(data stored in ACNUC7421 zone)

SWISSPROT: C7PVG5_CATAD

ID   C7PVG5_CATAD            Unreviewed;       333 AA.
AC   C7PVG5;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 57.
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=Caci_0368 {ECO:0000313|EMBL:ACU69321.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69321.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69321.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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: Acetyl-CoA + malonyl-[acyl-carrier-protein] =
CC       acetoacetyl-[acyl-carrier-protein] + CoA + CO(2).
CC       {ECO:0000256|HAMAP-Rule:MF_01815, ECO:0000256|SAAS:SAAS00088656}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01815, ECO:0000256|SAAS:SAAS00362799}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01815,
CC       ECO:0000256|SAAS:SAAS00362904}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815,
CC       ECO:0000256|SAAS:SAAS00362812}.
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001700; ACU69321.1; -; Genomic_DNA.
DR   RefSeq; WP_012784616.1; NC_013131.1.
DR   ProteinModelPortal; C7PVG5; -.
DR   STRING; 479433.Caci_0368; -.
DR   EnsemblBacteria; ACU69321; ACU69321; Caci_0368.
DR   KEGG; cai:Caci_0368; -.
DR   eggNOG; ENOG4105CCZ; Bacteria.
DR   eggNOG; COG0332; LUCA.
DR   HOGENOM; HOG000246674; -.
DR   KO; K00648; -.
DR   OMA; IDLAGAC; -.
DR   OrthoDB; POG091H02M9; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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-HAMAP.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-HAMAP.
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; C7PVG5.
DR   SWISS-2DPAGE; C7PVG5.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048631, ECO:0000313|EMBL:ACU69321.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048670};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048619};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048625};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048628};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048646};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048649};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048661, ECO:0000313|EMBL:ACU69321.1}.
FT   DOMAIN      106    186       ACP_syn_III. {ECO:0000259|Pfam:PF08545}.
FT   DOMAIN      238    327       ACP_syn_III_C. {ECO:0000259|Pfam:
FT                                PF08541}.
FT   REGION      255    259       ACP-binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01815}.
FT   ACT_SITE    112    112       {ECO:0000256|HAMAP-Rule:MF_01815}.
FT   ACT_SITE    254    254       {ECO:0000256|HAMAP-Rule:MF_01815}.
FT   ACT_SITE    284    284       {ECO:0000256|HAMAP-Rule:MF_01815}.
SQ   SEQUENCE   333 AA;  34450 MW;  69E7202BD9A9EFC2 CRC64;
     MTKAAVISGI GSSVPASVVT NDMLAERLDT TDDWIRRLTG IQTRHWIEPG QATSDLAVEA
     GSRAIESAGG EPPQAVVLAT ITPDRPCPAT APEVASRLGL EGVAAFDVAA VCSGFVYGLA
     TGTGLIAAGI AERVLVIGAD TISTILDPTD RSTGVIFGDG AGAVMLRAGE ADEPGALQAL
     DLGSDGTGTD LITVPAGGSR QRSTKSVPPT TDTYLKMAGR EVFRESVRRM VESCEAVLER
     TGWDAADVDR LVPHQANLRI MNSVADRLGM PRDRAVVDLD RVGNTSAASI PLALARAAAE
     GTVESGHRLL LTAFGGGLTW GSATLTWPDI KPV
//

If you have problems or comments...

PBIL Back to PBIL home page