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Database: UniProt
Entry: C1DIH0_AZOVD
LinkDB: C1DIH0_AZOVD
Original site: C1DIH0_AZOVD 
ID   C1DIH0_AZOVD            Unreviewed;       282 AA.
AC   C1DIH0;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=3-deoxy-8-phosphooctulonate synthase {ECO:0000256|ARBA:ARBA00012693};
DE            EC=2.5.1.55 {ECO:0000256|ARBA:ARBA00012693};
GN   Name=kdsA {ECO:0000313|EMBL:ACO78651.1};
GN   OrderedLocusNames=Avin_24680 {ECO:0000313|EMBL:ACO78651.1};
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO78651.1, ECO:0000313|Proteomes:UP000002424};
RN   [1] {ECO:0000313|EMBL:ACO78651.1, ECO:0000313|Proteomes:UP000002424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA   Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA   Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA   Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA   Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA   Dean D.R., Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT   to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-arabinose 5-phosphate + H2O + phosphoenolpyruvate = 3-deoxy-
CC         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; EC=2.5.1.55;
CC         Evidence={ECO:0000256|ARBA:ARBA00001069};
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000256|ARBA:ARBA00004756}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; 3-deoxy-D-manno-octulosonate
CC       biosynthesis; 3-deoxy-D-manno-octulosonate from D-ribulose 5-phosphate:
CC       step 2/3. {ECO:0000256|ARBA:ARBA00004845}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the KdsA family.
CC       {ECO:0000256|ARBA:ARBA00010499}.
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DR   EMBL; CP001157; ACO78651.1; -; Genomic_DNA.
DR   RefSeq; WP_012701044.1; NC_012560.1.
DR   AlphaFoldDB; C1DIH0; -.
DR   STRING; 322710.Avin_24680; -.
DR   EnsemblBacteria; ACO78651; ACO78651; Avin_24680.
DR   KEGG; avn:Avin_24680; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_6; -.
DR   OrthoDB; 9776934at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000002424; Chromosome.
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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006218; DAHP1/KDSA.
DR   InterPro; IPR006269; KDO8P_synthase.
DR   NCBIfam; TIGR01362; KDO8P_synth; 1.
DR   PANTHER; PTHR21057:SF2; 2-DEHYDRO-3-DEOXYPHOSPHOOCTONATE ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR21057; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE; 1.
DR   Pfam; PF00793; DAHP_synth_1; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          20..276
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   282 AA;  31152 MW;  9DF85524DA0E79D3 CRC64;
     MSFEVLYKIF PERRNGNHKD ELFIFAGPCV VENESITLQI AEALADIHQA CGIDIVFKAS
     FMKANRTSKS SFTGLPLDQS LYILQKVKTQ FGLKVLSDVH EYTNLDEIAD VIDVLQTPAF
     LVRQTEFLKK VAAVGKPINI KKGQFLSPTE MISVVDKVLS FGNSDLLVCE RGSSFGYNYL
     INDFRGMQQL MQMGQPLVFD ATHSVQRPGA LGDSSGGDAR YAPRLAKAAV ALGVDGIFLE
     THPDPALALS DGPNMIPLAL VKQLLRELKD LHQMVKEQST YI
//
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