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F4I1L3

- ACC2_ARATH

UniProt

F4I1L3 - ACC2_ARATH

Protein

Acetyl-CoA carboxylase 2

Gene

ACC2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 26 (01 Oct 2014)
      Sequence version 1 (28 Jun 2011)
      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.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 1PROSITE-ProRule annotation
    Metal bindingi454 – 4541Magnesium or manganese 1PROSITE-ProRule annotation
    Metal bindingi454 – 4541Magnesium or manganese 2PROSITE-ProRule annotation
    Metal bindingi456 – 4561Magnesium or manganese 2PROSITE-ProRule annotation
    Active sitei458 – 4581By similarity
    Binding sitei1841 – 18411Coenzyme ABy similarity
    Binding sitei2142 – 21421Coenzyme ABy similarity
    Binding sitei2144 – 21441Coenzyme ABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi317 – 37458ATPPROSITE-ProRule annotationAdd
    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

    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 Curated

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell

    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 – 11331PhosphothreonineBy similarity
    Modified residuei1293 – 12931PhosphoserineBy 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.Curated

    Protein-protein interaction databases

    BioGridi25754. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliF4I1L3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1855 – 18551R → K in AAG40564. (PubMed:7551584)Curated

    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

    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: October 1, 2014
    This is version 26 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