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Protein

Biotin carboxylase 1, chloroplastic

Gene

POPTRDRAFT_831870

Organism
Populus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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 activityi

ATP + biotin-[carboxyl-carrier-protein] + HCO3- = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].By similarity
ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA.By similarity

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Pathway:imalonyl-CoA biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes malonyl-CoA from acetyl-CoA.
Proteins known to be involved in this subpathway in this organism are:
  1. Biotin carboxylase 2, chloroplastic (POPTR_0018s14250g), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (accD), Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic (accD), Biotin carboxylase 1, chloroplastic (POPTRDRAFT_831870)
This subpathway is part of the pathway malonyl-CoA biosynthesis, which is itself part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes malonyl-CoA from acetyl-CoA, the pathway malonyl-CoA biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei179 – 1791ATPBy similarity
Binding sitei263 – 2631ATPBy similarity
Binding sitei298 – 2981ATPBy similarity
Metal bindingi338 – 3381Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi351 – 3511Magnesium or manganese 1PROSITE-ProRule annotation
Metal bindingi351 – 3511Magnesium or manganese 2PROSITE-ProRule annotation
Metal bindingi353 – 3531Magnesium or manganese 2PROSITE-ProRule annotation
Active sitei355 – 3551By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi211 – 27262ATPPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

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

UniPathwayiUPA00655; UER00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Biotin carboxylase 1, chloroplastic (EC:6.3.4.14)
Alternative name(s):
Acetyl-CoA carboxylase subunit A 1 (EC:6.4.1.2)
Short name:
ACC
Gene namesi
ORF Names:POPTRDRAFT_831870
OrganismiPopulus trichocarpa (Western balsam poplar) (Populus balsamifera subsp. trichocarpa)
Taxonomic identifieri3694 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsMalpighialesSalicaceaeSaliceaePopulus
ProteomesiUP000006729 Componentsi: Linkage group LGVI, Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5151ChloroplastSequence AnalysisAdd
BLAST
Chaini52 – 528477Biotin carboxylase 1, chloroplasticPRO_0000391773Add
BLAST

Proteomic databases

PRIDEiB9HBA8.

Interactioni

Subunit structurei

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).Curated

Protein-protein interaction databases

STRINGi3694.POPTR_0006s07780.1.

Structurei

3D structure databases

ProteinModelPortaliB9HBA8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 380198ATP-graspPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ATP-grasp domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiB9HBA8.
KOiK01961.
OMAiIYDEMEA.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. 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]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

B9HBA8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEATLPVCKS VTSTPGLFMG KTSGIRSSQC SFMMGNKVNF PRQRAQTAHV
60 70 80 90 100
HCAKNGGALG VTCRAEKILV ANRGEIAVRV IRTAHEMGIP CVAVYSTIDK
110 120 130 140 150
DALHVKLADE SVCIGEAPSS QSYLVIPNVL SAAISRRCTM LHPGYGFLAE
160 170 180 190 200
NAVFVEMCRE HGINFIGPNP DSIRVMGDKS TARETMKKAG VPTVPGSDGL
210 220 230 240 250
LQSTEEGVRL ANEIGYPVMI KATAGGGGRG MRLAKEPDEF VKLLQQAKSE
260 270 280 290 300
AAAAFGNDGV YLEKYVQNPR HIEFQVLADK FGNVVHFGER DCSIQRRNQK
310 320 330 340 350
LLEEAPSPAL TPELRKAMGD AAVSAAASIG YIGVGTVEFL LDERGSFYFM
360 370 380 390 400
EMNTRIQVEH PVTEMISSVD LIEEQIRVAM GEKLRYKQED IVLRGHSIEC
410 420 430 440 450
RINAEDAFKG FRPGPGRITA YLPSGGPFVR MDSHVYPDYV VPPSYDSLLG
460 470 480 490 500
KLIVWAPTRE KAIERMKRAL DDTIITGVPT TIDYHKLILE IEDFKNGNVD
510 520
TAFIPKHEKE LAAPQQIIPA KQLTNSAA
Length:528
Mass (Da):57,707
Last modified:March 24, 2009 - v1
Checksum:i741BC742900ECF41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000342 Genomic DNA. Translation: EEE91650.1.
RefSeqiXP_002308127.1. XM_002308091.2.

Genome annotation databases

EnsemblPlantsiPOPTR_0006s07780.1; POPTR_0006s07780.1; POPTR_0006s07780.
GeneIDi7485516.
KEGGipop:POPTR_0006s07780g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CM000342 Genomic DNA. Translation: EEE91650.1.
RefSeqiXP_002308127.1. XM_002308091.2.

3D structure databases

ProteinModelPortaliB9HBA8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3694.POPTR_0006s07780.1.

Proteomic databases

PRIDEiB9HBA8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiPOPTR_0006s07780.1; POPTR_0006s07780.1; POPTR_0006s07780.
GeneIDi7485516.
KEGGipop:POPTR_0006s07780g.

Phylogenomic databases

eggNOGiCOG0439.
HOGENOMiHOG000008988.
InParanoidiB9HBA8.
KOiK01961.
OMAiIYDEMEA.

Enzyme and pathway databases

UniPathwayiUPA00655; UER00711.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
3.40.50.20. 1 hit.
InterProiIPR004549. 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]
PfamiPF02785. Biotin_carb_C. 1 hit.
PF00289. CPSase_L_chain. 1 hit.
PF02786. CPSase_L_D2. 1 hit.
[Graphical view]
SMARTiSM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMiSSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
TIGRFAMsiTIGR00514. accC. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
PS50979. BC. 1 hit.
PS00866. CPSASE_1. 1 hit.
PS00867. CPSASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: cv. Nisqually.

Entry informationi

Entry nameiACCC1_POPTR
AccessioniPrimary (citable) accession number: B9HBA8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 2, 2010
Last sequence update: March 24, 2009
Last modified: July 22, 2015
This is version 48 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.