ID N8XA52_9GAMM Unreviewed; 285 AA.
AC N8XA52;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=F967_01501 {ECO:0000313|EMBL:ENV05979.1};
OS Acinetobacter sp. CIP 102637.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1144669 {ECO:0000313|EMBL:ENV05979.1, ECO:0000313|Proteomes:UP000023788};
RN [1] {ECO:0000313|EMBL:ENV05979.1, ECO:0000313|Proteomes:UP000023788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 102637 {ECO:0000313|EMBL:ENV05979.1,
RC ECO:0000313|Proteomes:UP000023788};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Acinetobacter sp. CIP 102637.";
RL Submitted (FEB-2013) 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:ENV05979.1}.
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DR EMBL; APPG01000033; ENV05979.1; -; Genomic_DNA.
DR RefSeq; WP_004677343.1; NZ_KB849435.1.
DR AlphaFoldDB; N8XA52; -.
DR PATRIC; fig|1144669.3.peg.1498; -.
DR HOGENOM; CLU_036666_0_0_6; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000023788; 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:UP000023788};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00056}.
FT DOMAIN 14..277
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 285 AA; 31554 MW; 82E267D3F457DCFB CRC64;
MSQLKPQEVV RLGDIQMANH LPFVLFGGMN VLESKDLAFE IAETYIDICK RLNIPYVFKA
SFDKANRSSL NSFRGPGLEK GIEWLGEIKK QFNVPIITDV HEPYQAAPVA EVADIIQLPA
FLSRQTDLVE AMAKTQAIIN IKKAQFLAPH EMRHILHKCL EAGNDKLILC ERGSAFGYNN
LVVDMLGFDI MKEMNVPVFF DVTHALQTPG GRADSAGGRR AQITTLARSG MATGLAGLFL
EAHPDPEHAK CDGPCALRLS QLEPFLAQLK ELDTLVKGFK KLDTH
//
