SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q38970

- ACC1_ARATH

UniProt

Q38970 - ACC1_ARATH

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Acetyl-CoA carboxylase 1
Gene
ACC1, EMB22, GK, PAS3, At1g36160, F15C21.1
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 1 By similarity
Metal bindingi352 – 3521Magnesium or manganese 1 By similarity
Metal bindingi352 – 3521Magnesium or manganese 2 By similarity
Metal bindingi354 – 3541Magnesium or manganese 2 By similarity
Active sitei356 – 3561 By similarity
Binding sitei1740 – 17401Coenzyme A By similarity
Binding sitei2041 – 20411Coenzyme A By similarity
Binding sitei2043 – 20431Coenzyme A By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi215 – 27258ATP Reviewed prediction
Add
BLAST

GO - Molecular functioni

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

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
Complete GO annotation...

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 Inferred

GO - Cellular componenti

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

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 1
PRO_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 Inferred.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ38970.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 543508Biotin carboxylation
Add
BLAST
Domaini189 – 381193ATP-grasp
Add
BLAST
Domaini677 – 74367Biotinyl-binding
Add
BLAST
Domaini1531 – 2110580Carboxyltransferase
Add
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

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

« Hide

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.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti337 – 3371V → I in AAC41645. 1 Publication
Sequence conflicti337 – 3371V → I in AAG40563. 1 Publication
Sequence conflicti1378 – 13792EQ → DE in AAC41645. 1 Publication
Sequence conflicti1378 – 13792EQ → DE in AAG40563. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 117 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

Similar proteinsi