ID I2DT96_9BURK Unreviewed; 487 AA.
AC I2DT96;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Biotin carboxylase {ECO:0000256|ARBA:ARBA00017242, ECO:0000256|RuleBase:RU365063};
DE EC=6.3.4.14 {ECO:0000256|ARBA:ARBA00013263, ECO:0000256|RuleBase:RU365063};
DE AltName: Full=Acetyl-coenzyme A carboxylase biotin carboxylase subunit A {ECO:0000256|ARBA:ARBA00033786, ECO:0000256|RuleBase:RU365063};
GN ORFNames=MYA_3513 {ECO:0000313|EMBL:AFJ87872.1};
OS Burkholderia sp. KJ006.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ87872.1, ECO:0000313|Proteomes:UP000010108};
RN [1] {ECO:0000313|EMBL:AFJ87872.1, ECO:0000313|Proteomes:UP000010108}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KJ006 {ECO:0000313|EMBL:AFJ87872.1,
RC ECO:0000313|Proteomes:UP000010108};
RX PubMed=22843575; DOI=10.1128/JB.00821-12;
RA Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT Strain KJ006.";
RL J. Bacteriol. 194:4432-4433(2012).
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|ARBA:ARBA00003761, 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|ARBA:ARBA00000861,
CC ECO:0000256|RuleBase:RU365063};
CC -!- PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from
CC acetyl-CoA: step 1/1. {ECO:0000256|ARBA:ARBA00004956,
CC 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|ARBA:ARBA00011750,
CC ECO:0000256|RuleBase:RU365063}.
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DR EMBL; CP003515; AFJ87872.1; -; Genomic_DNA.
DR RefSeq; WP_014724303.1; NC_017921.1.
DR AlphaFoldDB; I2DT96; -.
DR KEGG; buk:MYA_3513; -.
DR PATRIC; fig|416344.3.peg.3570; -.
DR HOGENOM; CLU_000395_3_2_4; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000010108; Chromosome 2.
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; PTHR48095:SF2; BIOTIN CARBOXYLASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755}.
FT DOMAIN 15..460
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 134..331
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 487 AA; 52800 MW; 377D96C879914247 CRC64;
MSLATSSGTF YRPSRIRTVL VANRGEIAVR IIRAAHELGM RAIAVVSDAD RDSLAARMAD
EAIHIGPSHA AKSYLNPAAI LDAARRCGAD AIHPGYGFLS ENAAFAAQVE AAGLIFVGPD
AHVIATMGDK ARARETAQRA NVPTVPGSDG VVHSLEEAQA VAARIGYPLM IKAAAGGGGR
GIRVSHDAAQ LEAELPLAQR EAQAAFGNGG VYLERFIARA RHIEVQVLGD GRNVVHLFER
ECSLQRRRQK ILEEAPSPSL TPAQRDALCE SATRLAREVG YRSAGTLEYL YDDARGKFYF
IEMNTRIQVE HPVTEAITGI DLVRETLRIA DGEPLRFAQQ DIAMRGAAIE CRINAEDPLQ
DFRPNPGRID TLVWPTGAGT RIDSLLYPGY VVPPFYDSLL AKLIVHDESR AAALQRLARA
LGELHVGGVK TTAPLHLALL ADDDVRAGRY HTNFLEAWMP QWREAVTARA RQHADTEADA
ARVGEAQ
//
