ID D3DJ75_HYDTT Unreviewed; 260 AA.
AC D3DJ75;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
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 ECO:0000313|EMBL:BAI69877.1};
GN OrderedLocusNames=HTH_1426 {ECO:0000313|EMBL:BAI69877.1};
OS Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobacter.
OX NCBI_TaxID=608538 {ECO:0000313|EMBL:BAI69877.1, ECO:0000313|Proteomes:UP000002574};
RN [1] {ECO:0000313|EMBL:BAI69877.1, ECO:0000313|Proteomes:UP000002574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6534 / IAM 12695 / TK-6 [Tokyo]
RC {ECO:0000313|Proteomes:UP000002574};
RX PubMed=20348262; DOI=10.1128/JB.00158-10;
RA Arai H., Kanbe H., Ishii M., Igarashi Y.;
RT "Complete genome sequence of the thermophilic, obligately
RT chemolithoautotrophic hydrogen-oxidizing bacterium Hydrogenobacter
RT thermophilus TK-6.";
RL J. Bacteriol. 192:2651-2652(2010).
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, ECO:0000256|HAMAP-
CC Rule:MF_00056}.
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; AP011112; BAI69877.1; -; Genomic_DNA.
DR RefSeq; WP_012964057.1; NC_017161.1.
DR AlphaFoldDB; D3DJ75; -.
DR STRING; 608538.HTH_1426; -.
DR KEGG; hth:HTH_1426; -.
DR PATRIC; fig|608538.5.peg.1446; -.
DR eggNOG; COG2877; Bacteria.
DR OrthoDB; 9780456at2; -.
DR UniPathway; UPA00030; -.
DR UniPathway; UPA00357; UER00474.
DR Proteomes; UP000002574; 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 Reference proteome {ECO:0000313|Proteomes:UP000002574};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00056}.
FT DOMAIN 1..252
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
SQ SEQUENCE 260 AA; 28638 MW; 7844F02EAD7CD583 CRC64;
MIIIAGPCVI ENEKVVFQVA QELKRLSELY PEFSFVFKSS FDKANRSSVK SFRGPGLEKG
LEILSKVKEE FGLKITTDVH ETWQVEPVSQ VVDIIQIPAF LSRQTDLLVA SAKTGKPVNV
KKGQFLAPWD VKNVVEKLMY AGAKEYYITE RGVSFGYNNL VVDFRSLVIM SSFTKVIFDA
THSVQLPGGA GDKSSGQREF VLPLIRAAVA VGCDGIFMET HPDPDSALSD GPNMLPLNSL
ESVLETIQRI RNALSSYSTG
//
