FABH_ARATH
ID FABH_ARATH Reviewed; 404 AA.
AC P49243; P93722; Q9SI84; Q9SXD3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=3-oxoacyl-[acyl-carrier-protein] synthase III, chloroplastic;
DE EC=2.3.1.180;
DE AltName: Full=Beta-ketoacyl-ACP synthase III;
DE Short=KAS III;
DE Flags: Precursor;
GN OrderedLocusNames=At1g62640; ORFNames=F23N19.2, T3P18.20;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=7991698; DOI=10.1104/pp.106.2.801;
RA Tai H., Post-Beittenmiller D., Jaworski J.G.;
RT "Cloning of a cDNA encoding 3-ketoacyl-acyl carrier protein synthase III
RT from Arabidopsis.";
RL Plant Physiol. 106:801-802(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Haouazine-Takvorian N., Takvorian A., Kreis M.;
RT "Cloning of a gene encoding 3-ketoacyl-acyl carrier protein synthase III
RT from Arabidopsis thaliana.";
RL (er) Plant Gene Register PGR97-149(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD43621.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF19534.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L31891; AAA61348.1; -; mRNA.
DR EMBL; Y11689; CAA72385.1; -; Genomic_DNA.
DR EMBL; AC005698; AAD43621.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007190; AAF19534.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33989.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33990.1; -; Genomic_DNA.
DR EMBL; AY063804; AAL36160.1; -; mRNA.
DR EMBL; AY091275; AAM14214.1; -; mRNA.
DR RefSeq; NP_001031221.1; NM_001036144.2.
DR RefSeq; NP_176452.1; NM_104942.4.
DR AlphaFoldDB; P49243; -.
DR SMR; P49243; -.
DR STRING; 3702.AT1G62640.1; -.
DR PaxDb; P49243; -.
DR PRIDE; P49243; -.
DR ProteomicsDB; 222440; -.
DR EnsemblPlants; AT1G62640.1; AT1G62640.1; AT1G62640.
DR EnsemblPlants; AT1G62640.2; AT1G62640.2; AT1G62640.
DR GeneID; 842561; -.
DR Gramene; AT1G62640.1; AT1G62640.1; AT1G62640.
DR Gramene; AT1G62640.2; AT1G62640.2; AT1G62640.
DR KEGG; ath:AT1G62640; -.
DR Araport; AT1G62640; -.
DR TAIR; locus:2026167; AT1G62640.
DR eggNOG; ENOG502QUK2; Eukaryota.
DR HOGENOM; CLU_039592_0_1_1; -.
DR InParanoid; P49243; -.
DR OMA; WGSEGDK; -.
DR OrthoDB; 689748at2759; -.
DR PhylomeDB; P49243; -.
DR BioCyc; ARA:AT1G62640-MON; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:P49243; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P49243; baseline and differential.
DR Genevisible; P49243; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
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; Reference proteome;
KW Transferase; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 44..404
FT /note="3-oxoacyl-[acyl-carrier-protein] synthase III,
FT chloroplastic"
FT /id="PRO_0000008732"
FT ACT_SITE 179
FT /evidence="ECO:0000250"
FT ACT_SITE 330
FT /evidence="ECO:0000250"
FT ACT_SITE 360
FT /evidence="ECO:0000250"
FT CONFLICT 108
FT /note="N -> T (in Ref. 1; AAA61348)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="G -> A (in Ref. 1; AAA61348)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="A -> D (in Ref. 1; AAA61348)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..268
FT /note="QND -> RNE (in Ref. 1; AAA61348)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="R -> S (in Ref. 1; AAA61348)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="M -> V (in Ref. 1; AAA61348)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 404 AA; 42847 MW; 72D49DFE4044B44E CRC64;
MANASGFFTH PSIPNLRSRI HVPVRVSGSG FCVSNRFSKR VLCSSVSSVD KDASSSPSQY
QRPRLVPSGC KLIGCGSAVP SLLISNDDLA KIVDTNDEWI ATRTGIRNRR VVSGKDSLVG
LAVEAATKAL EMAEVVPEDI DLVLMCTSTP DDLFGAAPQI QKALGCTKNP LAYDITAACS
GFVLGLVSAA CHIRGGGFKN VLVIGADSLS RFVDWTDRGT CILFGDAAGA VVVQACDIED
DGLFSFDVHS DGDGRRHLNA SVKESQNDGE SSSNGSVFGD FPPKQSSYSC IQMNGKEVFR
FAVKCVPQSI ESALQKAGLP ASAIDWLLLH QANQRIIDSV ATRLHFPPER VISNLANYGN
TSAASIPLAL DEAVRSGKVK PGHTIATSGF GAGLTWGSAI MRWR
