GenomeNet

Database: UniProt
Entry: A0A1V3N3D4_9SPHI
LinkDB: A0A1V3N3D4_9SPHI
Original site: A0A1V3N3D4_9SPHI 
ID   A0A1V3N3D4_9SPHI        Unreviewed;       271 AA.
AC   A0A1V3N3D4;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   08-MAY-2019, entry version 6.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000256|SAAS:SAAS00700405};
DE            EC=2.5.1.55 {ECO:0000256|SAAS:SAAS00700404};
GN   ORFNames=BWD42_06695 {ECO:0000313|EMBL:OOG19597.1};
OS   Sphingobacterium sp. CZ-UAM.
OC   Bacteria; Bacteroidetes; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Sphingobacterium.
OX   NCBI_TaxID=1933868 {ECO:0000313|EMBL:OOG19597.1, ECO:0000313|Proteomes:UP000188865};
RN   [1] {ECO:0000313|EMBL:OOG19597.1, ECO:0000313|Proteomes:UP000188865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CZ-UAM {ECO:0000313|EMBL:OOG19597.1,
RC   ECO:0000313|Proteomes:UP000188865};
RA   Steffani-Vallejo J.L., Licona-Cassani C., Cruz-Morales P., Lozano L.,
RA   Zuniga C., Morales M., Revah S., Utrilla J.;
RT   "Genome sequence of Sphingobacterium sp. CZ-UAM, isolated from a
RT   methanotrophic consortium.";
RL   Submitted (JAN-2017) 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:OOG19597.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; MTCM01000001; OOG19597.1; -; Genomic_DNA.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000188865; 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:UP000188865};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00700397};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|SAAS:SAAS00700406};
KW   Transferase {ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN        8    267       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   271 AA;  29632 MW;  5940B1F4A8F38DD5 CRC64;
     MINKYIPEIK NGTSQNFFLM AGPCAIEGEE IALRIAEKIV TITDKLNIPY IFKGSYRKAN
     RSRLDSFMGI GDEKALKILE KVGKTFGVPT VTDIHESHEA EMAAAYVDVL QIPAFLCRQT
     DLLVAAAKTN KVVNVKKGQF LSAGSMKFAV DKIVESGNEK VFLTDRGNMF GYQDLIVDYR
     GIPEMRSFNV PTVMDCTHSL QQPNQTSGVT GGKPALIETI AKAAIAVGAD GLFIETHPDP
     ANAKSDGANM LHLDLLEGLM EKLVRVRQAI L
//
DBGET integrated database retrieval system