ACCC_ALKHC
ID ACCC_ALKHC Reviewed; 452 AA.
AC Q9KDS9;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Biotin carboxylase;
DE EC=6.3.4.14 {ECO:0000250|UniProtKB:P24182};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000305};
GN Name=accC; OrderedLocusNames=BH1132;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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:P24182}.
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:0000250|UniProtKB:P24182};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00409};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000250|UniProtKB:P24182}.
CC -!- SUBUNIT: Acetyl-CoA carboxylase is a heterohexamer of biotin carboxyl
CC carrier protein, biotin carboxylase and the two subunits of carboxyl
CC transferase in a 2:2 complex. {ECO:0000250|UniProtKB:P24182}.
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DR EMBL; BA000004; BAB04851.1; -; Genomic_DNA.
DR PIR; D83791; D83791.
DR RefSeq; WP_010897302.1; NC_002570.2.
DR AlphaFoldDB; Q9KDS9; -.
DR SMR; Q9KDS9; -.
DR STRING; 272558.10173748; -.
DR EnsemblBacteria; BAB04851; BAB04851; BAB04851.
DR KEGG; bha:BH1132; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_9; -.
DR OMA; IYYDPML; -.
DR OrthoDB; 361205at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000001258; Chromosome.
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; 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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin; Fatty acid biosynthesis; Fatty acid metabolism;
KW Ligase; Lipid biosynthesis; Lipid metabolism; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..452
FT /note="Biotin carboxylase"
FT /id="PRO_0000146788"
FT DOMAIN 1..445
FT /note="Biotin carboxylation"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT ACT_SITE 292
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 164..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 200..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 235
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 237
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 275
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 288
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 290
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 292
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 295
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 338
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000250|UniProtKB:P24182"
FT BINDING 338
FT /ligand="hydrogencarbonate"
FT /ligand_id="ChEBI:CHEBI:17544"
FT /evidence="ECO:0000250|UniProtKB:P24182"
SQ SEQUENCE 452 AA; 49938 MW; 4BCF230D1A44E880 CRC64;
MFKKVLIANR GEIAVRIIRT CQKLNIRTVA IYSEADVDSL HVKHADEAFL IGKPPVAESY
LKVDTILEVA KQAGVDAIHP GYGLLSENAR FARACVEAGI SFIGPSPEVI ERMGSKIAAR
TAMQTAGVPV IPGSDVALAD EEEAVHLARK FGYPVMLKAS AGGGGIGMQL VRNDEEMRKA
FAGNQKRATS FFGDGTMFLE KAVENPRHIE VQIAADHHGH VVHLWERDCS IQRRHQKVVE
EAPSPFVDEA LREKIGQLAV KAAKAIDYRN LGTVECLVDG EKNIYFLEMN TRLQVEHPVT
EEITGIDLVE WQLLIAAGEQ LPYAQHEIPL QGHAIEVRIY AEDPVTFFPS PGMIKRFTLP
EGEGIRHEYA ISEGYKVTPF YDPMVAKLIV SADTRGEAIQ RLGRALKQYE IEGIKTNIPM
LKQVINHPVF QAGEATTAFV TNHLKVKTGR NP
