ACLB1_ORYSJ
ID ACLB1_ORYSJ Reviewed; 608 AA.
AC Q93VT8; A0A0P0V1J6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=ATP-citrate synthase beta chain protein 1;
DE Short=ATP-citrate synthase B-1;
DE EC=2.3.3.8;
DE AltName: Full=ATP-citrate lyase B-1;
DE AltName: Full=Citrate cleavage enzyme B-1;
GN Name=ACLB-1; OrderedLocusNames=Os01g0300200, LOC_Os01g19450;
GN ORFNames=OsJ_01435, P0487H02.31, P0682B08.9;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
CC -!- FUNCTION: ATP citrate-lyase is the primary enzyme responsible for the
CC synthesis of cytosolic acetyl-CoA, used for the elongation of fatty
CC acids and biosynthesis of isoprenoids, flavonoids and malonated
CC derivatives. May supply substrate to the cytosolic acetyl-CoA
CC carboxylase, which generates the malonyl-CoA used for the synthesis of
CC a multitude of compounds, including very long chain fatty acids and
CC flavonoids. In contrast to all known animal ACL enzymes having a
CC homomeric structure, plant ACLs are composed of alpha and beta chains
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ADP + oxaloacetate + phosphate = ATP + citrate +
CC CoA; Xref=Rhea:RHEA:21160, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:456216; EC=2.3.3.8;
CC -!- SUBUNIT: Heterooctamer of 4 alpha and 4 beta chains. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000305}.
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DR EMBL; AP002883; BAB67865.1; -; Genomic_DNA.
DR EMBL; AP003578; BAB60936.1; -; Genomic_DNA.
DR EMBL; AP008207; BAF04731.1; -; Genomic_DNA.
DR EMBL; AP014957; BAS71711.1; -; Genomic_DNA.
DR EMBL; CM000138; EAZ11568.1; -; Genomic_DNA.
DR EMBL; AK070568; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; XP_015621337.1; XM_015765851.1.
DR AlphaFoldDB; Q93VT8; -.
DR SMR; Q93VT8; -.
DR STRING; 4530.OS01T0300200-01; -.
DR PaxDb; Q93VT8; -.
DR PRIDE; Q93VT8; -.
DR EnsemblPlants; Os01t0300200-01; Os01t0300200-01; Os01g0300200.
DR EnsemblPlants; Os01t0300200-02; Os01t0300200-02; Os01g0300200.
DR GeneID; 4325777; -.
DR Gramene; Os01t0300200-01; Os01t0300200-01; Os01g0300200.
DR Gramene; Os01t0300200-02; Os01t0300200-02; Os01g0300200.
DR KEGG; osa:4325777; -.
DR eggNOG; KOG1254; Eukaryota.
DR InParanoid; Q93VT8; -.
DR OMA; IHVPDTF; -.
DR OrthoDB; 349367at2759; -.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000007752; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; Q93VT8; baseline and differential.
DR Genevisible; Q93VT8; OS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003878; F:ATP citrate synthase activity; IBA:GO_Central.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR Gene3D; 3.40.50.261; -; 1.
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.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR005811; CoA_ligase.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR Pfam; PF00285; Citrate_synt; 1.
DR Pfam; PF00549; Ligase_CoA; 1.
DR SUPFAM; SSF48256; SSF48256; 1.
DR SUPFAM; SSF51735; SSF51735; 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.
PE 2: Evidence at transcript level;
KW Acyltransferase; ATP-binding; Cytoplasm; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..608
FT /note="ATP-citrate synthase beta chain protein 1"
FT /id="PRO_0000412223"
FT ACT_SITE 273
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 214..234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 265..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 292..302
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000255"
FT CONFLICT 465
FT /note="R -> G (in Ref. 6; AK070568)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 608 AA; 66070 MW; 88C0D912DF9F5765 CRC64;
MATGQIFSKT TQALFYNYKQ LPIQRMLDFD FLCGRETPSV AGIINPGSDG FQKLFFGQEE
IAIPVHPTIE AACNAHPTAD VFINFASFRS AAASSMSALK QPTIRVVAII AEGVPESDTK
QLISYARANN KVIIGPATVG GIQAGAFKIG DTAGTIDNII QCKLYRPGSV GFVSKSGGMS
NEMYNTIARV TDGIYEGIAI GGDVFPGSTL SDHILRFNNI PQVKMMVVLG ELGGKDEYSL
VEALKQGKVQ KPVVAWVSGT CARLFKSEVQ FGHAGAKSGG ELESAQAKNQ ALKDAGAVVP
TSYEALETAI KETFEKLVED GKISPVTEIT PPPIPEDLKT AIKSGKVRAP THIISTISDD
RGEEPCYAGV PMSTIIEQGY GVGDVISLLW FKRSLPRYCT QFIEMCIMLC ADHGPCVSGA
HNSIVTARAG KDLVSSLVSG LLTIGPRFGG AIDDAARYFK DAYDRNLTPY EFVEGMKKKG
IRVPGIGHRI KSRDNRDKRV QLLQKYAHTH FPSVKYMEYA VQVETYTLSK ANNLVLNVDG
AIGSLFLDLL SGSGMFSKQE IDEIVEIGYL NGLFVLARSI GLIGHTFDQK RLKQPLYRHP
WEDVLYTK
