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FABH2_CUPWR
ID   FABH2_CUPWR             Reviewed;         402 AA.
AC   P49245;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase 3 B, chloroplastic;
DE            EC=2.3.1.180;
DE   AltName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III B;
DE   AltName: Full=Beta-ketoacyl-ACP synthase III B;
DE            Short=KAS III B;
DE   Flags: Precursor;
GN   Name=KAS3B;
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).
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; U15934; AAA97534.1; -; mRNA.
DR   AlphaFoldDB; P49245; -.
DR   SMR; P49245; -.
DR   PRIDE; P49245; -.
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           ?..402
FT                   /note="3-oxoacyl-[acyl-carrier-protein] synthase 3 B,
FT                   chloroplastic"
FT                   /id="PRO_0000008734"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   402 AA;  42458 MW;  6A6FB1234069EC74 CRC64;
     MANAYGFVGH SVPTMKRAAQ FQQMGSGFCS ADSISKRVFC CSVVQGADKP ASGDSRTEYR
     TPRLVSRGCK LVGSGSAMPA LQVSNDDLSK IVDTNDEWIS VRTGIRNRRV LTGKESLTNL
     ATVAARKALE MAQVDANDVD MVLMCTSTPE DLFGSAPQIQ KALGCKKNPL AYDITAACSG
     FVLGLVSAAC HIRGGGFNNI LVIGADSLSR YVDWTDRGTC ILFGDAAGAV LVQSCDAEED
     GLFAFDLHSD GDGQRHLKAA ITENGIDHAV GSNGSVSDFP PRSSSYSCIQ MNGKEVFRFA
     CRCVPQSIES ALGKAGLNGS NIDWLLLHQA NQRIIDAVAT RLEVPQERVI SNLANYGNTS
     AASIPLALDE AVRGGKVKAG HLIATAGFGA GLTWGSAIVR WG
 
 
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