ACC1_ORYSJ
ID ACC1_ORYSJ Reviewed; 2267 AA.
AC Q8S6N5; B9G5C9; Q0IY62; Q7G3D3;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Acetyl-CoA carboxylase 1;
DE EC=6.4.1.2;
DE Includes:
DE RecName: Full=Biotin carboxylase;
DE EC=6.3.4.14;
GN Name=ACC1; OrderedLocusNames=Os10g0363300, LOC_Os10g21910;
GN ORFNames=OsJ_31236, OSJNBa0073L01.2;
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=12791992; DOI=10.1126/science.1083523;
RA Yu Y., Rambo T., Currie J., Saski C., Kim H.-R., Collura K., Thompson S.,
RA Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S., Henry D.,
RA Oates R., Palmer M., Pries G., Gibson J., Anderson H., Paradkar M.,
RA Crane L., Dale J., Carver M.B., Wood T., Frisch D., Engler F.,
RA Soderlund C., Palmer L.E., Teytelman L., Nascimento L., De la Bastide M.,
RA Spiegel L., Ware D., O'Shaughnessy A., Dike S., Dedhia N., Preston R.,
RA Huang E., Ferraro K., Kuit K., Miller B., Zutavern T., Katzenberger F.,
RA Muller S., Balija V., Martienssen R.A., Stein L., Minx P., Johnson D.,
RA Cordum H., Mardis E., Cheng Z., Jiang J., Wilson R., McCombie W.R.,
RA Wing R.A., Yuan Q., Ouyang S., Liu J., Jones K.M., Gansberger K.,
RA Moffat K., Hill J., Tsitrin T., Overton L., Bera J., Kim M., Jin S.,
RA Tallon L., Ciecko A., Pai G., Van Aken S., Utterback T., Reidmuller S.,
RA Bormann J., Feldblyum T., Hsiao J., Zismann V., Blunt S., de Vazeille A.R.,
RA Shaffer T., Koo H., Suh B., Yang Q., Haas B., Peterson J., Pertea M.,
RA Volfovsky N., Wortman J., White O., Salzberg S.L., Fraser C.M., Buell C.R.,
RA Messing J., Song R., Fuks G., Llaca V., Kovchak S., Young S., Bowers J.E.,
RA Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT "In-depth view of structure, activity, and evolution of rice chromosome
RT 10.";
RL Science 300:1566-1569(2003).
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).
CC -!- FUNCTION: Multifunctional enzyme that catalyzes the carboxylation of
CC acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty
CC acid synthesis and in the cytosol in various biosynthetic pathways
CC including fatty acid elongation. {ECO:0000250|UniProtKB:Q38970}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-
CC CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2;
CC Evidence={ECO:0000250|UniProtKB:O04983};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC ChEBI:CHEBI:456216; EC=6.3.4.14;
CC Evidence={ECO:0000250|UniProtKB:O04983};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409,
CC ECO:0000255|PROSITE-ProRule:PRU00969};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-
CC ProRule:PRU00969};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP53321.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF26353.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=EEE50826.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC092548; AAM18728.1; -; Genomic_DNA.
DR EMBL; DP000086; AAP53321.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008216; BAF26353.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014966; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CM000147; EEE50826.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_015614129.1; XM_015758643.1.
DR RefSeq; XP_015614130.1; XM_015758644.1.
DR AlphaFoldDB; Q8S6N5; -.
DR SMR; Q8S6N5; -.
DR BioGRID; 817487; 1.
DR STRING; 4530.OS10T0363300-01; -.
DR PaxDb; Q8S6N5; -.
DR PRIDE; Q8S6N5; -.
DR EnsemblPlants; Os10t0363300-01; Os10t0363300-01; Os10g0363300.
DR GeneID; 4348450; -.
DR Gramene; Os10t0363300-01; Os10t0363300-01; Os10g0363300.
DR KEGG; osa:4348450; -.
DR eggNOG; KOG0368; Eukaryota.
DR HOGENOM; CLU_004031_1_0_1; -.
DR InParanoid; Q8S6N5; -.
DR OrthoDB; 156081at2759; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000000763; Chromosome 10.
DR Proteomes; UP000007752; Chromosome 10.
DR Proteomes; UP000059680; Chromosome 10.
DR Genevisible; Q8S6N5; OS.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR013537; AcCoA_COase_cen.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF08326; ACC_central; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Biotin; Cytoplasm; Fatty acid biosynthesis;
KW Fatty acid metabolism; Ligase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Manganese; Metal-binding; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..2267
FT /note="Acetyl-CoA carboxylase 1"
FT /id="PRO_0000412213"
FT DOMAIN 38..544
FT /note="Biotin carboxylation"
FT DOMAIN 190..384
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 671..745
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT DOMAIN 1502..1843
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 1847..2163
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1502..2163
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT ACT_SITE 357
FT /evidence="ECO:0000250"
FT BINDING 216..273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 353
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 353
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 355
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409,
FT ECO:0000255|PROSITE-ProRule:PRU00969"
FT BINDING 1752
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2053
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT BINDING 2055
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250"
FT MOD_RES 712
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ SEQUENCE 2267 AA; 252809 MW; 0B994DBBB3157FB1 CRC64;
MEGSYQMNGI LNGMSNSRHP SSPSEVDEFC KALGGDSPIH SVLVANNGMA AVKFMRSIRT
WALETFGTEK AILLVAMATP EDLKINAEHI RIADQFVEVP GGTNNNNYAN VQLIVEIAER
THVSAVWPGW GHASENPELP DALKEKGIIF LGPPSAAMAA LGDKIGSSLI AQAAGVPTLP
WSGSHVKIPP ESCNSIPEEM YRSACVSTTE EAVASCQVVG YPAMIKASWG GGGKGIRKVH
NDDEVRALFK QVQGEVPGSP IFIMKVASQS RHLEVQLLCD KHGNVAALHS RDCSVQRRHQ
KIIEEGPITV APSETVKELE QAARRLAKCV HYVGAATVEY LYSMETGEYY FLELNPRLQV
EHPVTEWIAE INLPAAQVVV GMGVPLYNIP EIRRFYGMEH GGGYDAWRKI SAVATKFDLD
NAQSVKPKGH CVAVRVTSED PDDGFKPTSG RVEELNFKSK PNVWAYFSVK SGGAIHEFSD
SQFGHVFAFG ESRSLAIANM VLGLKEIQIR GEIRTNVDYT VDLLNAAEYR ENKIHTGWLD
SRIAMRVRAE RPPWYLSVVG GALYEASSRS SSVVTDYVGY LSKGQIPPKH ISLVNLTVTL
NIEGSKYTIE TVRRGPRSYT LRMNGSEIEA EIHSLRDGGL LMQLDGNSHV IYAETEAAGT
RLLINGRTCL LQKEHDPSKL LADTPCKLLR FLVADGSHVD ADTPYAEVEV MKMCMPLLLP
ASGVIHFVMP EGQAMQAADL IARLDLDDPS SVRRAEPFHG TFPKLGPPTA VSGKVHQKFA
ASVNSAHMIL AGYEHNINEV VQDLLNCLDS PELPFLQWQE LMSVLATRLP KDLRNELDGK
YKEYELNSDF RKNKDFPAKL LRGIIEANLA YCSEKDRVTN ERLVEPLMSL VKSYEGGRES
HARVVVKSLF EEYLSVEELF SDNIQSDVIE RLRLQHAKDL EKVVYIVFSH QGVRTKNKLI
LRLMEALVYP NPSAYRDQLI RFSGLNNTVY SELALKASQL LEHTKLSELR TSIARSLSEL
EMFTEEGERV STPRRKMAIN ERMEDLVGAP LAVEDALVAL FDHSDPTLQR RVVETYIRRL
YQPYLVKGSV RMQWHRSGLI ALWEFSEEHI KQRNGQDAMS LKQQVEDPEE KRWGVMVVIK
SLQYLSSAID AALKETSHYK AGAGNVSNGN SASSSHGNML HIALVGINNQ MSTLQDSGDE
DQAQERINKI SKILKDSTVT SHLNGAGVRV VSCIIQRDEG RPPMRHSFQW SVDKIYYEED
PMLRHVEPPL STFLELNKVN LDGYNEVKYT PSRDRQWHIY TLIKNKKDQR SNDQRLFLRT
IVRQPGVTNG FLSGNVDNEV GRAQASSSYT SSSILRSLMA ALEEIELHAH NETVRSSYSH
MYLCILRVQQ LFDLIPFSRT IDNVGQDEAT ACTLLKNMAL NIYEHVGVRM HRLSVCQWEV
KLWLDCDGQA SGAWRVVVTN VTGHTCTVDI YREVEDSNTH KLFYHSVTPS LGPLHGIVLD
EPYKPLDAID LKRYSARKNE TTYCYDFPLA FETALKRSWK STLSVVAEAN EHNKSYAKVT
ELMFADSTGS WGTPLVPVER SPGINDIGIV AWIMKLSTPE FPSGREIIVV SNDVTFKAGS
FGPREDAFFD AVTNLACERK LPLIYLSATA GARLGVAEEI KACFNVGWSD DESPERGFHY
IYLTEQDYSR LSSSVIAHEL KLESGETRWV VDTIVGKEDG LGCENLHGSG AIASAYSKAY
KETFTLTFVT GRAVGIGAYL ARLGMRCIQR LDQPIILTGF SALNKLLGRE VYSSHMQLGG
PKIMATNGVV HLTVSDDLEG VSAILKWLSY VPPYVGGPLP IMKPLDPPDR PVTYFPENSC
DARAAICGVQ DSQGKWMGGM FDRESFVETL EGWAKTVVTG RAKLGGIPVG VIAVETQTMM
QVIPADPGQL DSAERVVPQA GQVWFPDSAT KTAQALLDFN REELPLFILA NWRGFSGGQR
DLFEGILQAG SNIVENLRTY NQPAFVYIPM GGELRGGAWV VVDSKINPEH IEMYAERTAK
GNVLEPEGLV EIKFRPKELE ECMLRLDPEL IKLSTRLREM KKENAGLSEM DTTRRSIIAR
MKQLMPIYTQ VATRFAELHD TSARMAAKGV IGKVVDWEES RSFFYRRLRR RVTEDALAKE
IREAAGEQLS QKSALDYIKK WYLSSNGSDG NSEKWNNDEA FFAWKDDPTN YENQLEELKA
ERVSKWLSRL AESPDVKALP NGLSIVLNKM NPSKREQVID GLRQLLG
