ID I5ATN6_EUBCE Unreviewed; 461 AA.
AC I5ATN6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Biotin carboxylase {ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|RuleBase:RU365063};
GN ORFNames=EubceDRAFT1_1347 {ECO:0000313|EMBL:EIM57159.1};
OS [Eubacterium] cellulosolvens 6.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=633697 {ECO:0000313|EMBL:EIM57159.1, ECO:0000313|Proteomes:UP000005753};
RN [1] {ECO:0000313|EMBL:EIM57159.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57159.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Anderson I.J., Johnson E.,
RA Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EIM57159.1, ECO:0000313|Proteomes:UP000005753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6 {ECO:0000313|EMBL:EIM57159.1,
RC ECO:0000313|Proteomes:UP000005753};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Gu W., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Johnson E., Mukhopadhyay B.,
RA Anderson I., Woyke T.;
RT "Improved High-Quality Draft sequence of Eubacterium cellulosolvens 6.";
RL Submitted (FEB-2012) 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:0000256|RuleBase:RU365063}.
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|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|RuleBase:RU365063}.
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:0000256|RuleBase:RU365063}.
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DR EMBL; CM001487; EIM57159.1; -; Genomic_DNA.
DR AlphaFoldDB; I5ATN6; -.
DR STRING; 633697.EubceDRAFT1_1347; -.
DR eggNOG; COG0439; Bacteria.
DR HOGENOM; CLU_000395_3_2_9; -.
DR OrthoDB; 9807469at2; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000005753; Chromosome.
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:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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 Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
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 NCBIfam; TIGR00514; accC; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 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; PS00866; CPSASE_1; 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|RuleBase:RU365063};
KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW Fatty acid metabolism {ECO:0000256|RuleBase:RU365063};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU365063};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU365063};
KW Lipid metabolism {ECO:0000256|RuleBase:RU365063};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000005753}.
FT DOMAIN 1..446
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 461 AA; 50959 MW; 57D63C6E9380079B CRC64;
MFKKILIANR GEIAMRVLRC AQEMGIETVV AYSSEDAETL PVQFATEAVC IGPAPAAKSY
LNQDSLIAAA LAYHCEAIHP GYGFLSENAE FARKCEKNGI IFIGPSSRMI KGMGDKQRAR
ALMKKYGVPV VPGSDGVLED WKEAARIAEK VGYPVLIKAS AGGGGRGMRT AYDANEIQAA
FENAQAEALA AFGDGSMYLE KLIQHPHHIE VQILGDRKGH IIHLGERDCS MQRRNQKLLE
EAPAKILTSR QREAIHKAAV RAAKAVHYVS AGTVEFVLDK EGNFYFIEMN TRIQVEHPVT
EMITGVDLIR EQIRIAAGLE LSYRQSDIRI SGHAIECRIN AENPAKNFAP CPGSVPFLHF
PCGCGIRIES ALYPGSKISP YYDSMIAKVI VHAPGRLEAI RKMRVALEEL TIQGVDTNVD
FLYLIMFNSD YMVGNVDTGF LEKDTEAIIR WGEESRKQSR R
//
