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Database: UniProt
Entry: R5EQH6_9GAMM
LinkDB: R5EQH6_9GAMM
Original site: R5EQH6_9GAMM 
ID   R5EQH6_9GAMM            Unreviewed;       284 AA.
AC   R5EQH6;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=BN779_01491 {ECO:0000313|EMBL:CCX93594.1};
OS   Succinatimonas sp. CAG:777.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Succinivibrionaceae; Succinatimonas.
OX   NCBI_TaxID=1262974 {ECO:0000313|EMBL:CCX93594.1, ECO:0000313|Proteomes:UP000018241};
RN   [1] {ECO:0000313|EMBL:CCX93594.1, ECO:0000313|Proteomes:UP000018241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:777 {ECO:0000313|Proteomes:UP000018241};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCX93594.1}.
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DR   EMBL; CAXH010000115; CCX93594.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5EQH6; -.
DR   STRING; 1262974.BN779_01491; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000018241; 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-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   Reference proteome {ECO:0000313|Proteomes:UP000018241};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00056}.
FT   DOMAIN          11..274
FT                   /note="DAHP synthetase I/KDSA"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
SQ   SEQUENCE   284 AA;  30995 MW;  5EC89F6FB6B07AA8 CRC64;
     MVDKVIKIGD IEVSNSGKFV LFGGMNVLES RDLAMQICEH YVKVTEKLHI PYVFKASFDK
     ANRSSIYSYR GPGLDEGMKI FEEIKKTFNV PVITDIHEKE QAPVVAQVVD VLQIPAFLAR
     QTDLVNAMAK TGKVINIKKP QFLSPGQMVN ITKKFEECGN SNLLLCDRGT CFGYDNLVVD
     MLGFGVMKQV CGNYPVIFDV THSLQCRDST GAASGGRRAQ VSDLARAGMA VGIGGLFLEA
     HPNPDTAKCD GPSALPLDKL EPFLAQCKAI DDLVKSFAPL DTSK
//
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