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Q38970

- ACC1_ARATH

UniProt

Q38970 - ACC1_ARATH

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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

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
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 Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  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 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

ExpressionAtlasiQ38970. baseline and differential.
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

« Hide

        10         20         30         40         50
MAGSVNGNHS AVGPGINYET VSQVDEFCKA LRGKRPIHSI LIANNGMAAV
60 70 80 90 100
KFIRSVRTWA YETFGTEKAI LLVGMATPED MRINAEHIRI ADQFVEVPGG
110 120 130 140 150
TNNNNYANVQ LIVEMAEVTR VDAVWPGWGH ASENPELPDA LDAKGIIFLG
160 170 180 190 200
PPASSMAALG DKIGSSLIAQ AADVPTLPWS GSHVKIPPNS NLVTIPEEIY
210 220 230 240 250
RQACVYTTEE AIASCQVVGY PAMIKASWGG GGKGIRKVHN DDEVRALFKQ
260 270 280 290 300
VQGEVPGSPI FIMKVASQSR HLEVQLLCDK HGNVSALHSR DCSVQRRHQK
310 320 330 340 350
IIEEGPITVA PPETVKKLEQ AARRLAKSVN YVGAATVEYL YSMDTGEYYF
360 370 380 390 400
LELNPRLQVE HPVTEWIAEI NLPAAQVAVG MGIPLWQIPE IRRFYGIEHG
410 420 430 440 450
GGYDSWRKTS VVAFPFDFDK AQSIRPKGHC VAVRVTSEDP DDGFKPTSGR
460 470 480 490 500
VQELSFKSKP NVWAYFSVKS GGGIHEFSDS QFGHVFAFGE SRALAIANMV
510 520 530 540 550
LGLKEIQIRG EIRTNVDYTI DLLHASDYRD NKIHTGWLDS RIAMRVRAER
560 570 580 590 600
PPWYLSVVGG ALYKASATSA AVVSDYVGYL EKGQIPPKHI SLVHSQVSLN
610 620 630 640 650
IEGSKYTIDV VRGGSGTYRL RMNKSEVVAE IHTLRDGGLL MQLDGKSHVI
660 670 680 690 700
YAEEEAAGTR LLIDGRTCLL QNDHDPSKLM AETPCKLMRY LISDNSNIDA
710 720 730 740 750
DTPYAEVEVM KMCMPLLSPA SGVIHFKMSE GQAMQAGELI ANLDLDDPSA
760 770 780 790 800
VRKAEPFHGS FPRLGLPTAI SGRVHQRCAA TLNAARMILA GYEHKVDEVV
810 820 830 840 850
QDLLNCLDSP ELPFLQWQEC FAVLATRLPK NLRNMLESKY REFESISRNS
860 870 880 890 900
LTTDFPAKLL KGILEAHLSS CDEKERGALE RLIEPLMSLA KSYEGGRESH
910 920 930 940 950
ARVIVHSLFE EYLSVEELFN DNMLADVIER MRQLYKKDLL KIVDIVLSHQ
960 970 980 990 1000
GIKNKNKLVL RLMEQLVYPN PAAYRDKLIR FSTLNHTNYS ELALKASQLL
1010 1020 1030 1040 1050
EQTKLSELRS NIARSLSELE MFTEDGENMD TPKRKSAINE RIEDLVSASL
1060 1070 1080 1090 1100
AVEDALVGLF DHSDHTLQRR VVETYIRRLY QPYVVKDSVR MQWHRSGLLA
1110 1120 1130 1140 1150
SWEFLEEHME RKNIGLDDPD TSEKGLVEKR SKRKWGAMVI IKSLQFLPSI
1160 1170 1180 1190 1200
ISAALRETKH NDYETAGAPL SGNMMHIAIV GINNQMSLLQ DSGDEDQAQE
1210 1220 1230 1240 1250
RVNKLAKILK EEEVSSSLCS AGVGVISCII QRDEGRTPMR HSFHWSLEKQ
1260 1270 1280 1290 1300
YYVEEPLLRH LEPPLSIYLE LDKLKGYSNI QYTPSRDRQW HLYTVTDKPV
1310 1320 1330 1340 1350
PIKRMFLRSL VRQATMNDGF ILQQGQDKQL SQTLISMAFT SKCVLRSLMD
1360 1370 1380 1390 1400
AMEELELNAH NAAMKPDHAH MFLCILREQQ IDDLVPFPRR VEVNAEDEET
1410 1420 1430 1440 1450
TVEMILEEAA REIHRSVGVR MHRLGVCEWE VRLWLVSSGL ACGAWRVVVA
1460 1470 1480 1490 1500
NVTGRTCTVH IYREVETPGR NSLIYHSITK KGPLHETPIS DQYKPLGYLD
1510 1520 1530 1540 1550
RQRLAARRSN TTYCYDFPLA FGTALELLWA SQHPGVKKPY KDTLINVKEL
1560 1570 1580 1590 1600
VFSKPEGSSG TSLDLVERPP GLNDFGMVAW CLDMSTPEFP MGRKLLVIAN
1610 1620 1630 1640 1650
DVTFKAGSFG PREDAFFLAV TELACAKKLP LIYLAANSGA RLGVAEEVKA
1660 1670 1680 1690 1700
CFKVGWSDEI SPENGFQYIY LSPEDHERIG SSVIAHEVKL SSGETRWVID
1710 1720 1730 1740 1750
TIVGKEDGIG VENLTGSGAI AGAYSKAYNE TFTLTFVSGR TVGIGAYLAR
1760 1770 1780 1790 1800
LGMRCIQRLD QPIILTGFST LNKLLGREVY SSHMQLGGPK IMGTNGVVHL
1810 1820 1830 1840 1850
TVSDDLEGVS AILNWLSYIP AYVGGPLPVL APLDPPERIV EYVPENSCDP
1860 1870 1880 1890 1900
RAAIAGVKDN TGKWLGGIFD KNSFIETLEG WARTVVTGRA KLGGIPVGVV
1910 1920 1930 1940 1950
AVETQTVMQI IPADPGQLDS HERVVPQAGQ VWFPDSAAKT AQALMDFNRE
1960 1970 1980 1990 2000
ELPLFILANW RGFSGGQRDL FEGILQAGST IVENLRTYRQ PVFVYIPMMG
2010 2020 2030 2040 2050
ELRGGAWVVV DSQINSDYVE MYADETARGN VLEPEGTIEI KFRTKELLEC
2060 2070 2080 2090 2100
MGRLDQKLIS LKAKLQDAKQ SEAYANIELL QQQIKAREKQ LLPVYIQIAT
2110 2120 2130 2140 2150
KFAELHDTSM RMAAKGVIKS VVEWSGSRSF FYKKLNRRIA ESSLVKNVRE
2160 2170 2180 2190 2200
ASGDNLAYKS SMRLIQDWFC NSDIAKGKEE AWTDDQVFFT WKDNVSNYEL
2210 2220 2230 2240 2250
KLSELRAQKL LNQLAEIGNS SDLQALPQGL ANLLNKVEPS KREELVAAIR

KVLG
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

ExpressionAtlasi Q38970. baseline and differential.
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: October 29, 2014
This is version 119 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