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F4I1L3 (ACC2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 24. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetyl-CoA carboxylase 2

EC=6.4.1.2

Including the following 1 domains:

  1. Biotin carboxylase
    EC=6.3.4.14
Gene names
Name:ACC2
Ordered Locus Names:At1g36180
ORF Names:F15C21.2
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length2355 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.

ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].

Cofactor

Biotin By similarity.

Binds 2 magnesium or manganese ions per subunit By similarity.

Pathway

Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1.

Subunit structure

Homodimer Probable.

Subcellular location

Cytoplasmcytosol Probable.

Tissue specificity

Widely expressed at low levels. Ref.1 Ref.4

Sequence similarities

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Contains 1 carboxyltransferase domain.

Sequence caution

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.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: F4I1L3-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 23552355Acetyl-CoA carboxylase 2
PRO_0000412212

Regions

Domain138 – 645508Biotin carboxylation
Domain291 – 485195ATP-grasp
Domain779 – 84567Biotinyl-binding
Domain1619 – 2211593Carboxyltransferase
Nucleotide binding317 – 37458ATP Potential

Sites

Active site4581 By similarity
Metal binding4401Magnesium or manganese 1 By similarity
Metal binding4541Magnesium or manganese 1 By similarity
Metal binding4541Magnesium or manganese 2 By similarity
Metal binding4561Magnesium or manganese 2 By similarity
Binding site18411Coenzyme A By similarity
Binding site21421Coenzyme A By similarity
Binding site21441Coenzyme A By similarity

Amino acid modifications

Modified residue11331Phosphothreonine By similarity
Modified residue12931Phosphoserine By similarity

Experimental info

Sequence conflict18551R → K in AAG40564. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: D3E322E33E847E0A

FASTA2,355262,729
        10         20         30         40         50         60 
MEMRALGSSC STGNGGSAPI TLTNISPWIT TVFPSTVKLR SSLRTFKGVS SRVRTFKGVS 

        70         80         90        100        110        120 
STRVLSRTKQ QFPLFCFLNP DPISFLENDV SEAERTVVLP DGSVNGAGSV NGYHSDVVPG 

       130        140        150        160        170        180 
RNVAEVNEFC KALGGKRPIH SILVATNGMA AVKFIRSVRT WAYETFGSEK AVKLVAMATP 

       190        200        210        220        230        240 
EDMRINAEHI RIADQFVEVP GGTNNNNYAN VQLIVEMAEV TRVDAVWPGW GHASENPELP 

       250        260        270        280        290        300 
DALKEKGIIF LGPPADSMIA LGDKIGSSLI AQAADVPTLP WSGSHVKIPP GRSLVTVPEE 

       310        320        330        340        350        360 
IYKKACVYTT EEAIASCQVV GYPAMIKASW GGGGKGIRKV HNDDEVRALF KQVQGEVPGS 

       370        380        390        400        410        420 
PIFIMKVASQ SRHLEAQLLC DQYGNVAALH SRDCSVQRRH QKIIEEGPIT VAPQETIKKL 

       430        440        450        460        470        480 
EQAARRLAKS VNYVGAATVE YLYSMDTGEY YFLELNPRLQ VEHPVTEWIA EVNLPAAQVA 

       490        500        510        520        530        540 
VGMGIPLWQI PEIRRFYGME HGGGYDSWRK TSVVASPFDF DEAESLRPKG HCVAVRVTSE 

       550        560        570        580        590        600 
DPDDGFKPTS GEIQELSFKS KPNMWSYFSV KSGGGIHEFS DSQFGHVFAF GESRSVAIAN 

       610        620        630        640        650        660 
MVLALKEIQI RGDIRTNVDY TIDLLHASDY RENKIHTGWL DSRIAMRVRA ERPPWYLSVV 

       670        680        690        700        710        720 
GGALYKASTT SSAVVSDYVG YLEKGQIPPK HISLVHSQVS LNIEGSKYTI DVVRGGSGTY 

       730        740        750        760        770        780 
RLRMSNSEVV AEIHTLRDGG LLMQLDGKSH VIYAKEEATG TRLLIDGRTC LLQNDHDPSK 

       790        800        810        820        830        840 
LMAETPCKLL RYLVSDNSSI DTDTPYAEVE VMKMCMPLIS PASGVIHFKL SEGQAMQAGE 

       850        860        870        880        890        900 
LIAKLDLDDP SAVRKAKPFR GSFPRLGLPT AISGKVHQRC AATLNAARMI LAGYDHKVDE 

       910        920        930        940        950        960 
VLQDLLNCLD SPELPFLQWQ ECFAVLATRL PKDLRNMLEL KYKEFEIISK TSLTPDFPAK 

       970        980        990       1000       1010       1020 
LLKGILEAHL SSCDEKERGS LERLIEPLMS LVKSYEGGRE SHARLIVHSL FEEYLSVEEL 

      1030       1040       1050       1060       1070       1080 
FNDNMLADVI ERMRQQYKKD RLKIVDIVLS HQGIIHKNKL VLRLMEQLVY PNPAAYREKL 

      1090       1100       1110       1120       1130       1140 
IRFSALNHTN YSQLALKASQ LLEQTKRSEL RSNIARSLSE LEMFTEAGEN MDTPKRKSAI 

      1150       1160       1170       1180       1190       1200 
SETMENLVSS SLAVEDALVG LFDHSDHTLQ RRVVETYIHR LYQPYVVKES VRMQWHQSGV 

      1210       1220       1230       1240       1250       1260 
IASWEFLEHF ERKNTGPDDH EISEKGIVAK SSKRKRGTMV IIKSLQFLPS IINASLRETN 

      1270       1280       1290       1300       1310       1320 
HSHCEYARAP LSGNMMHIAV VGINNQMSLL QDSGDEDQTQ ERVNKLAKIL KEEEVSLTLC 

      1330       1340       1350       1360       1370       1380 
SAGVGVISCI IQRDEGRTPM RHSFHWLMEK QYYVEEPLLR HVEPPLSVYL ELDKLKGYSN 

      1390       1400       1410       1420       1430       1440 
IQYSPSRDRQ WHMYSVTDRP VPIKRMFLRS LVRQTTMNDG FLLQQGQDYQ LSQTVLSMAF 

      1450       1460       1470       1480       1490       1500 
TSKCILRSLM NAMEELELNA HNAAMKPDHA HMFLCILREQ QIDDLVPYPR RFEVNAEDEE 

      1510       1520       1530       1540       1550       1560 
TTVETILEEA TQEIHRSVGV RMHALGVCEW EVRLWLVSSG LANGAWRVVV ANVTGRTCTV 

      1570       1580       1590       1600       1610       1620 
HIYREVEATG RNSLIYHSIT KKGPLHGTLI NGQYKPLNNL DRKRLAARRS NTTYCYDFPL 

      1630       1640       1650       1660       1670       1680 
AFETALELNW ASQHSGVRKP CKNRLINVKE LVFSNTEGSL GTSLIPVERP AGLNDIGMVA 

      1690       1700       1710       1720       1730       1740 
WILEMSTPEF PMGRKLLIVA NDVTFKAGSF GPREDAFFLA VTELACTKKL PLIYLAANSG 

      1750       1760       1770       1780       1790       1800 
ARLGVAEEVK ACFKVGWSDE VSPGNDFQYI YLSSEDYARI GSSVIAHEVK LPSGETRWVI 

      1810       1820       1830       1840       1850       1860 
DTIVGKEDGL GVENLTGSGA IAGAYSRAYN ETFTLTFVSG RSVGIGAYLA RLGMRCIQRL 

      1870       1880       1890       1900       1910       1920 
DQPIILTGFS TLNKLLGREV YSSHMQLGGP KIMGTNGVVH LTVSDDLEGV SAILNWLSYI 

      1930       1940       1950       1960       1970       1980 
PAYVGGPLPV LAPLDPPERT VEYIPENSCD PRAAIAGIND NTGKWLGGIF DKNSFVETLE 

      1990       2000       2010       2020       2030       2040 
GWARTVVTGR AKLGGIPIGV VAVETQTVMH VIPADPGQLD SHERVVPQAG QVWFPDSAAK 

      2050       2060       2070       2080       2090       2100 
TAQALMDFNR EQLPLFIIAN WRGFSGGQRD LFEGILQAGS AIVENLRTYR QPVFVYIPMM 

      2110       2120       2130       2140       2150       2160 
GELRGGAWVV VDSQINSDYI EMYADETARG NVLEPEGMIE IKFRRKELLE CMGRLDQTLI 

      2170       2180       2190       2200       2210       2220 
NLKANIQDAK RNKAYANIEL LQKQIKTREK QLLPVYTQIA TKFAELHDTS MRMAAKGVIK 

      2230       2240       2250       2260       2270       2280 
SVVEWSGSRS FFYKKLYRRI AESSLVRNIR KASGDILSYK SAMGLIQDWF RKSEIAKGKE 

      2290       2300       2310       2320       2330       2340 
EAWTDDQLFF TWKDNVSNYE QKLSELRTQK LLNQLAEIGN SSDLQALPQG LANLLNKVDL 

      2350 
SRREELVDAI RKVLG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF062308 Genomic DNA. Translation: AAG40564.1. Sequence problems.
AC025781 Genomic DNA. Translation: AAG51252.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31851.1.
PIRE86483.
RefSeqNP_174850.4. NM_103314.4. [F4I1L3-1]
UniGeneAt.51973.

3D structure databases

ProteinModelPortalF4I1L3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid25754. 1 interaction.

Proteomic databases

PRIDEF4I1L3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G36180.1; AT1G36180.1; AT1G36180. [F4I1L3-1]
GeneID840522.
KEGGath:AT1G36180.

Organism-specific databases

TAIRAT1G36180.

Phylogenomic databases

HOGENOMHOG000214115.
InParanoidQ9FR96.
OMAHICAGET.

Enzyme and pathway databases

UniPathwayUPA00655; UER00711.

Gene expression databases

ArrayExpressF4I1L3.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
3.90.226.10. 3 hits.
InterProIPR013537. 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]
PfamPF08326. 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]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52096. SSF52096. 2 hits.
SSF52440. SSF52440. 1 hit.
PROSITEPS50975. 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]
ProtoNetSearch...

Entry information

Entry nameACC2_ARATH
AccessionPrimary (citable) accession number: F4I1L3
Secondary accession number(s): Q9C8G0, Q9FR96
Entry history
Integrated into UniProtKB/Swiss-Prot: September 21, 2011
Last sequence update: June 28, 2011
Last modified: June 11, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names