(data stored in ACNUC4362 zone)

HOGENOM: ARATH_5_PE5533

ID   ARATH_5_PE5533                       STANDARD;      PRT;   608 AA.
AC   ARATH_5_PE5533; Q9FGX1;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=ATP-citrate synthase beta chain protein 2;
DE   Short=ATP-citrate synthase B-2; EC=2.3.3 8;AltName: Full=ATP-citrate
DE   lyase B-2;AltName: Full=Citrate cleavage enzyme B-2; (ARATH_5.PE5533).
GN   Name=ACLB-2; OrderedLocusNames=At5g49460; ORFNames=K7J8.14;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_5.PE5533.
CC       Arabidopsis thaliana chromosome 5 TAIR10 full sequence 1..26975502
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:ACLB2_ARATH
CC   -!- FUNCTION: ATP citrate-lyase is the primary enzyme responsible for
CC       the synthesis of cytosolic acetyl-CoA, used for the elongation of
CC       fatty acids and biosynthesis of isoprenoids, flavonoids and
CC       malonated derivatives. May supply substrate to the cytosolic
CC       acetyl-CoA carboxylase, which generates the malonyl-CoA used for
CC       the synthesis of a multitude of compounds, including very long
CC       chain fatty acids and flavonoids. Required for normal growth and
CC       development and elongation of C18 fatty acids to C20 to C24 fatty
CC       acids in seeds. n contrast to all known animal ACL enzymes having
CC       a homomeric structure, plant ACLs are composed of alpha and beta
CC       chains.
CC   -!- CATALYTIC ACTIVITY: ADP + phosphate + acetyl-CoA + oxaloacetate =
CC       ATP + citrate + CoA.
CC   -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains (Probable).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol.
CC   -!- TISSUE SPECIFICITY: Expressed in trichomes, epidermal leaf cells,
CC       anther tapetal cells, stigma and in young vascular bundles of
CC       expanding leaves, cotyledons, roots, pedicel of flowers and
CC       siliques.
CC   -!- DEVELOPMENTAL STAGE: Expressed in flower buds at stage 6 of
CC       development in tapetal cells and at stage 10 in the epidermal
CC       cells of growing petals and ovaries. In young siliques, expressed
CC       transiently in the inner integument of the ovules just prior to
CC       testal deposition. Expressed in the developing embryo with a
CC       maximal level at the heart and torpedo stages. The expression then
CC       disappears in the mature embryo. During seed germination,
CC       expressed in the vascular bundles, apical meristem, epidermis of
CC       the seedling cotyledon, stem, and root. Highly expressed in the
CC       root tip of seedlings 4 days after imbibition.
CC   -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha
CC       subunit family.
CC   -!- GENE_FAMILY: HOG000151479 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT5G49460;AT5G49460.1;AT5G49460.1.
DR   EMBL; AB023034; - ;
DR   EMBL; AK220717; - ;
DR   EMBL; AY035067; - ;
DR   EMBL; AY056594; - ;
DR   EMBL; AY062956; - ;
DR   UniProtKB/Swiss-Prot; Q9FGX1; -.
DR   EMBL; AB023034; BAB09916.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95814.1; -; Genomic_DNA.
DR   EMBL; AY035067; AAK59572.1; -; mRNA.
DR   EMBL; AY056594; AAL25638.1; -; mRNA.
DR   EMBL; AY062956; AAL33788.1; -; mRNA.
DR   IPI; IPI00537093; -.
DR   RefSeq; NP_199757.1; NM_124323.3.
DR   UniGene; At.19172; -.
DR   HSSP; P07459; 1SCU.
DR   ProteinModelPortal; Q9FGX1; -.
DR   SMR; Q9FGX1; 4-334, 380-599.
DR   STRING; Q9FGX1; -.
DR   PRIDE; Q9FGX1; -.
DR   EnsemblPlants; AT5G49460.1; AT5G49460.1; AT5G49460.
DR   GeneID; 835006; -.
DR   KEGG; ath:AT5G49460; -.
DR   NMPDR; fig|3702.1.peg.26786; -.
DR   TAIR; At5g49460; -.
DR   GeneTree; EPGT00070000030664; -.
DR   InParanoid; Q9FGX1; -.
DR   OMA; NTVARVT; -.
DR   PhylomeDB; Q9FGX1; -.
DR   ProtClustDB; PLN02522; -.
DR   ArrayExpress; Q9FGX1; -.
DR   Genevestigator; Q9FGX1; -.
DR   GO; GO:0009346; C:citrate lyase complex; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0003878; F:ATP citrate synthase activity; IDA:TAIR.
DR   GO; GO:0005488; F:binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:InterPro.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; TAS:TAIR.
DR   GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR   InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR   InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR   InterPro; IPR002020; Citrate_synthase-like.
DR   InterPro; IPR016141; Citrate_synthase-like_core.
DR   InterPro; IPR005810; CoA_lig_alpha.
DR   InterPro; IPR005811; CoA_ligase.
DR   InterPro; IPR016040; NAD(P)-bd_dom.
DR   InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR   InterPro; IPR016102; Succinyl-CoA_synth-like.
DR   Gene3D; G3DSA:1.10.580.10; Citrate_synthase_lrg_a-sub; 1.
DR   Gene3D; G3DSA:1.10.230.10; Citrate_synthase_sm_a-sub; 1.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Gene3D; G3DSA:3.40.50.261; Succinyl-CoA_synth-like; 1.
DR   Pfam; PF00285; Citrate_synt; 1.
DR   Pfam; PF00549; Ligase_CoA; 1.
DR   PRINTS; PR01798; SCOASYNTHASE.
DR   SUPFAM; SSF48256; Citrate_synthase_core; 1.
DR   PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR   PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
DR   PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1.
DR   HOGENOMDNA; ARATH_5.PE5533; -.
KW   AT5G49460pg.C_scaffold_1320000031; AT5G49460.10C_scaffold_1320000031;
KW   Q9FGX1; AB023034; AK220717; AY035067; AY056594; AY062956;
KW   Acyltransferase; ATP-binding; Complete proteome; Cytoplasm;
KW   Lipid synthesis; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transferase.
SQ   SEQUENCE   608 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MATGQLFSRT TQALFYNYKQ LPVQRMLDFD FLCGRETPSV AGIINPGSEG FQKLFFGQEE
     IAIPVHAAIE AACAAHPTAD VFINFASFRS AAASSMAALK QPTIKVVAII AEGVPESDTK
     QLIAYARANN KVVIGPATVG GIQAGAFKIG DTAGTIDNII QCKLYRPGSV GFVSKSGGMS
     NEMYNTVARV TDGIYEGIAI GGDVFPGSTL SDHILRFNNI PQIKMMVVLG ELGGRDEYSL
     VEALKEGKVN KPVVAWVSGT CARLFKSEVQ FGHAGAKSGG EMESAQAKNQ ALIDAGAIVP
     TSFEALESAI KETFEKLVEE GKVSPIKEVI PPQIPEDLNS AIKSGKVRAP THIISTISDD
     RGEEPCYAGV PMSSIIEQGY GVGDVISLLW FKRSLPRYCT KFIEICIMLC ADHGPCVSGA
     HNTIVTARAG KDLVSSLVSG LLTIGPRFGG AIDDAARYFK DACDRNLTPY EFVEGMKKKG
     IRVPGIGHRI KSRDNRDKRV ELLQKFARSN FPSVKYMEYA VTVETYTLSK ANNLVLNVDG
     AIGSLFLDLL AGSGMFTKQE IDEIVQIGYL NGLFVLARSI GLIGHTFDQK RLKQPLYRHP
     WEDVLYTK
//

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