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Q38970

- ACC1_ARATH

UniProt

Q38970 - ACC1_ARATH

Protein

Acetyl-CoA carboxylase 1

Gene

ACC1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Multifunctional enzyme that catalyzes the carboxylation of acetyl-CoA, forming malonyl-CoA, which is used in the plastid for fatty acid synthesis and in the cytosol in various biosynthetic pathways including fatty acid elongation. Required for very long chain fatty acids elongation. Necessary for embryo and plant development. Plays a central function in embryo morphogenesis, especially in apical meristem development. Involved in cell proliferation and tissue patterning. May act as a repressor of cytokinin response.6 Publications

    Catalytic activityi

    ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.
    ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

    Cofactori

    Biotin.By similarity
    Binds 2 magnesium or manganese ions per subunit.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi338 – 3381Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi352 – 3521Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi352 – 3521Magnesium or manganese 2PROSITE-ProRule annotation
    Metal bindingi354 – 3541Magnesium or manganese 2PROSITE-ProRule annotation
    Active sitei356 – 3561By similarity
    Binding sitei1740 – 17401Coenzyme ABy similarity
    Binding sitei2041 – 20411Coenzyme ABy similarity
    Binding sitei2043 – 20431Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi215 – 27258ATPPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. acetyl-CoA carboxylase activity Source: TAIR
    2. ATP binding Source: UniProtKB-KW
    3. biotin carboxylase activity Source: UniProtKB-EC
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. embryo development ending in seed dormancy Source: TAIR
    2. fatty acid elongation Source: TAIR
    3. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
    4. meristem structural organization Source: TAIR
    5. primary shoot apical meristem specification Source: TAIR
    6. response to cytokinin Source: TAIR
    7. root development Source: TAIR
    8. shoot system development Source: TAIR

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT1G36160-MONOMER.
    ARA:GQT-1121-MONOMER.
    ReactomeiREACT_185257. Defective HLCS causes multiple carboxylase deficiency.
    REACT_187915. Biotin transport and metabolism.
    UniPathwayiUPA00655; UER00711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acetyl-CoA carboxylase 1 (EC:6.4.1.2)
    Short name:
    AtACC1
    Alternative name(s):
    Protein EMBRYO DEFECTIVE 22
    Protein GURKE
    Protein PASTICCINO 3
    Including the following 1 domains:
    Biotin carboxylase (EC:6.3.4.14)
    Gene namesi
    Name:ACC1
    Synonyms:EMB22, GK, PAS3
    Ordered Locus Names:At1g36160
    ORF Names:F15C21.1
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G36160.

    Subcellular locationi

    Cytoplasmcytosol Curated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. plasma membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Embryo lethal with an arrest in development at the late globular stage in acc1-1 and acc1-2 null allele mutants. In the leaky pas3 and gk alleles, defect in embryo development, very short and thick hypocotyl and misshaped cotyledons that do not expand. Abnormal root development, abnormal fused leaves and compact rosettes with multiple shoots. Uncoordinated cell divisions in the apical region. Reduced levels of very long chain fatty acids in seeds.5 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1588 – 15881E → K in pas3-1; developmental phenotype and reduced levels of very long chain fatty acids in seeds. 1 Publication
    Mutagenesisi1787 – 17871G → S in pas3-2; developmental phenotype and reduced levels of very long chain fatty acids in seeds. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 22542254Acetyl-CoA carboxylase 1PRO_0000412211Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1031 – 10311Phosphothreonine1 Publication
    Modified residuei1192 – 11921Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ38970.

    Expressioni

    Tissue specificityi

    Expressed in roots, trichomes, epidermal leaf cells, siliques, petals, anthers, and seeds.4 Publications

    Developmental stagei

    Expressed in flower buds at stage 6 of development in tapetal cells and at stage 10 in the epidermal cells of growing petals and ovaries. In young siliques, expressed transiently in the inner integument of the ovules just prior to testal deposition.1 Publication

    Gene expression databases

    ArrayExpressiQ38970.
    GenevestigatoriQ38970.

    Interactioni

    Subunit structurei

    Homodimer.Curated

    Protein-protein interaction databases

    BioGridi25753. 4 interactions.
    IntActiQ38970. 1 interaction.
    STRINGi3702.AT1G36160.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliQ38970.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 543508Biotin carboxylationAdd
    BLAST
    Domaini189 – 381193ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini677 – 74367Biotinyl-bindingAdd
    BLAST
    Domaini1531 – 2110580CarboxyltransferaseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated
    Contains 1 carboxyltransferase domain.Curated

    Phylogenomic databases

    eggNOGiCOG0511.
    HOGENOMiHOG000214115.
    InParanoidiQ38970.
    KOiK11262.
    OMAiHVFSGQC.
    PhylomeDBiQ38970.

    Family and domain databases

    Gene3Di3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProiIPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view]
    PfamiPF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q38970-1 [UniParc]FASTAAdd to Basket

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    MAGSVNGNHS AVGPGINYET VSQVDEFCKA LRGKRPIHSI LIANNGMAAV     50
    KFIRSVRTWA YETFGTEKAI LLVGMATPED MRINAEHIRI ADQFVEVPGG 100
    TNNNNYANVQ LIVEMAEVTR VDAVWPGWGH ASENPELPDA LDAKGIIFLG 150
    PPASSMAALG DKIGSSLIAQ AADVPTLPWS GSHVKIPPNS NLVTIPEEIY 200
    RQACVYTTEE AIASCQVVGY PAMIKASWGG GGKGIRKVHN DDEVRALFKQ 250
    VQGEVPGSPI FIMKVASQSR HLEVQLLCDK HGNVSALHSR DCSVQRRHQK 300
    IIEEGPITVA PPETVKKLEQ AARRLAKSVN YVGAATVEYL YSMDTGEYYF 350
    LELNPRLQVE HPVTEWIAEI NLPAAQVAVG MGIPLWQIPE IRRFYGIEHG 400
    GGYDSWRKTS VVAFPFDFDK AQSIRPKGHC VAVRVTSEDP DDGFKPTSGR 450
    VQELSFKSKP NVWAYFSVKS GGGIHEFSDS QFGHVFAFGE SRALAIANMV 500
    LGLKEIQIRG EIRTNVDYTI DLLHASDYRD NKIHTGWLDS RIAMRVRAER 550
    PPWYLSVVGG ALYKASATSA AVVSDYVGYL EKGQIPPKHI SLVHSQVSLN 600
    IEGSKYTIDV VRGGSGTYRL RMNKSEVVAE IHTLRDGGLL MQLDGKSHVI 650
    YAEEEAAGTR LLIDGRTCLL QNDHDPSKLM AETPCKLMRY LISDNSNIDA 700
    DTPYAEVEVM KMCMPLLSPA SGVIHFKMSE GQAMQAGELI ANLDLDDPSA 750
    VRKAEPFHGS FPRLGLPTAI SGRVHQRCAA TLNAARMILA GYEHKVDEVV 800
    QDLLNCLDSP ELPFLQWQEC FAVLATRLPK NLRNMLESKY REFESISRNS 850
    LTTDFPAKLL KGILEAHLSS CDEKERGALE RLIEPLMSLA KSYEGGRESH 900
    ARVIVHSLFE EYLSVEELFN DNMLADVIER MRQLYKKDLL KIVDIVLSHQ 950
    GIKNKNKLVL RLMEQLVYPN PAAYRDKLIR FSTLNHTNYS ELALKASQLL 1000
    EQTKLSELRS NIARSLSELE MFTEDGENMD TPKRKSAINE RIEDLVSASL 1050
    AVEDALVGLF DHSDHTLQRR VVETYIRRLY QPYVVKDSVR MQWHRSGLLA 1100
    SWEFLEEHME RKNIGLDDPD TSEKGLVEKR SKRKWGAMVI IKSLQFLPSI 1150
    ISAALRETKH NDYETAGAPL SGNMMHIAIV GINNQMSLLQ DSGDEDQAQE 1200
    RVNKLAKILK EEEVSSSLCS AGVGVISCII QRDEGRTPMR HSFHWSLEKQ 1250
    YYVEEPLLRH LEPPLSIYLE LDKLKGYSNI QYTPSRDRQW HLYTVTDKPV 1300
    PIKRMFLRSL VRQATMNDGF ILQQGQDKQL SQTLISMAFT SKCVLRSLMD 1350
    AMEELELNAH NAAMKPDHAH MFLCILREQQ IDDLVPFPRR VEVNAEDEET 1400
    TVEMILEEAA REIHRSVGVR MHRLGVCEWE VRLWLVSSGL ACGAWRVVVA 1450
    NVTGRTCTVH IYREVETPGR NSLIYHSITK KGPLHETPIS DQYKPLGYLD 1500
    RQRLAARRSN TTYCYDFPLA FGTALELLWA SQHPGVKKPY KDTLINVKEL 1550
    VFSKPEGSSG TSLDLVERPP GLNDFGMVAW CLDMSTPEFP MGRKLLVIAN 1600
    DVTFKAGSFG PREDAFFLAV TELACAKKLP LIYLAANSGA RLGVAEEVKA 1650
    CFKVGWSDEI SPENGFQYIY LSPEDHERIG SSVIAHEVKL SSGETRWVID 1700
    TIVGKEDGIG VENLTGSGAI AGAYSKAYNE TFTLTFVSGR TVGIGAYLAR 1750
    LGMRCIQRLD QPIILTGFST LNKLLGREVY SSHMQLGGPK IMGTNGVVHL 1800
    TVSDDLEGVS AILNWLSYIP AYVGGPLPVL APLDPPERIV EYVPENSCDP 1850
    RAAIAGVKDN TGKWLGGIFD KNSFIETLEG WARTVVTGRA KLGGIPVGVV 1900
    AVETQTVMQI IPADPGQLDS HERVVPQAGQ VWFPDSAAKT AQALMDFNRE 1950
    ELPLFILANW RGFSGGQRDL FEGILQAGST IVENLRTYRQ PVFVYIPMMG 2000
    ELRGGAWVVV DSQINSDYVE MYADETARGN VLEPEGTIEI KFRTKELLEC 2050
    MGRLDQKLIS LKAKLQDAKQ SEAYANIELL QQQIKAREKQ LLPVYIQIAT 2100
    KFAELHDTSM RMAAKGVIKS VVEWSGSRSF FYKKLNRRIA ESSLVKNVRE 2150
    ASGDNLAYKS SMRLIQDWFC NSDIAKGKEE AWTDDQVFFT WKDNVSNYEL 2200
    KLSELRAQKL LNQLAEIGNS SDLQALPQGL ANLLNKVEPS KREELVAAIR 2250
    KVLG 2254
    Length:2,254
    Mass (Da):251,382
    Last modified:November 1, 1996 - v1
    Checksum:iF00A5AE316CC5E87
    GO

    Sequence cautioni

    The sequence AAF18638.2 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence AAG51250.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti337 – 3371V → I in AAC41645. (PubMed:7915036)Curated
    Sequence conflicti337 – 3371V → I in AAG40563. (PubMed:7551584)Curated
    Sequence conflicti1378 – 13792EQ → DE in AAC41645. (PubMed:7915036)Curated
    Sequence conflicti1378 – 13792EQ → DE in AAG40563. (PubMed:7551584)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27074 Genomic DNA. Translation: AAC41645.1.
    D34630 mRNA. Translation: BAA07012.1.
    AF062308 Genomic DNA. Translation: AAG40563.1.
    AC006228 Genomic DNA. Translation: AAF18638.2. Sequence problems.
    AC025781 Genomic DNA. Translation: AAG51250.1. Sequence problems.
    CP002684 Genomic DNA. Translation: AEE31849.1.
    CP002684 Genomic DNA. Translation: AEE31850.1.
    AK229488 mRNA. Translation: BAF01346.1.
    PIRiD86483.
    RefSeqiNP_001185143.1. NM_001198214.1.
    NP_174849.2. NM_103313.3.
    UniGeneiAt.39402.

    Genome annotation databases

    EnsemblPlantsiAT1G36160.1; AT1G36160.1; AT1G36160.
    AT1G36160.2; AT1G36160.2; AT1G36160.
    GeneIDi840521.
    KEGGiath:AT1G36160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27074 Genomic DNA. Translation: AAC41645.1 .
    D34630 mRNA. Translation: BAA07012.1 .
    AF062308 Genomic DNA. Translation: AAG40563.1 .
    AC006228 Genomic DNA. Translation: AAF18638.2 . Sequence problems.
    AC025781 Genomic DNA. Translation: AAG51250.1 . Sequence problems.
    CP002684 Genomic DNA. Translation: AEE31849.1 .
    CP002684 Genomic DNA. Translation: AEE31850.1 .
    AK229488 mRNA. Translation: BAF01346.1 .
    PIRi D86483.
    RefSeqi NP_001185143.1. NM_001198214.1.
    NP_174849.2. NM_103313.3.
    UniGenei At.39402.

    3D structure databases

    ProteinModelPortali Q38970.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 25753. 4 interactions.
    IntActi Q38970. 1 interaction.
    STRINGi 3702.AT1G36160.1-P.

    Proteomic databases

    PRIDEi Q38970.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G36160.1 ; AT1G36160.1 ; AT1G36160 .
    AT1G36160.2 ; AT1G36160.2 ; AT1G36160 .
    GeneIDi 840521.
    KEGGi ath:AT1G36160.

    Organism-specific databases

    TAIRi AT1G36160.

    Phylogenomic databases

    eggNOGi COG0511.
    HOGENOMi HOG000214115.
    InParanoidi Q38970.
    KOi K11262.
    OMAi HVFSGQC.
    PhylomeDBi Q38970.

    Enzyme and pathway databases

    UniPathwayi UPA00655 ; UER00711 .
    BioCyci ARA:AT1G36160-MONOMER.
    ARA:GQT-1121-MONOMER.
    Reactomei REACT_185257. Defective HLCS causes multiple carboxylase deficiency.
    REACT_187915. Biotin transport and metabolism.

    Miscellaneous databases

    PROi Q38970.

    Gene expression databases

    ArrayExpressi Q38970.
    Genevestigatori Q38970.

    Family and domain databases

    Gene3Di 3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.226.10. 3 hits.
    InterProi IPR013537. AcCoA_COase_cen.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR000022. Carboxyl_trans.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029045. ClpP/crotonase-like_dom.
    IPR011763. COA_CT_C.
    IPR011762. COA_CT_N.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    [Graphical view ]
    Pfami PF08326. ACC_central. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF01039. Carboxyl_trans. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52096. SSF52096. 2 hits.
    SSF52440. SSF52440. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS50989. COA_CT_CTER. 1 hit.
    PS50980. COA_CT_NTER. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of an Arabidopsis acetyl-coenzyme A carboxylase gene."
      Roesler K.R., Shorrosh B.S., Ohlrogge J.B.
      Plant Physiol. 105:611-617(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    2. "Genomic organization of 251 kDa acetyl-CoA carboxylase genes in Arabidopsis: tandem gene duplication has made two differentially expressed isozymes."
      Yanai Y., Kawasaki T., Shimada H., Wurtele E.S., Nikolau B.J., Ichikawa N.
      Plant Cell Physiol. 36:779-787(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1246-2254.
      Strain: cv. Columbia.
    6. "The GURKE gene is required for normal organization of the apical region in the Arabidopsis embryo."
      Torres-Ruiz R.A., Lohner A., Juergens G.
      Plant J. 10:1005-1016(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
    7. "Targeting of the Arabidopsis homomeric acetyl-coenzyme A carboxylase to plastids of rapeseeds."
      Roesler K., Shintani D., Savage L., Boddupalli S., Ohlrogge J.
      Plant Physiol. 113:75-81(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "The PASTICCINO genes of Arabidopsis thaliana are involved in the control of cell division and differentiation."
      Faure J.-D., Vittorioso P., Santoni V., Fraisier V., Prinsen E., Barlier I., Van Onckelen H., Caboche M., Bellini C.
      Development 125:909-918(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    9. "Molecular characterization of a heteromeric ATP-citrate lyase that generates cytosolic acetyl-coenzyme A in Arabidopsis."
      Fatland B.L., Ke J., Anderson M.D., Mentzen W.I., Cui L.W., Allred C.C., Johnston J.L., Nikolau B.J., Wurtele E.S.
      Plant Physiol. 130:740-756(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    10. "Multifunctional acetyl-CoA carboxylase 1 is essential for very long chain fatty acid elongation and embryo development in Arabidopsis."
      Baud S., Guyon V., Kronenberger J., Wuilleme S., Miquel M., Caboche M., Lepiniec L., Rochat C.
      Plant J. 33:75-86(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
      Strain: cv. Wassilewskija.
    11. "gurke and pasticcino3 mutants affected in embryo development are impaired in acetyl-CoA carboxylase."
      Baud S., Bellec Y., Miquel M., Bellini C., Caboche M., Lepiniec L., Faure J.D., Rochat C.
      EMBO Rep. 5:515-520(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-1588 AND GLY-1787.
      Strain: cv. Wassilewskija.
    12. "The GURKE gene encoding an acetyl-CoA carboxylase is required for partitioning the embryo apex into three subregions in Arabidopsis."
      Kajiwara T., Furutani M., Hibara K., Tasaka M.
      Plant Cell Physiol. 45:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    13. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1031 AND SER-1192, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: FUNCTION.
    15. "The flavonoid biosynthetic pathway in Arabidopsis: Structural and genetic diversity."
      Saito K., Yonekura-Sakakibara K., Nakabayashi R., Higashi Y., Yamazaki M., Tohge T., Fernie A.R.
      Plant Physiol. Biochem. 0:0-0(2013)
      Cited for: REVIEW, NOMENCLATURE.

    Entry informationi

    Entry nameiACC1_ARATH
    AccessioniPrimary (citable) accession number: Q38970
    Secondary accession number(s): Q0WNF3
    , Q38971, Q9C8G1, Q9SKV1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 21, 2011
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The acc1-1 and pas3-1 mutants can be partially complemented by exogenous supply of malonate.

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3