(data stored in SCRATCH zone)

SWISSPROT: E3J3K9_FRAIE

ID   E3J3K9_FRAIE            Unreviewed;       334 AA.
AC   E3J3K9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   08-MAY-2019, entry version 54.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 {ECO:0000256|HAMAP-Rule:MF_01815};
DE            EC=2.3.1.180 {ECO:0000256|HAMAP-Rule:MF_01815};
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE   AltName: Full=Beta-ketoacyl-ACP synthase III {ECO:0000256|HAMAP-Rule:MF_01815};
DE            Short=KAS III {ECO:0000256|HAMAP-Rule:MF_01815};
GN   Name=fabH {ECO:0000256|HAMAP-Rule:MF_01815};
GN   OrderedLocusNames=FraEuI1c_0123 {ECO:0000313|EMBL:ADP78211.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78211.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78211.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation reaction of fatty acid
CC       synthesis by the addition to an acyl acceptor of two carbons from
CC       malonyl-ACP. Catalyzes the first condensation reaction which
CC       initiates fatty acid synthesis and may therefore play a role in
CC       governing the total rate of fatty acid production. Possesses both
CC       acetoacetyl-ACP synthase and acetyl transacylase activities. Its
CC       substrate specificity determines the biosynthesis of branched-
CC       chain and/or straight-chain of fatty acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01815}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] +
CC         CO2 + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC         COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:78449,
CC         ChEBI:CHEBI:78450; EC=2.3.1.180; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01815, ECO:0000256|SAAS:SAAS01121373};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01815, ECO:0000256|SAAS:SAAS00048641}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01815,
CC       ECO:0000256|SAAS:SAAS00088601}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815,
CC       ECO:0000256|SAAS:SAAS00088631}.
CC   -!- DOMAIN: The last Arg residue of the ACP-binding site is essential
CC       for the weak association between ACP/AcpP and FabH.
CC       {ECO:0000256|HAMAP-Rule:MF_01815}.
CC   -!- SIMILARITY: Belongs to the FabH family. {ECO:0000256|HAMAP-
CC       Rule:MF_01815, ECO:0000256|SAAS:SAAS00554340}.
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DR   EMBL; CP002299; ADP78211.1; -; Genomic_DNA.
DR   RefSeq; WP_013421334.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0123; -.
DR   EnsemblBacteria; ADP78211; ADP78211; FraEuI1c_0123.
DR   KEGG; fri:FraEuI1c_0123; -.
DR   eggNOG; ENOG4105CCZ; Bacteria.
DR   eggNOG; COG0332; LUCA.
DR   HOGENOM; HOG000246674; -.
DR   KO; K00648; -.
DR   OMA; RTTCIIF; -.
DR   OrthoDB; 872193at2; -.
DR   BioCyc; FSP298654:G1GOT-125-MONOMER; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002484; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0033818; F:beta-ketoacyl-acyl-carrier-protein synthase III activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.47.10; -; 2.
DR   HAMAP; MF_01815; FabH; 1.
DR   InterPro; IPR013751; ACP_syn_III.
DR   InterPro; IPR013747; ACP_syn_III_C.
DR   InterPro; IPR004655; FabH_synth.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF08545; ACP_syn_III; 1.
DR   Pfam; PF08541; ACP_syn_III_C; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   TIGRFAMs; TIGR00747; fabH; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J3K9.
DR   SWISS-2DPAGE; E3J3K9.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00440245, ECO:0000313|EMBL:ADP78211.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048623};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00440270};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00088611};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00440289};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00440256}; Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00160587};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00440538, ECO:0000313|EMBL:ADP78211.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    308    328       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      117    193       ACP_syn_III. {ECO:0000259|Pfam:PF08545}.
FT   DOMAIN      243    332       ACP_syn_III_C. {ECO:0000259|Pfam:
FT                                PF08541}.
FT   REGION      260    264       ACP-binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01815}.
FT   ACT_SITE    123    123       {ECO:0000256|HAMAP-Rule:MF_01815}.
FT   ACT_SITE    259    259       {ECO:0000256|HAMAP-Rule:MF_01815}.
FT   ACT_SITE    290    290       {ECO:0000256|HAMAP-Rule:MF_01815}.
SQ   SEQUENCE   334 AA;  34524 MW;  4AA8C7F5DE7B38E5 CRC64;
     MTVELRSSVG AAGARILGVG AYRPPRVVPN SEISEAIDSS DEWIVSRSGI RSRRFAGADE
     PLGSMAAGAA GKAMAHAGIS AADLGCVLVA TMSNVVQSPS LATDVAARLG AEGVAAFDVS
     AACAGFSYAL AMANDMIRAG SARYVVVVGA ERMTDIIDPY DRGTAFLFGD GAGAVVVGPS
     DTAGIGPVVW GSDASKRDVI GHDSSYLEWR ESPERPWPVM RMDGPQVFRW ASWQMAPVAQ
     RALAAAGIEA SDLAAFIPHQ ANIRIIDTMC RVLKLPKSVV VARDIATTGN TSGASIPLAM
     EDLLARQLAP SGGLALLVGF GAGLVYAAQV VRLP
//

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