MCCB_DROME
ID MCCB_DROME Reviewed; 578 AA.
AC Q9V9A7; O18364; Q8SXT5;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Probable methylcrotonoyl-CoA carboxylase beta chain, mitochondrial;
DE Short=MCCase subunit beta;
DE EC=6.4.1.4;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 2;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit;
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta;
DE Flags: Precursor;
GN Name=Mccc2 {ECO:0000312|FlyBase:FBgn0042083};
GN Synonyms=l(2)04524 {ECO:0000312|FlyBase:FBgn0042083};
GN ORFNames=CG3267 {ECO:0000312|FlyBase:FBgn0042083};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|EMBL:AAM70824.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 43-126 AND 271-578, AND TISSUE SPECIFICITY.
RC TISSUE=Larval CNS, and Larval ring gland;
RX PubMed=9584098; DOI=10.1093/genetics/149.1.217;
RA Harvie P.D., Filippova M., Bryant P.J.;
RT "Genes expressed in the ring gland, the major endocrine organ of Drosophila
RT melanogaster.";
RL Genetics 149:217-231(1998).
CC -!- FUNCTION: Carboxyltransferase subunit of the 3-methylcrotonyl-CoA
CC carboxylase, an enzyme that catalyzes the conversion of 3-
CC methylcrotonyl-CoA to 3-methylglutaconyl-CoA, a critical step for
CC leucine and isovaleric acid catabolism (By similarity). Vital for adult
CC survival. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-methyl-(2E)-butenoyl-CoA + ATP + hydrogencarbonate = 3-
CC methyl-(2E)-glutaconyl-CoA + ADP + H(+) + phosphate;
CC Xref=Rhea:RHEA:13589, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57344,
CC ChEBI:CHEBI:57346, ChEBI:CHEBI:456216; EC=6.4.1.4;
CC -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC 3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in third instar larval ring gland
CC (lateral and medial secretory cells and corpus cardiacum cells) and
CC CNS. {ECO:0000269|PubMed:9584098}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; AE013599; AAM70824.1; -; Genomic_DNA.
DR EMBL; AF006654; AAB62570.1; -; mRNA.
DR EMBL; AY084145; AAL89883.1; -; mRNA.
DR RefSeq; NP_652724.1; NM_144467.2.
DR AlphaFoldDB; Q9V9A7; -.
DR SMR; Q9V9A7; -.
DR BioGRID; 72857; 2.
DR STRING; 7227.FBpp0085460; -.
DR PaxDb; Q9V9A7; -.
DR PRIDE; Q9V9A7; -.
DR DNASU; 59261; -.
DR EnsemblMetazoa; FBtr0086126; FBpp0085460; FBgn0042083.
DR GeneID; 59261; -.
DR KEGG; dme:Dmel_CG3267; -.
DR UCSC; CG3267-RA; d. melanogaster.
DR CTD; 64087; -.
DR FlyBase; FBgn0042083; Mccc2.
DR VEuPathDB; VectorBase:FBgn0042083; -.
DR eggNOG; KOG0540; Eukaryota.
DR GeneTree; ENSGT00940000155949; -.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; Q9V9A7; -.
DR OMA; AYLPIMS; -.
DR OrthoDB; 632665at2759; -.
DR PhylomeDB; Q9V9A7; -.
DR Reactome; R-DME-196780; Biotin transport and metabolism.
DR Reactome; R-DME-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00363; UER00861.
DR BioGRID-ORCS; 59261; 0 hits in 3 CRISPR screens.
DR ChiTaRS; CG3267; fly.
DR GenomeRNAi; 59261; -.
DR PRO; PR:Q9V9A7; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0042083; Expressed in embryonic/larval muscle system (Drosophila) and 38 other tissues.
DR ExpressionAtlas; Q9V9A7; baseline and differential.
DR Genevisible; Q9V9A7; DM.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; ISS:FlyBase.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:FlyBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0015936; P:coenzyme A metabolic process; ISS:FlyBase.
DR GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
DR GO; GO:0007563; P:regulation of eclosion; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 30..578
FT /note="Probable methylcrotonoyl-CoA carboxylase beta chain,
FT mitochondrial"
FT /id="PRO_0000000297"
FT DOMAIN 48..305
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 321..570
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 48..570
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 355..388
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
FT CONFLICT 50
FT /note="S -> R (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="F -> G (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="H -> N (in Ref. 3; AAL89883)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="L -> V (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="E -> R (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 376..377
FT /note="KL -> NV (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="Missing (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 578 AA; 62648 MW; AF5E2ABBE36B18F0 CRC64;
MIRLNWLFRS SSVLLRSQVR LLHVGDANVL HSEVDKQSAE YKENAREMAS LVGDLRNFTS
QVLKGGGQKA IERHTSRGKL LARERINLLL DKGSPFLELS ALAGHELYGE EVVNSGGIVT
GVGRVCGTEC LVVANDATVK GGSYYPITVK KHLRAQEIAQ ENRLPCIYLV DSGGANLPRQ
ADVFPDKLHF GRIFYNQANM SAQGIPQIAV VMGSCTAGGA YVPAMADESI IVKKQGTIFL
AGPPLVKAAT GEEVSAEDLG GADLHCKTSG VTDHYALDDE HALYLARQIV SNLNLSATNS
YNDQLMHSSQ VNFQTATPPS AVEEPRYDAE ELYGIVGPNL TKSFDVREVI ARIVDGSRFT
EFKKLYGETL VCGFAKLYGH TVGIVGNNGV LFSESALKGA HFIQLCAQRK IPLVFLQNIT
GFMVGRDAEA NGIAKNGAKM VTAVACANVP KFTVIIGGSY GAGNYGMCGR AYSPRFLYMW
PNSRISVMGG TQAANVMAQI TEDQRKRAGK EFSEEEAQKL KAPIVEMFEA EGSPYYSTAR
LWDDGIIDPA NTRQILGLSL KAALNNAGQE TKFGVFRM
