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F4I1L3

- ACC2_ARATH

UniProt

F4I1L3 - ACC2_ARATH

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Protein

Acetyl-CoA carboxylase 2

Gene
ACC2, At1g36180, F15C21.2
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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 By similarity.

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 bindingi440 – 4401Magnesium or manganese 1 By similarity
Metal bindingi454 – 4541Magnesium or manganese 1 By similarity
Metal bindingi454 – 4541Magnesium or manganese 2 By similarity
Metal bindingi456 – 4561Magnesium or manganese 2 By similarity
Active sitei458 – 4581 By similarity
Binding sitei1841 – 18411Coenzyme A By similarity
Binding sitei2142 – 21421Coenzyme A By similarity
Binding sitei2144 – 21441Coenzyme A By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi317 – 37458ATP Reviewed predictionAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. fatty acid biosynthetic process Source: UniProtKB-KW
  2. malonyl-CoA biosynthetic process Source: UniProtKB-UniPathway
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

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 2 (EC:6.4.1.2)
Including the following 1 domains:
Biotin carboxylase (EC:6.3.4.14)
Gene namesi
Name:ACC2
Ordered Locus Names:At1g36180
ORF Names:F15C21.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G36180.

Subcellular locationi

Cytoplasmcytosol Inferred

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23552355Acetyl-CoA carboxylase 2PRO_0000412212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1133 – 11331Phosphothreonine By similarity
Modified residuei1293 – 12931Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiF4I1L3.

Expressioni

Tissue specificityi

Widely expressed at low levels.2 Publications

Gene expression databases

ArrayExpressiF4I1L3.

Interactioni

Subunit structurei

Homodimer Inferred.

Protein-protein interaction databases

BioGridi25754. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliF4I1L3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 645508Biotin carboxylationAdd
BLAST
Domaini291 – 485195ATP-graspAdd
BLAST
Domaini779 – 84567Biotinyl-bindingAdd
BLAST
Domaini1619 – 2211593CarboxyltransferaseAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.

Phylogenomic databases

HOGENOMiHOG000214115.
InParanoidiQ9FR96.
OMAiHICAGET.

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.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: F4I1L3-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MEMRALGSSC STGNGGSAPI TLTNISPWIT TVFPSTVKLR SSLRTFKGVS     50
SRVRTFKGVS STRVLSRTKQ QFPLFCFLNP DPISFLENDV SEAERTVVLP 100
DGSVNGAGSV NGYHSDVVPG RNVAEVNEFC KALGGKRPIH SILVATNGMA 150
AVKFIRSVRT WAYETFGSEK AVKLVAMATP EDMRINAEHI RIADQFVEVP 200
GGTNNNNYAN VQLIVEMAEV TRVDAVWPGW GHASENPELP DALKEKGIIF 250
LGPPADSMIA LGDKIGSSLI AQAADVPTLP WSGSHVKIPP GRSLVTVPEE 300
IYKKACVYTT EEAIASCQVV GYPAMIKASW GGGGKGIRKV HNDDEVRALF 350
KQVQGEVPGS PIFIMKVASQ SRHLEAQLLC DQYGNVAALH SRDCSVQRRH 400
QKIIEEGPIT VAPQETIKKL EQAARRLAKS VNYVGAATVE YLYSMDTGEY 450
YFLELNPRLQ VEHPVTEWIA EVNLPAAQVA VGMGIPLWQI PEIRRFYGME 500
HGGGYDSWRK TSVVASPFDF DEAESLRPKG HCVAVRVTSE DPDDGFKPTS 550
GEIQELSFKS KPNMWSYFSV KSGGGIHEFS DSQFGHVFAF GESRSVAIAN 600
MVLALKEIQI RGDIRTNVDY TIDLLHASDY RENKIHTGWL DSRIAMRVRA 650
ERPPWYLSVV GGALYKASTT SSAVVSDYVG YLEKGQIPPK HISLVHSQVS 700
LNIEGSKYTI DVVRGGSGTY RLRMSNSEVV AEIHTLRDGG LLMQLDGKSH 750
VIYAKEEATG TRLLIDGRTC LLQNDHDPSK LMAETPCKLL RYLVSDNSSI 800
DTDTPYAEVE VMKMCMPLIS PASGVIHFKL SEGQAMQAGE LIAKLDLDDP 850
SAVRKAKPFR GSFPRLGLPT AISGKVHQRC AATLNAARMI LAGYDHKVDE 900
VLQDLLNCLD SPELPFLQWQ ECFAVLATRL PKDLRNMLEL KYKEFEIISK 950
TSLTPDFPAK LLKGILEAHL SSCDEKERGS LERLIEPLMS LVKSYEGGRE 1000
SHARLIVHSL FEEYLSVEEL FNDNMLADVI ERMRQQYKKD RLKIVDIVLS 1050
HQGIIHKNKL VLRLMEQLVY PNPAAYREKL IRFSALNHTN YSQLALKASQ 1100
LLEQTKRSEL RSNIARSLSE LEMFTEAGEN MDTPKRKSAI SETMENLVSS 1150
SLAVEDALVG LFDHSDHTLQ RRVVETYIHR LYQPYVVKES VRMQWHQSGV 1200
IASWEFLEHF ERKNTGPDDH EISEKGIVAK SSKRKRGTMV IIKSLQFLPS 1250
IINASLRETN HSHCEYARAP LSGNMMHIAV VGINNQMSLL QDSGDEDQTQ 1300
ERVNKLAKIL KEEEVSLTLC SAGVGVISCI IQRDEGRTPM RHSFHWLMEK 1350
QYYVEEPLLR HVEPPLSVYL ELDKLKGYSN IQYSPSRDRQ WHMYSVTDRP 1400
VPIKRMFLRS LVRQTTMNDG FLLQQGQDYQ LSQTVLSMAF TSKCILRSLM 1450
NAMEELELNA HNAAMKPDHA HMFLCILREQ QIDDLVPYPR RFEVNAEDEE 1500
TTVETILEEA TQEIHRSVGV RMHALGVCEW EVRLWLVSSG LANGAWRVVV 1550
ANVTGRTCTV HIYREVEATG RNSLIYHSIT KKGPLHGTLI NGQYKPLNNL 1600
DRKRLAARRS NTTYCYDFPL AFETALELNW ASQHSGVRKP CKNRLINVKE 1650
LVFSNTEGSL GTSLIPVERP AGLNDIGMVA WILEMSTPEF PMGRKLLIVA 1700
NDVTFKAGSF GPREDAFFLA VTELACTKKL PLIYLAANSG ARLGVAEEVK 1750
ACFKVGWSDE VSPGNDFQYI YLSSEDYARI GSSVIAHEVK LPSGETRWVI 1800
DTIVGKEDGL GVENLTGSGA IAGAYSRAYN ETFTLTFVSG RSVGIGAYLA 1850
RLGMRCIQRL DQPIILTGFS TLNKLLGREV YSSHMQLGGP KIMGTNGVVH 1900
LTVSDDLEGV SAILNWLSYI PAYVGGPLPV LAPLDPPERT VEYIPENSCD 1950
PRAAIAGIND NTGKWLGGIF DKNSFVETLE GWARTVVTGR AKLGGIPIGV 2000
VAVETQTVMH VIPADPGQLD SHERVVPQAG QVWFPDSAAK TAQALMDFNR 2050
EQLPLFIIAN WRGFSGGQRD LFEGILQAGS AIVENLRTYR QPVFVYIPMM 2100
GELRGGAWVV VDSQINSDYI EMYADETARG NVLEPEGMIE IKFRRKELLE 2150
CMGRLDQTLI NLKANIQDAK RNKAYANIEL LQKQIKTREK QLLPVYTQIA 2200
TKFAELHDTS MRMAAKGVIK SVVEWSGSRS FFYKKLYRRI AESSLVRNIR 2250
KASGDILSYK SAMGLIQDWF RKSEIAKGKE EAWTDDQLFF TWKDNVSNYE 2300
QKLSELRTQK LLNQLAEIGN SSDLQALPQG LANLLNKVDL SRREELVDAI 2350
RKVLG 2355
Length:2,355
Mass (Da):262,729
Last modified:June 28, 2011 - v1
Checksum:iD3E322E33E847E0A
GO

Sequence cautioni

The sequence AAG40564.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence AAG51252.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1855 – 18551R → K in AAG40564. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF062308 Genomic DNA. Translation: AAG40564.1. Sequence problems.
AC025781 Genomic DNA. Translation: AAG51252.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31851.1.
PIRiE86483.
RefSeqiNP_174850.4. NM_103314.4. [F4I1L3-1]
UniGeneiAt.51973.

Genome annotation databases

EnsemblPlantsiAT1G36180.1; AT1G36180.1; AT1G36180. [F4I1L3-1]
GeneIDi840522.
KEGGiath:AT1G36180.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF062308 Genomic DNA. Translation: AAG40564.1 . Sequence problems.
AC025781 Genomic DNA. Translation: AAG51252.1 . Sequence problems.
CP002684 Genomic DNA. Translation: AEE31851.1 .
PIRi E86483.
RefSeqi NP_174850.4. NM_103314.4. [F4I1L3-1 ]
UniGenei At.51973.

3D structure databases

ProteinModelPortali F4I1L3.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 25754. 1 interaction.

Proteomic databases

PRIDEi F4I1L3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G36180.1 ; AT1G36180.1 ; AT1G36180 . [F4I1L3-1 ]
GeneIDi 840522.
KEGGi ath:AT1G36180.

Organism-specific databases

TAIRi AT1G36180.

Phylogenomic databases

HOGENOMi HOG000214115.
InParanoidi Q9FR96.
OMAi HICAGET.

Enzyme and pathway databases

UniPathwayi UPA00655 ; UER00711 .
Reactomei REACT_185257. Defective HLCS causes multiple carboxylase deficiency.
REACT_187915. Biotin transport and metabolism.

Gene expression databases

ArrayExpressi F4I1L3.

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. "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], TISSUE SPECIFICITY.
    Strain: cv. Columbia.
  2. "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.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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: TISSUE SPECIFICITY.
    Strain: cv. Wassilewskija.

Entry informationi

Entry nameiACC2_ARATH
AccessioniPrimary (citable) accession number: F4I1L3
Secondary accession number(s): Q9C8G0, Q9FR96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: June 28, 2011
Last modified: September 3, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

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