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Database: UniProt
Entry: A4G2D3_HERAR
LinkDB: A4G2D3_HERAR
Original site: A4G2D3_HERAR 
ID   A4G2D3_HERAR            Unreviewed;       280 AA.
AC   A4G2D3;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 82.
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:CAL60670.1};
GN   OrderedLocusNames=HEAR0454 {ECO:0000313|EMBL:CAL60670.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL60670.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL60670.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M.,
RA   Leize E., Lieutaud A., Lievremont D., Makita Y., Mangenot S.,
RA   Nitschke W., Ortet P., Perdrial N., Schoepp B., Siguier N.,
RA   Simeonova D.D., Rouy Z., Segurens B., Turlin E., Vallenet D.,
RA   Van Dorsselaer A., Weiss S., Weissenbach J., Lett M.C., Danchin A.,
RA   Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-
RT   rich environments.";
RL   PLoS Genet. 3:518-530(2007).
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|HAMAP-Rule:MF_00056,
CC       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}.
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DR   EMBL; CU207211; CAL60670.1; -; Genomic_DNA.
DR   RefSeq; WP_011870015.1; NC_009138.1.
DR   STRING; 204773.HEAR0454; -.
DR   EnsemblBacteria; CAL60670; CAL60670; HEAR0454.
DR   KEGG; har:HEAR0454; -.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   HOGENOM; HOG000023021; -.
DR   KO; K01627; -.
DR   OMA; IKKPQFM; -.
DR   OrthoDB; 687380at2; -.
DR   BioCyc; HARS204773:HEAR_RS02100-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000006697; Chromosome.
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   Complete proteome {ECO:0000313|Proteomes:UP000006697};
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:UP000006697};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00080156, ECO:0000313|EMBL:CAL60670.1}.
FT   DOMAIN        8    271       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   280 AA;  30613 MW;  D2406070B5164608 CRC64;
     MIKIGDIKVD NALPFVLFGG INVLESRDLA MKSCEEYVRV TQKLGIPYVF KASFDKANRS
     SIHSYRGPGL EEGMRIFEEV KKTFNVPVIT DVHEVHQAEI VAEVADVLQL PAFLARQTDL
     VVALAKTGSV INIKKPQFLS PSQMMNIVEK FKEAGNEQLI LCDRGTCFGY DNLVVDMLGF
     GVMKKVCNNL PIIFDVTHAL QQRDPGGAAS GGRREQVADL ARAGMSVGLA GLFLEAHPDP
     KSAKCDGPSA LPLDKLEPFL AQLKQLDDLV KSFAPLDIEA
//
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