GenomeNet

Database: UniProt
Entry: KDSA_FUSNN
LinkDB: KDSA_FUSNN
Original site: KDSA_FUSNN 
ID   KDSA_FUSNN              Reviewed;         278 AA.
AC   Q8RE91;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 2.
DT   18-SEP-2019, entry version 105.
DE   RecName: Full=2-dehydro-3-deoxyphosphooctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
DE            EC=2.5.1.55 {ECO:0000255|HAMAP-Rule:MF_00056};
DE   AltName: Full=3-deoxy-D-manno-octulosonic acid 8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE   AltName: Full=KDO-8-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE            Short=KDO 8-P synthase {ECO:0000255|HAMAP-Rule:MF_00056};
DE            Short=KDOPS {ECO:0000255|HAMAP-Rule:MF_00056};
DE   AltName: Full=Phospho-2-dehydro-3-deoxyoctonate aldolase {ECO:0000255|HAMAP-Rule:MF_00056};
GN   Name=kdsA {ECO:0000255|HAMAP-Rule:MF_00056}; OrderedLocusNames=FN1224;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP
OS   101130 / JCM 8532 / LMG 13131).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae;
OC   Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L.,
RA   Vasieva O., Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A.,
RA   Larsen N., D'Souza M., Walunas T., Pusch G., Haselkorn R.,
RA   Fonstein M., Kyrpides N.C., Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium
RT   nucleatum strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
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:0000255|HAMAP-Rule:MF_00056};
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:0000255|HAMAP-Rule:MF_00056}.
CC   -!- PATHWAY: Bacterial outer membrane biogenesis; lipopolysaccharide
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00056}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00056}.
CC   -!- SIMILARITY: Belongs to the KdsA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00056}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL95420.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE009951; AAL95420.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_604121.1; NC_003454.1.
DR   SMR; Q8RE91; -.
DR   STRING; 190304.FN1224; -.
DR   PRIDE; Q8RE91; -.
DR   EnsemblBacteria; AAL95420; AAL95420; FN1224.
DR   GeneID; 992017; -.
DR   KEGG; fnu:FN1224; -.
DR   PATRIC; fig|190304.8.peg.1787; -.
DR   eggNOG; ENOG4105CXR; Bacteria.
DR   eggNOG; COG2877; LUCA.
DR   HOGENOM; HOG000023021; -.
DR   InParanoid; Q8RE91; -.
DR   KO; K01627; -.
DR   OMA; FRGIPTM; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000002521; 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; -; 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   Complete proteome; Cytoplasm; Lipopolysaccharide biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN         1    278       2-dehydro-3-deoxyphosphooctonate
FT                                aldolase.
FT                                /FTId=PRO_0000187128.
SQ   SEQUENCE   278 AA;  30937 MW;  AF0B460EA5309AE8 CRC64;
     MLINDVNKVK VGNIVFGGKK RFVLIAGPCV MESQELMDEV AGGIKEICDR LGIEYIFKAS
     FDKANRSSIY SYRGPGLEEG MKMLTKIKEK FNVPVITDVH EAWQCKEVAK VADILQIPAF
     LCRQTDLLIA AAETGKAVNI KKGQFLAPWD MKNIVVKMEE SRNKNIMLCE RGSTFGYNNM
     VVDMRSLLEM RKFNYPVIFD VTHSVQKPGG LGTATSGDRE YVYPLLRAGL AIGVDAIFAE
     VHPNPAEAKS DGPNMLYLKD LEEILKIAIE IDKIVKGV
//
DBGET integrated database retrieval system