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FABH1_CUPWR
ID   FABH1_CUPWR             Reviewed;         400 AA.
AC   P49244;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 A, chloroplastic;
DE            EC=2.3.1.180;
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III A;
DE   AltName: Full=Beta-ketoacyl-ACP synthase III A;
DE            Short=KAS III A;
DE   Flags: Precursor;
GN   Name=KAS3A;
OS   Cuphea wrightii (Wright's waxweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Lythraceae; Cuphea.
OX   NCBI_TaxID=35942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Embryo;
RX   PubMed=7784524; DOI=10.1104/pp.108.1.443;
RA   Slabaugh M.B., Tai H., Jaworski J., Knapp S.J.;
RT   "cDNA clones encoding beta-ketoacyl-acyl carrier protein synthase III from
RT   Cuphea wrightii.";
RL   Plant Physiol. 108:443-444(1995).
RN   [2]
RP   SEQUENCE REVISION TO 18-34.
RA   Slabaugh M.B., Tai H., Jaworski J., Knapp S.J.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis
CC       by the addition to an acyl acceptor of two carbons from malonyl-ACP.
CC       KAS III catalyzes the first condensation reaction which initiates fatty
CC       acid synthesis and may therefore play a role in governing the total
CC       rate of fatty acid production. Possesses both acetoacetyl-ACP synthase
CC       and acetyl transacylase activities (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + H(+) + malonyl-[ACP] = 3-oxobutanoyl-[ACP] + CO2
CC         + CoA; Xref=Rhea:RHEA:12080, Rhea:RHEA-COMP:9623, Rhea:RHEA-
CC         COMP:9625, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:78449, ChEBI:CHEBI:78450;
CC         EC=2.3.1.180;
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. FabH family.
CC       {ECO:0000305}.
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DR   EMBL; U15935; AAA97533.1; -; mRNA.
DR   AlphaFoldDB; P49244; -.
DR   SMR; P49244; -.
DR   PRIDE; P49244; -.
DR   BRENDA; 2.3.1.180; 1755.
DR   UniPathway; UPA00094; -.
DR   GO; GO:0009507; C:chloroplast; 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-EC.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.47.10; -; 1.
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   2: Evidence at transcript level;
KW   Chloroplast; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Plastid; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..400
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 A,
FT                   chloroplastic"
FT                   /id="PRO_0000008733"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        326
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        356
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  42415 MW;  7A0AE5589BEB0535 CRC64;
     MANASGFLGS SVPALRRATQ PQHSISSSRG SSSDFVFKRV FCCSAVQGSD RQSLGDSRSP
     RLVSRGCKLI GSGSAIPSLQ ISNDDLAKIV DTNDEWISVR TGIRNRRVLT GKDSLTNLAS
     EAARKALEMA QIDADDVDMV LMCTSTPEDL FGSAPQISKA LGCKKNPLSY DITAACSGFV
     LGLVSAACHI RGGGFNNVLV IGADSLSRYV DWTDRGTCIL FGDAAGAVVV QSCDAEEDGL
     FAFDLHSDGD GQRHLKAAIK EDEVDKALGS NGSIRDFPPR RSSYSCIQMN GKEVFRFACR
     CVPQSIESAL GKAGLNGSNI DWLLLHQANQ RIIDAVATRL EVPQERIISN LANYGNTSAA
     SIPLALDEAV RSGNVKPGHV IATAGFGAGL TWGSAIIRWG
 
 
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