVD ILQIPAFLSR
     QTDLLHAAAQ TGAIVNVKKG QFLSPNDMRN VVDKIHESGS ERILLTERGA SFGYNNLVVD
     MRAFPIMRSF GYPVIFDGTH SVQLPGGAGT SSSGQREYVE YLVRAAVGAG VDGLFLEVHD
     NPPEALSDGP NMVYLDKLEE LLKEALAIYE VVRRKLN
//
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