ACCA3_MYCLE
ID ACCA3_MYCLE Reviewed; 598 AA.
AC P46392;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit {ECO:0000250|UniProtKB:P96890};
DE Includes:
DE RecName: Full=Biotin carboxylase {ECO:0000250|UniProtKB:P96890};
DE Short=BC {ECO:0000250|UniProtKB:P96890};
DE EC=6.3.4.14 {ECO:0000250|UniProtKB:P96890};
DE Includes:
DE RecName: Full=Biotin carboxyl carrier protein {ECO:0000250|UniProtKB:P96890};
DE Short=BCCP {ECO:0000250|UniProtKB:P96890};
GN Name=bccA; OrderedLocusNames=ML0726; ORFNames=B1308_C1_129;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7909542; DOI=10.1128/jb.176.9.2525-2531.1994;
RA Norman E., de Smet K.A.L., Stoker N.G., Ratledge C., Wheeler P.R.,
RA Dale J.W.;
RT "Lipid synthesis in mycobacteria: characterization of the biotin carboxyl
RT carrier protein genes from Mycobacterium leprae and M. tuberculosis.";
RL J. Bacteriol. 176:2525-2531(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: Component of a biotin-dependent acyl-CoA carboxylase complex.
CC This subunit catalyzes the ATP-dependent carboxylation of the biotin
CC carried by the biotin carboxyl carrier (BCC) domain, resulting in the
CC formation of carboxyl biotin. {ECO:0000250|UniProtKB:P96890}.
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:P96890};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000250|UniProtKB:P96890};
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 -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01066};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:P96890}.
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000250|UniProtKB:P96890}.
CC -!- SUBUNIT: The biotin-dependent acyl-CoA carboxylase complex is composed
CC of AccA3, which contains the biotin carboxylase (BC) and biotin
CC carboxyl carrier protein (BCCP) domains, and an AccD protein, which
CC contains the carboxyl transferase (CT) domain.
CC {ECO:0000250|UniProtKB:P96890}.
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DR EMBL; X63470; CAA45070.1; -; Genomic_DNA.
DR EMBL; U00012; AAA85920.1; -; Genomic_DNA.
DR EMBL; AL583919; CAC30235.1; -; Genomic_DNA.
DR PIR; A55579; A55579.
DR PIR; G86999; G86999.
DR RefSeq; NP_301567.1; NC_002677.1.
DR RefSeq; WP_010907891.1; NC_002677.1.
DR AlphaFoldDB; P46392; -.
DR SMR; P46392; -.
DR STRING; 272631.ML0726; -.
DR EnsemblBacteria; CAC30235; CAC30235; CAC30235.
DR KEGG; mle:ML0726; -.
DR PATRIC; fig|272631.5.peg.1321; -.
DR Leproma; ML0726; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_6_11; -.
DR OMA; ITHFHTP; -.
DR UniPathway; UPA00094; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000000806; Chromosome.
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-UniPathway.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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..598
FT /note="Biotin-dependent acyl-coenzyme A carboxylase alpha3
FT subunit"
FT /id="PRO_0000146797"
FT DOMAIN 8..452
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT DOMAIN 127..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 522..598
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT REGION 506..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 282
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 295
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 295
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 297
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOD_RES 564
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT CONFLICT 30
FT /note="D -> H (in Ref. 1; CAA45070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 598 AA; 63863 MW; 5F2E291D7C54515D CRC64;
MASHASSRIA KVLVANRGEI AVRVIRAARD ARLPSVAVYA EPDAEAPHVR LADEAFALGG
HTSAESYLDF GKILDAAAKS GANAIHPGYG FLAENADFAQ AVIDAGLIWI GPSPQSIRDL
GDKVTARHIA ARAQAPLVPG TPDPVKNADE VVAFAKEHGV PIAIKAAFGG GGKGMKVART
LEEISELYES AVREATVAFG RGECFVERYL DKPRHVEAQV IADQHGNIVV AGTRDCSLQR
RFQKLVEEAP APFLTDAQRK EIHESAKRIC KEAHYYGAGT VEYLVGQDGL ISFLEVNTRL
QVEHPVTEET TGIDLVLQQF KIANGEKLEL IKDPIPCGHA IEFRINGEDA GRNFLPSPGP
VSKFHPPTGP GVRLDSGVET GSVIGGQFDS MLAKLIVHGA TRQEALARAR RALDEFEVEG
LATVIPFHRA VVSDPALIGD NNSFSVHTRW IETEWNNTIE PFIDNQPLDE EDTRPQQTVI
VEVDGRRLEV SLPADLALAN PAGCNPAGVI RKKPKPRKRG GHTGAATSGD AVTAPMQGTV
VKVAVAEGQT VMTGDLVVVL EAMKMENPVT AHKDGIITGL AVEAGTAITQ GTVLAEIK
