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B9HBA8 (ACCC1_POPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 40. 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 1, chloroplastic

EC=6.3.4.14
Alternative name(s):
Acetyl-CoA carboxylase subunit A 1
Short name=ACC
EC=6.4.1.2
Gene names
ORF Names:POPTRDRAFT_831870
OrganismPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa) [Reference proteome]
Taxonomic identifier3694 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus

Protein attributes

Sequence length528 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 – 5151Chloroplast Potential
Chain52 – 528477Biotin carboxylase 1, chloroplastic
PRO_0000391773

Regions

Domain183 – 380198ATP-grasp
Nucleotide binding211 – 27262ATP By similarity

Sites

Active site3551 By similarity
Metal binding3381Magnesium or manganese 1 By similarity
Metal binding3511Magnesium or manganese 1 By similarity
Metal binding3511Magnesium or manganese 2 By similarity
Metal binding3531Magnesium or manganese 2 By similarity
Binding site1791ATP By similarity
Binding site2631ATP By similarity
Binding site2981ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B9HBA8 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 741BC742900ECF41

FASTA52857,707
        10         20         30         40         50         60 
MEATLPVCKS VTSTPGLFMG KTSGIRSSQC SFMMGNKVNF PRQRAQTAHV HCAKNGGALG 

        70         80         90        100        110        120 
VTCRAEKILV ANRGEIAVRV IRTAHEMGIP CVAVYSTIDK DALHVKLADE SVCIGEAPSS 

       130        140        150        160        170        180 
QSYLVIPNVL SAAISRRCTM LHPGYGFLAE NAVFVEMCRE HGINFIGPNP DSIRVMGDKS 

       190        200        210        220        230        240 
TARETMKKAG VPTVPGSDGL LQSTEEGVRL ANEIGYPVMI KATAGGGGRG MRLAKEPDEF 

       250        260        270        280        290        300 
VKLLQQAKSE AAAAFGNDGV YLEKYVQNPR HIEFQVLADK FGNVVHFGER DCSIQRRNQK 

       310        320        330        340        350        360 
LLEEAPSPAL TPELRKAMGD AAVSAAASIG YIGVGTVEFL LDERGSFYFM EMNTRIQVEH 

       370        380        390        400        410        420 
PVTEMISSVD LIEEQIRVAM GEKLRYKQED IVLRGHSIEC RINAEDAFKG FRPGPGRITA 

       430        440        450        460        470        480 
YLPSGGPFVR MDSHVYPDYV VPPSYDSLLG KLIVWAPTRE KAIERMKRAL DDTIITGVPT 

       490        500        510        520 
TIDYHKLILE IEDFKNGNVD TAFIPKHEKE LAAPQQIIPA KQLTNSAA 

« 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
CM000342 Genomic DNA. Translation: EEE91650.1.
RefSeqXP_002308127.1. XM_002308091.2.

3D structure databases

ProteinModelPortalB9HBA8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING3694.estExt_fgenesh4_pm.C_LG_VI0248.

Proteomic databases

PRIDEB9HBA8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsPOPTR_0006s07780.1; POPTR_0006s07780.1; POPTR_0006s07780.
GeneID7485516.
KEGGpop:POPTR_831870.

Phylogenomic databases

eggNOGCOG0439.
HOGENOMHOG000008988.
KOK01961.
OMAGRITMWH.
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 nameACCC1_POPTR
AccessionPrimary (citable) accession number: B9HBA8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 40 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