GenomeNet

Database: UniProt
Entry: B9N843
LinkDB: B9N843
Original site: B9N843 
ID   ACCC2_POPTR             Reviewed;         526 AA.
AC   B9N843; U5FKU1;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 2.
DT   16-JAN-2019, entry version 68.
DE   RecName: Full=Biotin carboxylase 2, chloroplastic;
DE            EC=6.3.4.14;
DE   AltName: Full=Acetyl-CoA carboxylase subunit A 2;
DE            Short=ACC;
DE            EC=6.4.1.2;
DE   Flags: Precursor;
GN   ORFNames=POPTR_0018s14250g;
OS   Populus trichocarpa (Western balsam poplar) (Populus balsamifera
OS   subsp. trichocarpa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; fabids; Malpighiales; Salicaceae; Saliceae;
OC   Populus.
OX   NCBI_TaxID=3694;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nisqually;
RX   PubMed=16973872; DOI=10.1126/science.1128691;
RA   Tuskan G.A., Difazio S., Jansson S., Bohlmann J., Grigoriev I.,
RA   Hellsten U., Putnam N., Ralph S., Rombauts S., Salamov A., Schein J.,
RA   Sterck L., Aerts A., Bhalerao R.R., Bhalerao R.P., Blaudez D.,
RA   Boerjan W., Brun A., Brunner A., Busov V., Campbell M., Carlson J.,
RA   Chalot M., Chapman J., Chen G.-L., Cooper D., Coutinho P.M.,
RA   Couturier J., Covert S., Cronk Q., Cunningham R., Davis J.,
RA   Degroeve S., Dejardin A., dePamphilis C.W., Detter J., Dirks B.,
RA   Dubchak I., Duplessis S., Ehlting J., Ellis B., Gendler K.,
RA   Goodstein D., Gribskov M., Grimwood J., Groover A., Gunter L.,
RA   Hamberger B., Heinze B., Helariutta Y., Henrissat B., Holligan D.,
RA   Holt R., Huang W., Islam-Faridi N., Jones S., Jones-Rhoades M.,
RA   Jorgensen R., Joshi C., Kangasjaervi J., Karlsson J., Kelleher C.,
RA   Kirkpatrick R., Kirst M., Kohler A., Kalluri U., Larimer F.,
RA   Leebens-Mack J., Leple J.-C., Locascio P., Lou Y., Lucas S.,
RA   Martin F., Montanini B., Napoli C., Nelson D.R., Nelson C.,
RA   Nieminen K., Nilsson O., Pereda V., Peter G., Philippe R., Pilate G.,
RA   Poliakov A., Razumovskaya J., Richardson P., Rinaldi C., Ritland K.,
RA   Rouze P., Ryaboy D., Schmutz J., Schrader J., Segerman B., Shin H.,
RA   Siddiqui A., Sterky F., Terry A., Tsai C.-J., Uberbacher E.,
RA   Unneberg P., Vahala J., Wall K., Wessler S., Yang G., Yin T.,
RA   Douglas C., Marra M., Sandberg G., Van de Peer Y., Rokhsar D.S.;
RT   "The genome of black cottonwood, Populus trichocarpa (Torr. & Gray).";
RL   Science 313:1596-1604(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nisqually;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Grigoriev I.V., Terry A., Salamov A.A., Otillar R., Lou Y., Lucas S.,
RA   Hammon N., Glavina del Rio T., Detter J., Kalin E., Tice H.,
RA   Pitluck S., Chapman J., Putnam N.H., Brunner A., Busov V.,
RA   Campbell M., Chalot M., Covert S., Davis J., DiFazio S., Gribskov M.,
RA   Gunter L., Hamberger B., Jansson S., Joshi C., Larimer F., Martin F.,
RA   Napoli C., Nelson D., Ralph S., Rombauts S., Rouze P., Schrader J.,
RA   Tsai C., Vahala J., Tuskan G., Rokhsar D.;
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is a component of the acetyl coenzyme A
CC       carboxylase complex; first, biotin carboxylase catalyzes the
CC       carboxylation of the carrier protein and then the transcarboxylase
CC       transfers the carboxyl group to form malonyl-CoA.
CC       {ECO:0000250|UniProtKB:O04983}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein]
CC         = ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505,
CC         Rhea:RHEA-COMP:10506, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:83144,
CC         ChEBI:CHEBI:83145, ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) +
CC         malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384,
CC         ChEBI:CHEBI:456216; EC=6.4.1.2;
CC         Evidence={ECO:0000250|UniProtKB:O04983};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000250};
CC   -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA
CC       from acetyl-CoA: step 1/1.
CC   -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer composed of
CC       biotin carboxyl carrier protein, biotin carboxylase and two
CC       subunits each of ACCase subunit alpha and ACCase plastid-coded
CC       subunit beta (accD). {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
DR   EMBL; CM009307; ERP49997.1; -; Genomic_DNA.
DR   RefSeq; XP_006372200.1; XM_006372138.1.
DR   SMR; B9N843; -.
DR   STRING; 3694.POPTR_0018s14250.1; -.
DR   PRIDE; B9N843; -.
DR   GeneID; 18107844; -.
DR   KEGG; pop:18107844; -.
DR   eggNOG; ENOG410IU5C; Eukaryota.
DR   eggNOG; COG0439; LUCA.
DR   HOGENOM; HOG000008988; -.
DR   InParanoid; B9N843; -.
DR   KO; K01961; -.
DR   OMA; FVEICSH; -.
DR   UniPathway; UPA00655; UER00711.
DR   Proteomes; UP000006729; Chromosome 18.
DR   Proteomes; UP000006729; Unassembled WGS sequence.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:2001295; P:malonyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR00514; accC; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Biotin; Chloroplast; Complete proteome;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Ligase;
KW   Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding; Plastid; Reference proteome;
KW   Transit peptide.
FT   TRANSIT       1     71       Chloroplast. {ECO:0000255}.
FT   CHAIN        72    526       Biotin carboxylase 2, chloroplastic.
FT                                /FTId=PRO_0000391774.
FT   DOMAIN      185    382       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     213    274       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   ACT_SITE    357    357       {ECO:0000250}.
FT   METAL       340    340       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       353    353       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       353    353       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       355    355       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   BINDING     181    181       ATP. {ECO:0000250}.
FT   BINDING     265    265       ATP. {ECO:0000250}.
FT   BINDING     300    300       ATP. {ECO:0000250}.
SQ   SEQUENCE   526 AA;  57497 MW;  CAC6A56109E42892 CRC64;
     MEATLPVCKS VTSTPGLFMK RNSGIRNSQC SFMVGTKVNF PRQRTQATQA NHCAKKNGGA
     LGVTCRAEKI LVANRGEIAV RVIRTAHELG IPCVAVYSTI DKDALHVKLA DESVCIGEAP
     SNQSYLVIQN VLSAAISRGC TMLHPGYGFL AENAVFVEMC REHGINFIGP NPDSIRVMGD
     KSTARETMKK ANVPTVPGSD GLLQSTEEAV KLASEIGYPV MIKATAGGGG RGMRLAKEPD
     EFVKLLQQAK SEAAAAFGND GVYLEKYVQN PRHIEFQVLA DKFGNVVHFG ERDCSIQRRN
     QKLLEEAPSP ALTPELRKAM GDAAVAAAAS IGYIGVGTVE FLLDERGSFY FMEMNTRIQV
     EHPVTEMISS VDLIEEQIRV AMGEKIQYKQ EDIVLRGHSI ECRINAEDAF KGFRPGPGRI
     TAYLPSGGPF VRMDSHVYPD YVVPPSYDSL LGKLIVWAPT REKAIERMKR ALDDTIITGV
     PTTIDYHKLI LDIEDFKNGN VDTAFIPKHE QELAAPQQII LANSAS
//
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