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Database: UniProt
Entry: M4Z7K1_9BRAD
LinkDB: M4Z7K1_9BRAD
Original site: M4Z7K1_9BRAD 
ID   M4Z7K1_9BRAD            Unreviewed;       287 AA.
AC   M4Z7K1;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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   ORFNames=S58_35360 {ECO:0000313|EMBL:BAM89529.1};
OS   Bradyrhizobium oligotrophicum S58.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=1245469 {ECO:0000313|EMBL:BAM89529.1, ECO:0000313|Proteomes:UP000011841};
RN   [1] {ECO:0000313|EMBL:BAM89529.1, ECO:0000313|Proteomes:UP000011841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S58 {ECO:0000313|EMBL:BAM89529.1,
RC   ECO:0000313|Proteomes:UP000011841};
RX   PubMed=23396330; DOI=10.1128/AEM.00009-13;
RA   Okubo T., Fukushima S., Itakura M., Oshima K., Longtonglang A.,
RA   Teaumroong N., Mitsui H., Hattori M., Hattori R., Hattori T.,
RA   Minamisawa K.;
RT   "Genome analysis suggests that the soil oligotrophic bacterium Agromonas
RT   oligotrophica (Bradyrhizobium oligotrophicum) is a nitrogen-fixing symbiont
RT   of Aeschynomene indica.";
RL   Appl. Environ. Microbiol. 79:2542-2551(2013).
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, ECO:0000256|HAMAP-
CC         Rule:MF_00056};
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, ECO:0000256|HAMAP-
CC       Rule:MF_00056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00056}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000256|ARBA:ARBA00010499,
CC       ECO:0000256|HAMAP-Rule:MF_00056}.
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DR   EMBL; AP012603; BAM89529.1; -; Genomic_DNA.
DR   RefSeq; WP_015666641.1; NC_020453.1.
DR   AlphaFoldDB; M4Z7K1; -.
DR   STRING; 1245469.S58_35360; -.
DR   KEGG; aol:S58_35360; -.
DR   PATRIC; fig|1245469.3.peg.3607; -.
DR   eggNOG; COG2877; Bacteria.
DR   HOGENOM; CLU_036666_0_0_5; -.
DR   OrthoDB; 9776934at2; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000011841; 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; Aldolase class I; 1.
DR   HAMAP; MF_00056; KDO8P_synth; 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, ECO:0000256|HAMAP-Rule:MF_00056};
KW   Lipopolysaccharide biosynthesis {ECO:0000256|HAMAP-Rule:MF_00056};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00056}.
FT   DOMAIN          15..271
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   287 AA;  29705 MW;  7F66037F5A607E0C CRC64;
     MNASISAAPV VTLGSVKFGN QLPLAVIAGP CQLESRAHAL EVASALKEIA TRLNIGLVYK
     TSFDKANRSS GSAARGLGLA QSLPIFAEIR SSFGLPVLTD VHDASQCAEV AQAVDILQIP
     AFLCRQTDLL LAAAATGKVV NVKKGQFLAP WDMANVVAKI TSAGNPNVLV TERGVSFGYN
     TLVSDMRALP IMARTTGAPV VFDATHSVQQ PGGKGTSSGG EREFVPVLAR AAVAVGVAGV
     FIETHPDPDH APSDGPNMVP LAQFEGLLRT LMAFDALAKG QTAAAPR
//
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