MCCB_DICDI
ID MCCB_DICDI Reviewed; 588 AA.
AC Q8T2J9; Q55AB9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=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=mccb; Synonyms=mccc2; ORFNames=DDB_G0271960;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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. {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 -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing alpha
CC subunits and six beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AccD/PCCB family. {ECO:0000305}.
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DR EMBL; AAFI02000007; EAL71414.1; -; Genomic_DNA.
DR RefSeq; XP_645342.1; XM_640250.1.
DR AlphaFoldDB; Q8T2J9; -.
DR SMR; Q8T2J9; -.
DR STRING; 44689.DDB0234167; -.
DR PaxDb; Q8T2J9; -.
DR PRIDE; Q8T2J9; -.
DR EnsemblProtists; EAL71414; EAL71414; DDB_G0271960.
DR GeneID; 8618230; -.
DR KEGG; ddi:DDB_G0271960; -.
DR dictyBase; DDB_G0271960; mccB.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_0_1_1; -.
DR InParanoid; Q8T2J9; -.
DR OMA; AYLPIMS; -.
DR PhylomeDB; Q8T2J9; -.
DR Reactome; R-DDI-196780; Biotin transport and metabolism.
DR Reactome; R-DDI-70895; Branched-chain amino acid catabolism.
DR UniPathway; UPA00363; UER00861.
DR PRO; PR:Q8T2J9; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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: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 3: Inferred from homology;
KW ATP-binding; Ligase; Mitochondrion; Nucleotide-binding; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..588
FT /note="Methylcrotonoyl-CoA carboxylase beta chain,
FT mitochondrial"
FT /id="PRO_0000327449"
FT DOMAIN 72..329
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 329..570
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 72..570
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT REGION 366..395
FT /note="Acyl-CoA binding"
FT /evidence="ECO:0000255"
SQ SEQUENCE 588 AA; 64025 MW; 5A5AA09C6D32FDC6 CRC64;
MLKSISLLKN NQILLKNIIN NGRIINNVGE KLSSKSLLKI NYSSSTTDRT FNILDGTIDK
NSAEYKDNLI NMNSTLKQLK ENIEKIKLGG GEKLNQKNIS RGKLLVRERI EALIDVGSPF
LEFSQLAGWG MYGKEEVAAG GIITGIGKIH GVECVIVAND STVKGGTYFP ITVKKHLRAQ
EIAQENNLPC IYLVDSGGAN LPRQADVFPD RDHFGRIFFN QANMSAKRIP QIAVVMGSCT
AGGAYVPAMA DESVIVKGTG TIFLGGPPLV KAATGEIVTS EELGGADLHC RTSGVTDHYA
RDDAEAIAIT RRIVSNLNRK KQPSPVITET EEPLYPTSEL AGIVPSDLKK NFDIRKVIAR
LVDGSRFDEF KELYGTTLIC GFARVHGMPV GIIANNGILF SESAVKGAHF IELCNQRGIP
LVFLQNITGF MVGKTYESKG IAKDGAKMVM AVATAKVPKI TMIIGGSFGA GNYGMCGRSY
SPRFLYMWPN AKISVMGGEQ AASVLAQIQK DNMAKENKQW SPEEENTFKK PISDKFEEEG
SIYYSSARCW DDGVIDPQDS RKVIALSLSA CMNQPINPPS DGFGVFRM
