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B9N843 (ACCC2_POPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Biotin carboxylase 2, chloroplastic

EC=6.3.4.14
Alternative name(s):
Acetyl-CoA carboxylase subunit A 2
Short name=ACC
EC=6.4.1.2
Gene names
ORF Names:POPTR_0018s14250g
OrganismPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) [Reference proteome]
Taxonomic identifier3694 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA By similarity.

Catalytic activity

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

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

Cofactor

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

Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein, biotin carboxylase and two subunits each of ACCase subunit alpha and ACCase plastid-coded subunit beta (accD) Probable.

Subcellular location

Plastidchloroplast Potential.

Sequence similarities

Contains 1 ATP-grasp domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7171Chloroplast Potential
Chain72 – 526455Biotin carboxylase 2, chloroplastic
PRO_0000391774

Regions

Domain185 – 382198ATP-grasp
Nucleotide binding213 – 27462ATP By similarity

Sites

Active site3571 By similarity
Metal binding3401Magnesium or manganese 1 By similarity
Metal binding3531Magnesium or manganese 1 By similarity
Metal binding3531Magnesium or manganese 2 By similarity
Metal binding3551Magnesium or manganese 2 By similarity
Binding site1811ATP By similarity
Binding site2651ATP By similarity
Binding site3001ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B9N843 [UniParc].

Last modified February 19, 2014. Version 2.
Checksum: CAC6A56109E42892

FASTA52657,497
        10         20         30         40         50         60 
MEATLPVCKS VTSTPGLFMK RNSGIRNSQC SFMVGTKVNF PRQRTQATQA NHCAKKNGGA 

        70         80         90        100        110        120 
LGVTCRAEKI LVANRGEIAV RVIRTAHELG IPCVAVYSTI DKDALHVKLA DESVCIGEAP 

       130        140        150        160        170        180 
SNQSYLVIQN VLSAAISRGC TMLHPGYGFL AENAVFVEMC REHGINFIGP NPDSIRVMGD 

       190        200        210        220        230        240 
KSTARETMKK ANVPTVPGSD GLLQSTEEAV KLASEIGYPV MIKATAGGGG RGMRLAKEPD 

       250        260        270        280        290        300 
EFVKLLQQAK SEAAAAFGND GVYLEKYVQN PRHIEFQVLA DKFGNVVHFG ERDCSIQRRN 

       310        320        330        340        350        360 
QKLLEEAPSP ALTPELRKAM GDAAVAAAAS IGYIGVGTVE FLLDERGSFY FMEMNTRIQV 

       370        380        390        400        410        420 
EHPVTEMISS VDLIEEQIRV AMGEKIQYKQ EDIVLRGHSI ECRINAEDAF KGFRPGPGRI 

       430        440        450        460        470        480 
TAYLPSGGPF VRMDSHVYPD YVVPPSYDSL LGKLIVWAPT REKAIERMKR ALDDTIITGV 

       490        500        510        520 
PTTIDYHKLI LDIEDFKNGN VDTAFIPKHE QELAAPQQII LANSAS 

« Hide

References

« Hide 'large scale' references
[1]"The genome of black cottonwood, Populus trichocarpa (Torr. & Gray)."
Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I., Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J., Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D., Boerjan W., Brun A. expand/collapse author list , Brunner A., Busov V., Campbell M., Carlson J., Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M., Couturier J., Covert S., Cronk Q., Cunningham R., Davis J., Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B., Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K., Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L., Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D., Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M., Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C., Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F., Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S., Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C., Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G., Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K., Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H., Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E., Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T., Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.
Science 313:1596-1604(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Nisqually.
[2]US DOE Joint Genome Institute (JGI-PGF)
Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S., Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H., Pitluck S., Chapman J., Putnam N.H., Brunner A., Busov V., Campbell M., Chalot M. expand/collapse author list , Covert S., Davis J., DiFazio S., Gribskov M., Gunter L., Hamberger B., Jansson S., Joshi C., Larimer F., Martin F., Napoli C., Nelson D., Ralph S., Rombauts S., Rouze P., Schrader J., Tsai C., Vahala J., Tuskan G., Rokhsar D.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Nisqually.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CM000354 Genomic DNA. Translation: ERP49997.1.
RefSeqXP_006372200.1. XM_006372138.1.

3D structure databases

ProteinModelPortalB9N843.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3694.grail3.0164004802.

Proteomic databases

PRIDEB9N843.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID18107844.
KEGGpop:POPTR_673504.

Phylogenomic databases

eggNOGCOG0439.
HOGENOMHOG000008988.
KOK01961.
ProtClustDBCLSN2686481.

Enzyme and pathway databases

UniPathwayUPA00655; UER00711.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProIPR004549. Acetyl_CoA_COase_biotin_COase.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR011764. Biotin_carboxylation_dom.
IPR005482. Biotin_COase_C.
IPR005481. CarbamoylP_synth_lsu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
[Graphical view]
PfamPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsTIGR00514. accC. 1 hit.
PROSITEPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACCC2_POPTR
AccessionPrimary (citable) accession number: B9N843
Secondary accession number(s): U5FKU1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: February 19, 2014
Last modified: March 19, 2014
This is version 38 of the entry and version 2 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