ACCA1_MYCTU
ID ACCA1_MYCTU Reviewed; 654 AA.
AC P9WPQ3; L0T9T8; P0A508; P46401;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit {ECO:0000305};
DE Includes:
DE RecName: Full=Biotin carboxylase {ECO:0000305};
DE Short=BC {ECO:0000305};
DE EC=6.3.4.14 {ECO:0000305|PubMed:25695631};
DE Includes:
DE RecName: Full=Biotin carboxyl carrier protein {ECO:0000305};
DE Short=BCCP {ECO:0000305};
GN Name=accA1; Synonyms=bccA; OrderedLocusNames=Rv2501c;
GN ORFNames=MTCY07A7.07c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate 50410;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [3]
RP PUPYLATION AT LYS-322, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT.
RX PubMed=25695631; DOI=10.1371/journal.ppat.1004623;
RA Ehebauer M.T., Zimmermann M., Jakobi A.J., Noens E.E., Laubitz D.,
RA Cichocki B., Marrakchi H., Laneelle M.A., Daffe M., Sachse C.,
RA Dziembowski A., Sauer U., Wilmanns M.;
RT "Characterization of the mycobacterial acyl-CoA carboxylase holo complexes
RT reveals their functional expansion into amino acid catabolism.";
RL PLoS Pathog. 11:e1004623-e1004623(2015).
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 (PubMed:25695631). When associated with
CC the beta1 subunit AccD1, is involved in branched amino-acid catabolism
CC with methylcrotonyl coenzyme A as the substrate (PubMed:25695631).
CC {ECO:0000269|PubMed:25695631}.
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:0000305|PubMed:25695631};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13502;
CC Evidence={ECO:0000305|PubMed:25695631};
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: Amino-acid degradation; L-leucine degradation.
CC {ECO:0000269|PubMed:25695631}.
CC -!- SUBUNIT: The biotin-dependent acyl-CoA carboxylase complex is composed
CC of AccA1, which contains the biotin carboxylase (BC) and biotin
CC carboxyl carrier protein (BCCP) domains, and AccD1, which contains the
CC carboxyl transferase (CT) domain (PubMed:25695631). The AccA1/AccD1
CC complex forms a dodecamer (PubMed:25695631).
CC {ECO:0000269|PubMed:25695631}.
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DR EMBL; Z19549; CAA79609.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP45295.1; -; Genomic_DNA.
DR PIR; B55579; B55579.
DR RefSeq; NP_217017.1; NC_000962.3.
DR RefSeq; WP_003899356.1; NZ_NVQJ01000063.1.
DR AlphaFoldDB; P9WPQ3; -.
DR SMR; P9WPQ3; -.
DR STRING; 83332.Rv2501c; -.
DR PaxDb; P9WPQ3; -.
DR DNASU; 887309; -.
DR GeneID; 45426495; -.
DR GeneID; 887309; -.
DR KEGG; mtu:Rv2501c; -.
DR TubercuList; Rv2501c; -.
DR eggNOG; COG4770; Bacteria.
DR OMA; FVEICSH; -.
DR PhylomeDB; P9WPQ3; -.
DR UniPathway; UPA00363; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR011761; ATP-grasp.
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 1: Evidence at protein level;
KW ATP-binding; Biotin; Isopeptide bond; Ligase; Magnesium; Manganese;
KW Metal-binding; Nucleotide-binding; Reference proteome; Ubl conjugation.
FT CHAIN 1..654
FT /note="Biotin-dependent 3-methylcrotonyl-coenzyme A
FT carboxylase alpha1 subunit"
FT /id="PRO_0000146798"
FT DOMAIN 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00969"
FT DOMAIN 120..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 578..653
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT BINDING 148..209
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
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 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
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="1"
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="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 292
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MOD_RES 620
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT CROSSLNK 322
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
SQ SEQUENCE 654 AA; 70592 MW; FAA0A1A46432CABF CRC64;
MFDTVLVANR GEIAVRVIRT LRRLGIRSVA VYSDPDVDAR HVLEADAAVR LGPAPARESY
LDIGKVLDAA ARTGAQAIHP GYGFLAENAD FAAACERARV VFLGPPARAI EVMGDKIAAK
NAVAAFDVPV VPGVARAGLT DDALVTAAAE VGYPVLIKPS AGGGGKGMRL VQDPARLPEA
LVSARREAMS SFGDDTLFLE RFVLRPRHIE VQVLADAHGN VVHLGERECS LQRRHQKVIE
EAPSPLLDPQ TRERIGVAAC NTARCVDYVG AGTVEFIVSA QRPDEFFFME MNTRLQVEHP
VTEAITGLDL VEWQLRVGAG EKLGFAQNDI ELRGHAIEAR VYAEDPAREF LPTGGRVLAV
FEPAGPGVRV DSSLLGGTVV GSDYDPLLTK VIAHGADREE ALDRLDQALA RTAVLGVQTN
VEFLRFLLAD ERVRVGDLDT AVLDERSADF TARPAPDDVL AAGGLYRQWA LARRAQGDLW
AAPSGWRGGG HMAPVRTAMR TPLRSETVSV WGPPESAQVQ VGDGEIDCAS VQVTREQMSV
TISGLRRDYR WAEADRHLWI ADERGTWHLR EAEEHKIHRA VGARPAEVVS PMPGSVIAVQ
VESGSQISAG DVVVVVEAMK MEHSLEAPVS GRVQVLVSVG DQVKVEQVLA RIKD
