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Database: UniProt
Entry: H3KA94_9FIRM
LinkDB: H3KA94_9FIRM
Original site: H3KA94_9FIRM 
ID   H3KA94_9FIRM            Unreviewed;       276 AA.
AC   H3KA94;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   11-DEC-2019, entry version 43.
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=HMPREF9454_02167 {ECO:0000313|EMBL:EHR33593.1};
OS   Megamonas funiformis YIT 11815.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Megamonas.
OX   NCBI_TaxID=742816 {ECO:0000313|EMBL:EHR33593.1, ECO:0000313|Proteomes:UP000005963};
RN   [1] {ECO:0000313|EMBL:EHR33593.1, ECO:0000313|Proteomes:UP000005963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 11815 {ECO:0000313|EMBL:EHR33593.1,
RC   ECO:0000313|Proteomes:UP000005963};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Megamonas funiformis YIT 11815.";
RL   Submitted (JAN-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|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-phosphate:
CC       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 EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHR33593.1}.
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DR   EMBL; ADMB01000093; EHR33593.1; -; Genomic_DNA.
DR   RefSeq; WP_008539762.1; NZ_JH601092.1.
DR   EnsemblBacteria; EHR33593; EHR33593; HMPREF9454_02167.
DR   PATRIC; fig|742816.3.peg.2102; -.
DR   OrthoDB; 687380at2; -.
DR   BioCyc; GCF_000245775-HMP:HMPREF9454_RS10670-MONOMER; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000005963; 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; -; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00056, 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..264
FT                   /note="DAHP_synth_1"
FT                   /evidence="ECO:0000259|Pfam:PF00793"
FT   COILED          253..273
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   276 AA;  30189 MW;  A9320E0A3E8ED672 CRC64;
     MHTVKIGNFE VGAGNPLVLL AGPCVLESYE RSLYIGKTIK EITSRLGIPY VFKASFDKAN
     RSSYNGYRGP GLEKGLKWLQ SIKDELNVPV VTDIHNETQV EPVSKVVDVL QIPAFLSRQT
     DLLYTAAKSG CVVNVKKGQF LAPADMKNVV KKLEEAGSEK ILLTERGASF GYNNLVVDMR
     SFPIMRSTGY PVIFDATHSV QLPGGAGTSS AGNREYVEFL ARGAAGVGVD GFFMEVHDNP
     EEALCDGPNM VYLDKLEDLL KDLIAINEIT KKKINK
//
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