ACCD1_MYCTU
ID ACCD1_MYCTU Reviewed; 529 AA.
AC I6YDK7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase beta1 subunit {ECO:0000305};
DE AltName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0000303|PubMed:25695631};
DE Short=MCC {ECO:0000303|PubMed:25695631};
DE EC=2.1.3.- {ECO:0000269|PubMed:25695631};
GN Name=accD1 {ECO:0000303|PubMed:17114269};
GN OrderedLocusNames=Rv2502c {ECO:0000312|EMBL:CCP45296.1};
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 [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 [2]
RP INDUCTION.
RC STRAIN=H37Rv;
RX PubMed=17114269; DOI=10.1128/jb.01019-06;
RA Daniel J., Oh T.J., Lee C.M., Kolattukudy P.E.;
RT "AccD6, a member of the Fas II locus, is a functional carboxyltransferase
RT subunit of the acyl-coenzyme A carboxylase in Mycobacterium tuberculosis.";
RL J. Bacteriol. 189:911-917(2007).
RN [3]
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 [4]
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).
RN [5] {ECO:0007744|PDB:4Q0G}
RP X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS).
RG TB Structural Genomics Consortium (TBSGC);
RA Bie H.Y., Yin J., James M.N.G.;
RT "Crystal structure of beta subunit of acyl-CoA carboxylase AccD1 from
RT Mycobacterium tuberculosis.";
RL Submitted (APR-2014) to the PDB data bank.
CC -!- FUNCTION: Component of a biotin-dependent acyl-CoA carboxylase complex.
CC This subunit transfers the CO2 from carboxybiotin to the CoA ester
CC substrate (PubMed:25695631). When associated with the alpha1 subunit
CC AccA1, is involved in branched amino-acid catabolism with
CC methylcrotonyl coenzyme A as the substrate (PubMed:25695631). Shows
CC residual with propionyl-CoA and acetyl-CoA (PubMed:25695631).
CC {ECO:0000269|PubMed:25695631}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-(2E)-butenoyl-CoA + N(6)-carboxybiotinyl-L-lysyl-
CC [protein] = 3-methyl-(2E)-glutaconyl-CoA + N(6)-biotinyl-L-lysyl-
CC [protein]; Xref=Rhea:RHEA:13025, Rhea:RHEA-COMP:10505, Rhea:RHEA-
CC COMP:10506, ChEBI:CHEBI:57344, ChEBI:CHEBI:57346, ChEBI:CHEBI:83144,
CC ChEBI:CHEBI:83145; Evidence={ECO:0000269|PubMed:25695631};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13026;
CC Evidence={ECO:0000269|PubMed:25695631};
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}.
CC -!- INDUCTION: Does not show significant changes in expression throughout
CC M.tuberculosis growth phases. {ECO:0000269|PubMed:17114269}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AL123456; CCP45296.1; -; Genomic_DNA.
DR RefSeq; NP_217018.1; NC_000962.3.
DR RefSeq; WP_003412778.1; NZ_NVQJ01000063.1.
DR PDB; 4Q0G; X-ray; 2.31 A; A/B/C=1-529.
DR PDBsum; 4Q0G; -.
DR AlphaFoldDB; I6YDK7; -.
DR SMR; I6YDK7; -.
DR STRING; 83332.Rv2502c; -.
DR PaxDb; I6YDK7; -.
DR PRIDE; I6YDK7; -.
DR DNASU; 887168; -.
DR GeneID; 45426496; -.
DR GeneID; 887168; -.
DR KEGG; mtu:Rv2502c; -.
DR PATRIC; fig|83332.111.peg.2799; -.
DR TubercuList; Rv2502c; -.
DR eggNOG; COG4799; Bacteria.
DR OMA; AYLPIMS; -.
DR PhylomeDB; I6YDK7; -.
DR UniPathway; UPA00363; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; PTHR22855; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..529
FT /note="Biotin-dependent 3-methylcrotonyl-coenzyme A
FT carboxylase beta1 subunit"
FT /id="PRO_0000452368"
FT DOMAIN 16..272
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 275..521
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT HELIX 12..32
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 36..44
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:4Q0G"
FT TURN 69..74
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4Q0G"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 113..129
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:4Q0G"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 246..257
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 283..286
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 298..304
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 344..360
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 364..370
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 384..397
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 402..411
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 413..417
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 441..458
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 465..483
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:4Q0G"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:4Q0G"
FT HELIX 503..514
FT /evidence="ECO:0007829|PDB:4Q0G"
SQ SEQUENCE 529 AA; 56778 MW; 05117F0D699B5646 CRC64;
MTTPSIAIAP SFADEHRRLV AELNNKLAAA ALGGNERARK RHVSRGKLLP RERVDRLLDP
GSPFLELAPL AAGGMYGDES PGAGIITGIG RVSGRQCVIV ANDATVKGGT YYPMTVKKHL
RAQEVALQNM LPCIYLVDSG GAFLPRQDEV FPDREHFGRI FYNQATMSAK GIPQVAAVLG
SCTAGGAYVP AMSDEAVIVR EQGTIFLGGP PLVKAATGEI VSAEELGGGD LHSRTSGVTD
HLADDDEDAL RIVRAIADTF GPCEPAQWDV RRSVEPKYPQ AELYDVVPPD PRVPYDVHEV
VVRIVDGSEF SEFKAKYGKT LVTAFARVHG HPVGIVANNG VLFSESALKG AHFIELCDKR
KIPLLFLQNI AGFMVGRDYE AGGIAKHGAK MVTAVACARV PKLTVVIGGS YGAGNYSMCG
RAYSPRFLWM WPNARISVMG GEQAASVLAT VRGEQLSAAG TPWSPDEEEA FKAPIRAQYE
DQGNPYYSTA RLWDDGIIDP ADTRTVVGLA LSLCAHAPLD QVGYGVFRM
