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Database: UniProt
Entry: S8FCM2_9BACT
LinkDB: S8FCM2_9BACT
Original site: S8FCM2_9BACT 
ID   S8FCM2_9BACT            Unreviewed;       267 AA.
AC   S8FCM2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   08-MAY-2019, entry version 26.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|SAAS:SAAS00700405};
DE            EC=2.5.1.55 {ECO:0000256|SAAS:SAAS00700404};
GN   Name=kdsA {ECO:0000313|EMBL:EPT33726.1};
GN   ORFNames=HMPREF9012_0711 {ECO:0000313|EMBL:EPT33726.1};
OS   Bacteroidetes bacterium oral taxon 272 str. F0290.
OC   Bacteria; Bacteroidetes.
OX   NCBI_TaxID=888054 {ECO:0000313|EMBL:EPT33726.1, ECO:0000313|Proteomes:UP000015345};
RN   [1] {ECO:0000313|EMBL:EPT33726.1, ECO:0000313|Proteomes:UP000015345}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0290 {ECO:0000313|EMBL:EPT33726.1,
RC   ECO:0000313|Proteomes:UP000015345};
RA   Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M.,
RA   Haft D.H., Methe B., Sutton G., Nelson K.E.;
RL   Submitted (JUL-2013) 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|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|SAAS:SAAS00700401}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00700398}.
CC   -!- SIMILARITY: Belongs to the KdsA family.
CC       {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:EPT33726.1}.
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DR   EMBL; AUTU01000016; EPT33726.1; -; Genomic_DNA.
DR   RefSeq; WP_021311648.1; NZ_AUTU01000016.1.
DR   EnsemblBacteria; EPT33726; EPT33726; HMPREF9012_0711.
DR   PATRIC; fig|888054.3.peg.1155; -.
DR   BioCyc; GCF_000442105-HMP:HMPREF9012_RS05480-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000015345; 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-EC.
DR   GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 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   Complete proteome {ECO:0000313|Proteomes:UP000015345};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|SAAS:SAAS00700406};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015345};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156,
KW   ECO:0000313|EMBL:EPT33726.1}.
FT   DOMAIN       11    266       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   267 AA;  29269 MW;  C4DBD06E02289EBA CRC64;
     MITFQDLKAA DNFFLLAGPC VIEGEEMALR IAERIVKITD KLHIPYLFKG SYRKANRSRI
     DSFTGIGDKK ALQVLRMVHQ TFDIPVVTDI HAVEEAEMAA EYADVLQIPA FLCRQTDLLV
     AAAKTGKVVN IKKGQFLSPE AMSFAAGKII ETGNNKVMLT ERGTTFGYQD LIVDFRGIPT
     MKAFGHPVIL DTTHSLQRPN QTDGVTGGQP QLIETIAKAG IAVGADGIFM ETHEDPSIAK
     SDGANMLKLD LLEGLLEKLV KIRKALQ
//
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