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KDSA_ACIB3
ID   KDSA_ACIB3              Reviewed;         285 AA.
AC   B7H226;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
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};
GN   OrderedLocusNames=ABBFA_001556;
OS   Acinetobacter baumannii (strain AB307-0294).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=557600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AB307-0294;
RX   PubMed=18931120; DOI=10.1128/jb.00834-08;
RA   Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA   MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA   Bonomo R.A., Gill S.R.;
RT   "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT   baumannii.";
RL   J. Bacteriol. 190:8053-8064(2008).
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: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-phosphate:
CC       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}.
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DR   EMBL; CP001172; ACJ58772.1; -; Genomic_DNA.
DR   RefSeq; WP_000080538.1; NZ_CP001172.1.
DR   PDB; 6BNG; X-ray; 2.20 A; A/B=5-285.
DR   PDBsum; 6BNG; -.
DR   AlphaFoldDB; B7H226; -.
DR   SMR; B7H226; -.
DR   GeneID; 60879310; -.
DR   HOGENOM; CLU_036666_0_0_6; -.
DR   OMA; FRGIPTM; -.
DR   UniPathway; UPA00030; -.
DR   UniPathway; UPA00357; UER00474.
DR   Proteomes; UP000006924; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Lipopolysaccharide biosynthesis; Transferase.
FT   CHAIN           1..285
FT                   /note="2-dehydro-3-deoxyphosphooctonate aldolase"
FT                   /id="PRO_1000116872"
FT   STRAND          8..12
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          15..17
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          24..31
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           35..52
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          56..62
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           78..92
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          96..99
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           106..112
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           126..134
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          137..142
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           152..161
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          167..171
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           186..192
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   TURN            193..195
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          198..201
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           202..205
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           219..222
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   STRAND          236..245
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           259..261
FT                   /evidence="ECO:0007829|PDB:6BNG"
FT   HELIX           262..277
FT                   /evidence="ECO:0007829|PDB:6BNG"
SQ   SEQUENCE   285 AA;  31550 MW;  8A66BA33FB4865BA CRC64;
     MSQLKPQEVV RLGDIQMANH LPFVLFGGMN VLESKDLAFE IAETYIDICK RLDIPYVFKA
     SFDKANRSSL HSFRGPGLEK GIEWLGDIKK HFNVPIITDV HEPYQAAPVA EVADIIQLPA
     FLSRQTDLVE AMAKTQAIIN IKKAQFLAPH EMRHILHKCL EAGNDKLILC ERGSAFGYNN
     LVVDMLGFDI MKEMNVPVFF DVTHALQTPG GRSDSAGGRR AQITTLARAG MATGLAGLFL
     ESHPDPDKAK CDGPSALRLS QLEPFLAQLK ELDTLVKGFK KLDTH
 
 
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