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Database: UniProt
Entry: R6IPX8_9PROT
LinkDB: R6IPX8_9PROT
Original site: R6IPX8_9PROT 
ID   R6IPX8_9PROT            Unreviewed;       280 AA.
AC   R6IPX8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   08-MAY-2019, entry version 26.
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=BN570_00389 {ECO:0000313|EMBL:CDB40027.1};
OS   Azospirillum sp. CAG:260.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum; environmental samples.
OX   NCBI_TaxID=1262706 {ECO:0000313|EMBL:CDB40027.1};
RN   [1] {ECO:0000313|EMBL:CDB40027.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J.,
RA   Sunagawa S., Plichta D., Gautier L., Le Chatelier E., Peletier E.,
RA   Bonde I., Nielsen T., Manichanh C., Arumugam M., Batto J.,
RA   Santos M.B.Q.D., Blom N., Borruel N., Burgdorf K.S., Boumezbeur F.,
RA   Casellas F., Dore J., Guarner F., Hansen T., Hildebrand F., Kaas R.S.,
RA   Kennedy S., Kristiansen K., Kultima J.R., Leonard P., Levenez F.,
RA   Lund O., Moumen B., Le Paslier D., Pons N., Pedersen O., Prifti E.,
RA   Qin J., Raes J., Tap J., Tims S., Ussery D.W., Yamada T.,
RA   MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P., Wang J.,
RA   Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units
RT   of genetic variation.";
RL   Submitted (NOV-2012) 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|HAMAP-Rule:MF_00056,
CC         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|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}.
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:CDB40027.1}.
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DR   EMBL; CBDP010000047; CDB40027.1; -; Genomic_DNA.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
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   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   Transferase {ECO:0000256|HAMAP-Rule:MF_00056,
KW   ECO:0000256|SAAS:SAAS00080156}.
FT   DOMAIN       10    261       DAHP_synth_1. {ECO:0000259|Pfam:PF00793}.
SQ   SEQUENCE   280 AA;  30192 MW;  EDC0BA87E497F3E5 CRC64;
     MEQHQVKIGN FEIGNKLPLA LIAGPCQIQS RQHAVELAGK LVELTSKLGI NYIFKASFDK
     ANRTSITGAR GVGIEEGIRT FDEIKKIYGC PIVTDIHERE QCQIIAPHVD MLQIPAFLCR
     QTDLVVAAAK TGKVVNIKKG QFLAPWDMKN IVKKSVDSGN ANVCITERGT SFGYNTLVTD
     MRGLPQMARD TGCPVIFDAT HSVQQPGGLG GSSGGQGEFA PVLARAAVAV GVAAVFIETH
     EDPAKSPSDG PNMIPLHAME KVVSDLMAYD CLTKSRIQDY
//
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