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Database: UniProt
Entry: O04849_BRANA
LinkDB: O04849_BRANA
Original site: O04849_BRANA 
ID   O04849_BRANA            Unreviewed;       640 AA.
AC   O04849;
DT   01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:CAA71346.1};
DE            EC=6.4.1.2 {ECO:0000313|EMBL:CAA71346.1};
DE   Flags: Fragment;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000313|EMBL:CAA71346.1};
RN   [1] {ECO:0000313|EMBL:CAA71346.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=9096417; DOI=10.1073/pnas.94.7.3465;
RA   Schulte W., Topfer R., Stracke R., Schell J., Martini N.;
RT   "Multi-functional acetyl-CoA carboxylase from Brassica napus is encoded by
RT   a multi-gene family: indication for plastidic localization of at least one
RT   isoform.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:3465-3470(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + N(6)-biotinyl-L-lysyl-[protein] =
CC         ADP + H(+) + N(6)-carboxybiotinyl-L-lysyl-[protein] + phosphate;
CC         Xref=Rhea:RHEA:13501, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145,
CC         ChEBI:CHEBI:456216; EC=6.3.4.14;
CC         Evidence={ECO:0000256|ARBA:ARBA00000861};
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DR   EMBL; Y10301; CAA71346.1; -; Genomic_DNA.
DR   PIR; T07923; T07923.
DR   AlphaFoldDB; O04849; -.
DR   EnsemblPlants; CDX91737; CDX91737; GSBRNA2T00153243001.
DR   Gramene; CDX91737; CDX91737; GSBRNA2T00153243001.
DR   ExpressionAtlas; O04849; baseline.
DR   GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR   InterPro; IPR049076; ACCA.
DR   InterPro; IPR049074; ACCA_BT.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
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   PANTHER; PTHR45728:SF3; ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR   Pfam; PF21385; ACCA_BT; 1.
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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAA71346.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}.
FT   DOMAIN          33..540
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          186..378
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   NON_TER         640
FT                   /evidence="ECO:0000313|EMBL:CAA71346.1"
SQ   SEQUENCE   640 AA;  70096 MW;  02E587EBA3B78E1C CRC64;
     MAGSVNGYQT PGRNHVSVSE VDDFCIALGG KRPIHSILIA NNGMAAVKFI RSVRTWAYET
     FGTERAILLV GMATPEDMRI NAEHIRIADQ FVEVPGGTNN NNYANVQLIV EMAEVTRVDA
     VWPGWGHASE NPELPDALKA KGIIFLGPPA ASMAALGDKI GSSLIAQAAD VPTLPWSGSH
     VKIPPDSSLV TIPEEIYRQA CVYTTEEAIA SCQVVGYPAM IKASWGGGGK GIRKVHNADE
     VRALFKQVQG EVPGSPIFIM KVASQSRHLE VQLLCDQYGN VSALHSRDCS VQRRHQKIIE
     EGPITVAPQE TIKKLEQAGR RLAKSVNYVG AATVEYLYSM DTGEYYFLEL NPRLQVEHPV
     TEWIAEINLP AAQVAVGMGI PLWQIPEIRR FYGIEHGGGY DSWRKTSVLA SPFDFDKAES
     IRPKGHCVAV RVTSEDPDDG FKPTSGKVQE LSFKSKPNVW AYFSVKSGGG IHEFSDSQFG
     HVFAFGESRA LAIANMVLGL KEIQIRGEIR TNVDYTIDLL HASDYRENKI HTGWLDSRIA
     MRVRAERPPW YLSVVGGALY KASATSAAVV SDYVGYLEKG QIPPKHISLV HSQVSLNIEG
     SKYTIDVVRG GSGSYRLRMN NSEVVAEIHT LRDGGLLMQA
//
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