ID A0A2Z6EXE0_9BURK Unreviewed; 455 AA.
AC A0A2Z6EXE0;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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 Name=accC {ECO:0000313|EMBL:GLR00478.1};
GN ORFNames=GCM10007934_02890 {ECO:0000313|EMBL:GLR00478.1}, MCB1EB_1901
GN {ECO:0000313|EMBL:BBE10062.1};
OS Mycoavidus cysteinexigens.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Mycoavidus.
OX NCBI_TaxID=1553431 {ECO:0000313|EMBL:BBE10062.1, ECO:0000313|Proteomes:UP000282597};
RN [1] {ECO:0000313|EMBL:BBE10062.1, ECO:0000313|Proteomes:UP000282597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1-EB {ECO:0000313|EMBL:BBE10062.1,
RC ECO:0000313|Proteomes:UP000282597};
RX PubMed=29540638; DOI=10.1264/jsme2.ME17138;
RA Sharmin D., Guo Y., Nishizawa T., Ohshima S., Sato Y., Takashima Y.,
RA Narisawa K., Ohta H.;
RT "Comparative Genomic Insights into Endofungal Lifestyles of Two Bacterial
RT Endosymbionts, Mycoavidus cysteinexigens and Burkholderia rhizoxinica.";
RL Microbes Environ. 33:66-76(2018).
RN [2] {ECO:0000313|EMBL:GLR00478.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR00478.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GLR00478.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 110909 {ECO:0000313|EMBL:GLR00478.1};
RA Sun Q., Mori K.;
RT "Draft genome sequence of Mycoavidus cysteinexigens strain NBRC 110909.";
RL Submitted (JAN-2023) 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|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; AP018150; BBE10062.1; -; Genomic_DNA.
DR EMBL; BSOD01000005; GLR00478.1; -; Genomic_DNA.
DR RefSeq; WP_045364759.1; NZ_BSOD01000005.1.
DR AlphaFoldDB; A0A2Z6EXE0; -.
DR GeneID; 84624505; -.
DR KEGG; mcys:MCB1EB_1901; -.
DR UniPathway; UPA00655; UER00711.
DR Proteomes; UP000282597; Chromosome.
DR Proteomes; UP001156688; Unassembled WGS sequence.
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; 3.40.50.20; -; 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 InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase.
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 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};
KW Biotin {ECO:0000256|ARBA:ARBA00023267, 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000282597}.
FT DOMAIN 1..445
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 455 AA; 50527 MW; 9DBD3D60182C8681 CRC64;
MFEKILIANR GEIALRIQRA CRELGVKTVV VYSEADKEAK YVRLADEAVC IGPAPSAQSY
LNMPAIISAA EVTDAEAIHP GYGFLSENAD FAERVEQSGF TFIGPRPETI RLMGDKVSAK
QTMIKAGVPC VPGSEGALPE DPKEIIKLAR QITYPVIIKA AGGGGGRGMR VVHTEAALIN
AVNMTREEAG RAFGNPNVYM EKFLENPRHI EIQVLADSFK HAIWLGERDC SMQRRHQKVI
EEAPAPHISR RLIERIGDRC VDACKKMGYL GAGTFEFLYE NNEFYFIEMN TRVQVEHPVT
EMITGIDIVQ EQIRVAAGEK LRFKQREVIL KGHAIECRIN AEDAYKFTPS PGRITSWHAP
GGPGIRVDSH AYHSYFVPSH YDSMIGKVIA YGATREQAIS RMSIALSEMV VEGIHTNIPL
HRELMLDAKF VEGGTSIHYL ENKLAAKHQA TLQKA
//
