(data stored in SCRATCH zone)

SWISSPROT: C7PXF3_CATAD

ID   C7PXF3_CATAD            Unreviewed;       339 AA.
AC   C7PXF3;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 56.
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_0567 {ECO:0000313|EMBL:ACU69504.1};
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:ACU69504.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69504.1, 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}.
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DR   EMBL; CP001700; ACU69504.1; -; Genomic_DNA.
DR   RefSeq; WP_012784799.1; NC_013131.1.
DR   ProteinModelPortal; C7PXF3; -.
DR   STRING; 479433.Caci_0567; -.
DR   EnsemblBacteria; ACU69504; ACU69504; Caci_0567.
DR   KEGG; cai:Caci_0567; -.
DR   eggNOG; ENOG4105CCZ; Bacteria.
DR   eggNOG; COG0332; LUCA.
DR   HOGENOM; HOG000246674; -.
DR   KO; K00648; -.
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; C7PXF3.
DR   SWISS-2DPAGE; C7PXF3.
KW   Acyltransferase {ECO:0000256|HAMAP-Rule:MF_01815,
KW   ECO:0000256|SAAS:SAAS00048631, ECO:0000313|EMBL:ACU69504.1};
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:ACU69504.1}.
FT   DOMAIN      110    190       ACP_syn_III. {ECO:0000259|Pfam:PF08545}.
FT   DOMAIN      241    330       ACP_syn_III_C. {ECO:0000259|Pfam:
FT                                PF08541}.
FT   REGION      258    262       ACP-binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_01815}.
FT   ACT_SITE    116    116       {ECO:0000256|HAMAP-Rule:MF_01815}.
FT   ACT_SITE    257    257       {ECO:0000256|HAMAP-Rule:MF_01815}.
FT   ACT_SITE    287    287       {ECO:0000256|HAMAP-Rule:MF_01815}.
SQ   SEQUENCE   339 AA;  35000 MW;  009DFE17DFBD435C CRC64;
     MTTRAAVVQG VGGCVPPRSV DNNELSSRLE TSDAWIRERL GIGRRYVADG VSTVDLAVEA
     GARALEMADA GAGLGPLDVV LLATTTPDRL CPASAPEVAS RLGYTGIAAF DVNAVCAGFV
     HALATGNALI RGHMADRVLV IGADTFTTLV DPADRLTASI FGDGAGALVL RAGTPDEPGA
     LRAFDLGSDG SQVATVEVPG GGARDRLGMP VANQRPYLVM DGPAVFRRAV QEMTASSLRV
     LAKAKWDAGS VRRFVPHQAN IRIIRGVAER LGIGAERVVA NIEDVGNTVA ASIPLALADA
     HDSGRLGAGE RVLMTSIGAG LAWGSAVLTW PELQGKARL
//

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