MCCA_DICDI
ID MCCA_DICDI Reviewed; 699 AA.
AC Q54KE6;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial;
DE Short=MCCase subunit alpha;
DE EC=6.4.1.4;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase 1;
DE AltName: Full=3-methylcrotonyl-CoA carboxylase biotin-containing subunit;
DE AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit alpha;
DE Flags: Precursor;
GN Name=mccA; Synonyms=mccc1; ORFNames=DDB_G0287377;
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=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: Biotin-attachment 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
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}.
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DR EMBL; AAFI02000100; EAL63756.1; -; Genomic_DNA.
DR RefSeq; XP_637277.1; XM_632185.1.
DR AlphaFoldDB; Q54KE6; -.
DR SMR; Q54KE6; -.
DR STRING; 44689.DDB0230065; -.
DR PaxDb; Q54KE6; -.
DR EnsemblProtists; EAL63756; EAL63756; DDB_G0287377.
DR GeneID; 8626108; -.
DR KEGG; ddi:DDB_G0287377; -.
DR dictyBase; DDB_G0287377; mccA.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_1_1; -.
DR InParanoid; Q54KE6; -.
DR OMA; FVEICSH; -.
DR PhylomeDB; Q54KE6; -.
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:Q54KE6; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; ISS:dictyBase.
DR GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin; Ligase; Mitochondrion; Nucleotide-binding;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..699
FT /note="Methylcrotonoyl-CoA carboxylase subunit alpha,
FT mitochondrial"
FT /id="PRO_0000327665"
FT DOMAIN 30..475
FT /note="Biotin carboxylation"
FT DOMAIN 148..345
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 624..699
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT ACT_SITE 320
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 665
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 699 AA; 77089 MW; B1FD14E7E286A96D CRC64;
MFSLGKLVKK DAFFYRYITN VNKDLKIKPI TKILIANRGE IACRVMRTAK SKGVKTVAVY
SEADKNSLHV SMADESYLIG PAAAKESYLC GNKIIDVAKR SGAQAIHPGY GFLSENSDFA
DLCEREGIIF IGPPSDAIKA MGSKSASKDI MIKAGVPTIP GYHGEDQSMS VLKSEAAKIG
YPVLIKAVMG GGGKGMRIVE REEDLEDGVE SSKREATASF GDSRVLVEKY LVHPRHVEIQ
VFADRHGNCV HLFERDCSVQ RRHQKIIEEA PAPHLSEELR KKMGDAAVAA AKAVGYVGAG
TVEFILSADN SFFFMEMNTR LQVEHPITEM ITKQDLVEWQ LKVAESQTLP MEQEQLKIHG
HSFEARIYAE NPDSDFLPGT GKLAHLSTPT PSDTLRVETG VRQGDEVSVY YDPMIAKLVV
WDQDREKALR YLRNALDEYH IIGLNTNISF LKRLSTHPSF MAGEVETGFI PIHRESLMAP
QAPMSDDSLA LAATSLLLKE ITQQKSKEDP NSPWSSLGGF RINHNLKKQV KFNQKDNKVV
VNVEFIGGGG AAANGKHNFK VTLDNGNVVE VLDAKLNQNN ETISAHVNGR FYNNIKSVIV
KDTLTIFNEG QQYQLDIPQD VKPKGADGVL GSLVSPMPGK ITKVMVNVGD MVKKGQPILL
MEAMKMEHTI RSPIDGKVES LPYNVNEIVE DKKTLAVIV
