GenomeNet

Database: UniProt
Entry: Q8S6N5
LinkDB: Q8S6N5
Original site: Q8S6N5 
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   13-FEB-2019, entry version 102.
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; Magnoliophyta; 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.,
RA   Thompson S., Simmons J., Yang T.-J., Nah G., Patel A.J., Thurmond S.,
RA   Henry D., Oates R., Palmer M., Pries G., Gibson J., Anderson H.,
RA   Paradkar M., Crane L., Dale J., Carver M.B., Wood T., Frisch D.,
RA   Engler F., Soderlund C., Palmer L.E., Teytelman L., Nascimento L.,
RA   De la Bastide M., Spiegel L., Ware D., O'Shaughnessy A., Dike S.,
RA   Dedhia N., Preston R., Huang E., Ferraro K., Kuit K., Miller B.,
RA   Zutavern T., Katzenberger F., Muller S., Balija V., Martienssen R.A.,
RA   Stein L., Minx P., Johnson D., Cordum H., Mardis E., Cheng Z.,
RA   Jiang J., Wilson R., McCombie W.R., Wing R.A., Yuan Q., Ouyang S.,
RA   Liu J., Jones K.M., Gansberger K., Moffat K., Hill J., Tsitrin T.,
RA   Overton L., Bera J., Kim M., Jin S., Tallon L., Ciecko A., Pai G.,
RA   Van Aken S., Utterback T., Reidmuller S., Bormann J., Feldblyum T.,
RA   Hsiao J., Zismann V., Blunt S., de Vazeille A.R., Shaffer T., Koo H.,
RA   Suh B., Yang Q., Haas B., Peterson J., Pertea M., Volfovsky N.,
RA   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.,
RA   Bowers J.E., Paterson A.H., Johns M.A., Mao L., Pan H., Dean R.A.;
RT   "In-depth view of structure, activity, and evolution of rice
RT   chromosome 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.,
RA   McCombie W.R., Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S.,
RA   Childs K.L., Davidson R.M., Lin H., Quesada-Ocampo L.,
RA   Vaillancourt B., Sakai H., Lee S.S., Kim J., Numa H., Itoh T.,
RA   Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using
RT   next 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.,
RA   Cong L., Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J.,
RA   Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X.,
RA   Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y.,
RA   Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J.,
RA   Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y.,
RA   Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y.,
RA   Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z.,
RA   Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T.,
RA   Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J.,
RA   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
CC       of acetyl-CoA, forming malonyl-CoA, which is used in the plastid
CC       for fatty acid synthesis and in the cytosol in various
CC       biosynthetic pathways including fatty acid elongation.
CC       {ECO:0000250|UniProtKB:Q38970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         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] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from 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};
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   UniGene; Os.9680; -.
DR   ProteinModelPortal; Q8S6N5; -.
DR   SMR; Q8S6N5; -.
DR   STRING; 39947.LOC_Os10g21910.1; -.
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   eggNOG; COG0439; LUCA.
DR   eggNOG; COG0511; LUCA.
DR   eggNOG; COG4799; LUCA.
DR   HOGENOM; HOG000214115; -.
DR   InParanoid; Q8S6N5; -.
DR   KO; K11262; -.
DR   OrthoDB; 156081at2759; -.
DR   Reactome; R-OSA-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-OSA-196780; Biotin transport and metabolism.
DR   Reactome; R-OSA-200425; Import of palmitoyl-CoA into the mitochondrial matrix.
DR   Reactome; R-OSA-75105; Fatty acyl-CoA biosynthesis.
DR   UniPathway; UPA00655; UER00711.
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; IEA:UniProtKB-EC.
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; IEA:UniProtKB-KW.
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; Complete proteome; Cytoplasm;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW   Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN         1   2267       Acetyl-CoA carboxylase 1.
FT                                /FTId=PRO_0000412213.
FT   DOMAIN       38    544       Biotin carboxylation.
FT   DOMAIN      190    384       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      671    745       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   DOMAIN     1502   1843       CoA carboxyltransferase N-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01136}.
FT   DOMAIN     1847   2163       CoA carboxyltransferase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01137}.
FT   NP_BIND     216    273       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   REGION     1502   2163       Carboxyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU01138}.
FT   ACT_SITE    357    357       {ECO:0000250}.
FT   METAL       339    339       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       353    353       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       353    353       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       355    355       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   BINDING    1752   1752       Coenzyme A. {ECO:0000250}.
FT   BINDING    2053   2053       Coenzyme A. {ECO:0000250}.
FT   BINDING    2055   2055       Coenzyme A. {ECO:0000250}.
FT   MOD_RES     712    712       N6-biotinyllysine. {ECO:0000255|PROSITE-
FT                                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
//
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