ACCD5_MYCTU
ID ACCD5_MYCTU Reviewed; 548 AA.
AC P9WQH7; L0TF57; P96885;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta5 subunit {ECO:0000305};
DE AltName: Full=Acetyl-CoA carboxylase {ECO:0000305};
DE Short=ACC {ECO:0000305};
DE EC=2.1.3.15 {ECO:0000269|PubMed:16354663, ECO:0000269|PubMed:16385038, ECO:0000269|PubMed:28222482};
DE AltName: Full=Propionyl-CoA carboxylase {ECO:0000305};
DE Short=PCC {ECO:0000305};
DE EC=2.1.3.- {ECO:0000269|PubMed:16354663, ECO:0000269|PubMed:16385038, ECO:0000269|PubMed:28222482};
GN Name=accD5 {ECO:0000303|PubMed:16354663}; Synonyms=pccB;
GN OrderedLocusNames=Rv3280; ORFNames=MTCY71.20;
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 PROTEIN SEQUENCE OF 2-14, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=16354663; DOI=10.1074/jbc.m511761200;
RA Oh T.J., Daniel J., Kim H.J., Sirakova T.D., Kolattukudy P.E.;
RT "Identification and characterization of Rv3281 as a novel subunit of a
RT biotin-dependent acyl-CoA carboxylase in Mycobacterium tuberculosis
RT H37Rv.";
RL J. Biol. Chem. 281:3899-3908(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, PATHWAY, AND SUBUNIT.
RX PubMed=16385038; DOI=10.1128/jb.188.2.477-486.2006;
RA Gago G., Kurth D., Diacovich L., Tsai S.C., Gramajo H.;
RT "Biochemical and structural characterization of an essential acyl coenzyme
RT A carboxylase from Mycobacterium tuberculosis.";
RL J. Bacteriol. 188:477-486(2006).
RN [4]
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 [5]
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 [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND PATHWAY.
RX PubMed=28222482; DOI=10.1111/febs.14046;
RA Bazet Lyonnet B., Diacovich L., Gago G., Spina L., Bardou F., Lemassu A.,
RA Quemard A., Gramajo H.;
RT "Functional reconstitution of the Mycobacterium tuberculosis long-chain
RT acyl-CoA carboxylase from multiple acyl-CoA subunits.";
RL FEBS J. 284:1110-1125(2017).
RN [7] {ECO:0007744|PDB:2A7S}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), STRUCTURE-BASED INHIBITOR DESIGN,
RP AND SUBUNIT.
RX PubMed=16492739; DOI=10.1073/pnas.0510580103;
RA Lin T.W., Melgar M.M., Kurth D., Swamidass S.J., Purdon J., Tseng T.,
RA Gago G., Baldi P., Gramajo H., Tsai S.C.;
RT "Structure-based inhibitor design of AccD5, an essential acyl-CoA
RT carboxylase carboxyltransferase domain of Mycobacterium tuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3072-3077(2006).
RN [8] {ECO:0007744|PDB:2BZR}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), AND SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=17157300; DOI=10.1016/j.febslet.2006.11.054;
RA Holton S.J., King-Scott S., Nasser Eddine A., Kaufmann S.H., Wilmanns M.;
RT "Structural diversity in the six-fold redundant set of acyl-CoA
RT carboxyltransferases in Mycobacterium tuberculosis.";
RL FEBS Lett. 580:6898-6902(2006).
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:16354663, PubMed:16385038, PubMed:28222482). When
CC associated with the alpha3 subunit AccA3, is involved in the
CC carboxylation of acetyl-CoA and propionyl-CoA, with a preference for
CC propionyl-CoA (PubMed:16354663, PubMed:16385038, PubMed:28222482). Is
CC also required for the activity of the long-chain acyl-CoA carboxylase
CC (LCC) complex (PubMed:28222482). {ECO:0000269|PubMed:16354663,
CC ECO:0000269|PubMed:16385038, ECO:0000269|PubMed:28222482}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-carboxybiotinyl-L-lysyl-[protein] = malonyl-
CC CoA + N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:54728,
CC Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:57384, ChEBI:CHEBI:83144, ChEBI:CHEBI:83145; EC=2.1.3.15;
CC Evidence={ECO:0000269|PubMed:16354663, ECO:0000269|PubMed:16385038,
CC ECO:0000269|PubMed:28222482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54729;
CC Evidence={ECO:0000269|PubMed:16354663, ECO:0000269|PubMed:16385038,
CC ECO:0000269|PubMed:28222482};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-carboxybiotinyl-L-lysyl-[protein] + propanoyl-CoA =
CC methylmalonyl-CoA + N(6)-biotinyl-L-lysyl-[protein];
CC Xref=Rhea:RHEA:66612, Rhea:RHEA-COMP:10505, Rhea:RHEA-COMP:10506,
CC ChEBI:CHEBI:57392, ChEBI:CHEBI:59916, ChEBI:CHEBI:83144,
CC ChEBI:CHEBI:83145; Evidence={ECO:0000269|PubMed:16354663,
CC ECO:0000269|PubMed:16385038, ECO:0000269|PubMed:28222482};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66613;
CC Evidence={ECO:0000269|PubMed:16354663, ECO:0000269|PubMed:16385038,
CC ECO:0000269|PubMed:28222482};
CC -!- ACTIVITY REGULATION: Carboxylase activity of the AccA3/AccD5 complex is
CC stimulated by interaction with AccE5. {ECO:0000269|PubMed:16354663,
CC ECO:0000269|PubMed:16385038}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=232 uM for acetyl-CoA (in the presence of alpha3 subunit)
CC {ECO:0000269|PubMed:16354663};
CC KM=377 uM for acetyl-CoA (in the presence of alpha3 and epsilon
CC subunits) {ECO:0000269|PubMed:16354663};
CC KM=220 uM for acetyl-CoA (in the presence of alpha3 and epsilon
CC subunits) {ECO:0000269|PubMed:28222482};
CC KM=105 uM for propionyl-CoA (in the presence of alpha3 subunit)
CC {ECO:0000269|PubMed:16354663};
CC KM=233 uM for propionyl-CoA (in the presence of alpha3 and epsilon
CC subunits) {ECO:0000269|PubMed:16354663};
CC KM=240 uM for propionyl-CoA (in the presence of alpha3 and epsilon
CC subunits) {ECO:0000269|PubMed:28222482};
CC Vmax=302 pmol/min/mg enzyme with acetyl-CoA as substrate (in the
CC presence of alpha3 subunit) {ECO:0000269|PubMed:16354663};
CC Vmax=2709 pmol/min/mg enzyme with acetyl-CoA as substrate (in the
CC presence of alpha3 and epsilon subunits)
CC {ECO:0000269|PubMed:16354663};
CC Vmax=120 nmol/min/mg enzyme with acetyl-CoA as substrate (in the
CC presence of alpha3 and epsilon subunits)
CC {ECO:0000269|PubMed:28222482};
CC Vmax=1095 pmol/min/mg enzyme with propionyl-CoA as substrate(in the
CC presence of alpha3 subunit) {ECO:0000269|PubMed:16354663};
CC Vmax=3442 pmol/min/mg enzyme with propionyl-CoA as substrate (in the
CC presence of alpha3 and epsilon subunits)
CC {ECO:0000269|PubMed:16354663};
CC Vmax=680 nmol/min/mg enzyme with propionyl-CoA as substrate (in the
CC presence of alpha3 and epsilon subunits)
CC {ECO:0000269|PubMed:28222482};
CC -!- PATHWAY: Lipid metabolism; mycolic acid biosynthesis.
CC {ECO:0000305|PubMed:16385038, ECO:0000305|PubMed:28222482}.
CC -!- SUBUNIT: Forms homohexamers (PubMed:16492739, PubMed:17157300). The
CC biotin-dependent acyl-CoA carboxylase complex is composed of AccA3,
CC which contains the biotin carboxylase (BC) and biotin carboxyl carrier
CC protein (BCCP) domains, and AccD5, which contains the carboxyl
CC transferase (CT) domain (PubMed:16354663, PubMed:16385038). The
CC AccA3/AccD5 complex forms a dodecamer, and can associate with the
CC epsilon subunit AccE5 (Rv3280), which stimulates carboxylation by the
CC complex (PubMed:16354663, PubMed:16385038). Is also part of the long-
CC chain acyl-CoA carboxylase (LCC) complex, which is composed of AccA3,
CC AccD4, AccD5 and AccE5. The four subunits are essential for activity,
CC but AccD5, together with AccE5, probably plays a structural role rather
CC than a catalytic one (PubMed:28222482). {ECO:0000269|PubMed:16354663,
CC ECO:0000269|PubMed:16385038, ECO:0000269|PubMed:16492739,
CC ECO:0000269|PubMed:17157300, ECO:0000269|PubMed:28222482}.
CC -!- INTERACTION:
CC P9WQH7; P9WQH7: accD5; NbExp=2; IntAct=EBI-7151762, EBI-7151762;
CC -!- INDUCTION: Expressed at higher levels during the exponential growth
CC phase. {ECO:0000269|PubMed:17114269}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46099.1; -; Genomic_DNA.
DR PIR; A70980; A70980.
DR RefSeq; NP_217797.1; NC_000962.3.
DR RefSeq; WP_003417136.1; NZ_NVQJ01000003.1.
DR PDB; 2A7S; X-ray; 2.90 A; A/B/C/D/E/F=1-548.
DR PDB; 2BZR; X-ray; 2.20 A; A/B/C/D/E/F=1-548.
DR PDBsum; 2A7S; -.
DR PDBsum; 2BZR; -.
DR AlphaFoldDB; P9WQH7; -.
DR SMR; P9WQH7; -.
DR MINT; P9WQH7; -.
DR STRING; 83332.Rv3280; -.
DR PaxDb; P9WQH7; -.
DR DNASU; 888725; -.
DR GeneID; 888725; -.
DR KEGG; mtu:Rv3280; -.
DR TubercuList; Rv3280; -.
DR eggNOG; COG4799; Bacteria.
DR OMA; YAYAECT; -.
DR PhylomeDB; P9WQH7; -.
DR BioCyc; MetaCyc:G185E-7554-MON; -.
DR UniPathway; UPA00915; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009317; C:acetyl-CoA carboxylase complex; IDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0032991; C:protein-containing complex; IPI:MTBBASE.
DR GO; GO:0003989; F:acetyl-CoA carboxylase activity; IDA:MTBBASE.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004658; F:propionyl-CoA carboxylase activity; IDA:MTBBASE.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0015977; P:carbon fixation; IDA:MTBBASE.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
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 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; Direct protein sequencing; Lipid metabolism;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16354663"
FT CHAIN 2..548
FT /note="Biotin-dependent acetyl-/propionyl-coenzyme A
FT carboxylase beta5 subunit"
FT /id="PRO_0000199799"
FT DOMAIN 25..281
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 295..541
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 25..39
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:2BZR"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 162..176
FT /evidence="ECO:0007829|PDB:2BZR"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:2BZR"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 232..236
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 249..254
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 255..266
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 300..302
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:2A7S"
FT HELIX 315..321
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 322..324
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 327..330
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:2BZR"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:2A7S"
FT HELIX 359..361
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 365..380
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 405..418
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 423..432
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 433..438
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 442..444
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 462..469
FT /evidence="ECO:0007829|PDB:2BZR"
FT TURN 470..475
FT /evidence="ECO:0007829|PDB:2A7S"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:2A7S"
FT HELIX 485..499
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:2BZR"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:2BZR"
FT HELIX 520..530
FT /evidence="ECO:0007829|PDB:2BZR"
FT TURN 531..533
FT /evidence="ECO:0007829|PDB:2BZR"
SQ SEQUENCE 548 AA; 59354 MW; A1C4C382ABBE3FAE CRC64;
MTSVTDRSAH SAERSTEHTI DIHTTAGKLA ELHKRREESL HPVGEDAVEK VHAKGKLTAR
ERIYALLDED SFVELDALAK HRSTNFNLGE KRPLGDGVVT GYGTIDGRDV CIFSQDATVF
GGSLGEVYGE KIVKVQELAI KTGRPLIGIN DGAGARIQEG VVSLGLYSRI FRNNILASGV
IPQISLIMGA AAGGHVYSPA LTDFVIMVDQ TSQMFITGPD VIKTVTGEEV TMEELGGAHT
HMAKSGTAHY AASGEQDAFD YVRELLSYLP PNNSTDAPRY QAAAPTGPIE ENLTDEDLEL
DTLIPDSPNQ PYDMHEVITR LLDDEFLEIQ AGYAQNIVVG FGRIDGRPVG IVANQPTHFA
GCLDINASEK AARFVRTCDC FNIPIVMLVD VPGFLPGTDQ EYNGIIRRGA KLLYAYGEAT
VPKITVITRK AYGGAYCVMG SKDMGCDVNL AWPTAQIAVM GASGAVGFVY RQQLAEAAAN
GEDIDKLRLR LQQEYEDTLV NPYVAAERGY VDAVIPPSHT RGYIGTALRL LERKIAQLPP
KKHGNVPL
