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Database: UniProt
Entry: A0A1M3G3L8_9SPHI
LinkDB: A0A1M3G3L8_9SPHI
Original site: A0A1M3G3L8_9SPHI 
ID   A0A1M3G3L8_9SPHI        Unreviewed;       274 AA.
AC   A0A1M3G3L8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   08-MAY-2019, entry version 7.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|SAAS:SAAS00700405};
DE            EC=2.5.1.55 {ECO:0000256|SAAS:SAAS00700404};
GN   ORFNames=BGO54_02220 {ECO:0000313|EMBL:OJW34325.1};
OS   Sphingobacteriales bacterium 46-32.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=1895839 {ECO:0000313|EMBL:OJW34325.1, ECO:0000313|Proteomes:UP000184358};
RN   [1] {ECO:0000313|EMBL:OJW34325.1, ECO:0000313|Proteomes:UP000184358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=46-32 {ECO:0000313|EMBL:OJW34325.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T.,
RA   Anantharaman K., Tringe S., Hettich R.L., Harrison S.T.,
RA   Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process
RT   performance in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJW34325.1}.
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DR   EMBL; MKTY01000017; OJW34325.1; -; Genomic_DNA.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000184358; 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:UP000184358};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|SAAS:SAAS00700406};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN       16    271       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   274 AA;  29782 MW;  BD51547430AC44CC CRC64;
     MTPFLKDLFA GQQYDEKNFF LIAGPCVVES EELVMEVAEK VSGICRNLGI PYVFKASYRK
     ANRTSAGSFT GIGDEAALQL VQKAGRAFSV PTTSDIHAHE EAAIAARYID ILQIPAFLCR
     QTDLLYAAGE TGKIVNVKKG QFLSGPAMKF AVEKIKHTGN HKIILTERGT TFGYQDLVVD
     FRNIPWMQEH QTPVVMDVTH SLQQPNQSSG VTGGNPQLIG TIAKAAIATG ANGLFIETHP
     EPAKALSDGA NMLRLDLLEG LLQQLVKLRK AVIS
//
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