ID R5Q1W7_9PROT Unreviewed; 283 AA.
AC R5Q1W7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=BN820_01537 {ECO:0000313|EMBL:CCZ22805.1};
OS Acetobacter sp. CAG:977.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1262685 {ECO:0000313|EMBL:CCZ22805.1, ECO:0000313|Proteomes:UP000018259};
RN [1] {ECO:0000313|EMBL:CCZ22805.1, ECO:0000313|Proteomes:UP000018259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:977 {ECO:0000313|Proteomes:UP000018259};
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:CCZ22805.1}.
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DR EMBL; CAZQ010000099; CCZ22805.1; -; Genomic_DNA.
DR STRING; 1262685.BN820_01537; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000018259; 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:UP000018259};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00056}.
FT DOMAIN 10..281
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 283 AA; 30173 MW; 51FED33EF1CC18B1 CRC64;
MTNRRITVGN VTAGNDLPFV LIGGPCQIES KDHAIGLAGK IYEIAKELDI PYIFKASFDK
ANRTSATGAR GIGLEKALDV FSEIKKLYGC PVVTDVHEPY QCAEVAPVVD VLQIPAFLCR
QTDLVVAAAK TGRVLNIKKG QFLAPWDMKN VVAKAETAGN PNVMVTERGV SFGYNTLVVD
MRSLPIMAQQ TGCPVIMDAT HAVQQPGGQG TSTGGQREFA PVLARAAXVL ARAAVAVGVA
GVFIETHENP DKSPSDGPNM IPLADLKDVL STLKSIDKLM KNY
//
