ID O04850_BRANA Unreviewed; 371 AA.
AC O04850;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Acetyl-CoA carboxylase {ECO:0000313|EMBL:CAA71347.1};
DE EC=6.4.1.2 {ECO:0000313|EMBL:CAA71347.1};
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:CAA71347.1};
RN [1] {ECO:0000313|EMBL:CAA71347.1}
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; Y10302; CAA71347.1; -; Genomic_DNA.
DR PIR; T07938; T07938.
DR AlphaFoldDB; O04850; -.
DR EnsemblPlants; CDY20938; CDY20938; GSBRNA2T00013313001.
DR Gramene; CDY20938; CDY20938; GSBRNA2T00013313001.
DR ExpressionAtlas; O04850; baseline.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.90.1770.10; PreATP-grasp domain; 1.
DR InterPro; IPR049076; ACCA.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR PANTHER; PTHR45728:SF7; ACETYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR45728; ACETYL-COA CARBOXYLASE, ISOFORM A; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50979; BC; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CAA71347.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 135..371
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT NON_TER 371
FT /evidence="ECO:0000313|EMBL:CAA71347.1"
SQ SEQUENCE 371 AA; 39746 MW; 82F54696912CF1E1 CRC64;
MEMRALVSCS AAGNGASDRF RLSNVSPWIT SARGASGSDS PATVKLGSSS MIRAFKGVSI
YKNKTRRNVL SQRNKQFRPM AYLGRKDLSS PDPTSFCDND ISEPQGTGSI NGNDHSAVRV
SQVDEFCKAH GGKRPIHSIL VATNGMAAVK LIRSVRAWSY QTFGSEKSIS LVAMATPEDM
RINAEHIRIA DQFMQVPGGT NNNNYANVHL IVEMAQATGV DAVWPGWGHA SENPELPDAL
KAKGVIFLGP TAASMLALGD KIGSSLIAQA ADVPTLPWSG SHVKIPPGSS MVTIPEEMYR
QACVYTTEEA VASCQVVGYP AMIKASWGGG GKGIREVHDD DEVRTLFKQV QGEVPGSPIF
IMKVASQSRH L
//
