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Database: UniProt
Entry: Q54KE6
LinkDB: Q54KE6
Original site: Q54KE6 
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   05-DEC-2018, entry version 113.
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; Mycetozoa; Dictyostelids; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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-methylbut-2-enoyl-CoA + ATP + hydrogencarbonate = ADP +
CC         H(+) + phosphate + trans-3-methylglutaconyl-CoA;
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-
CC       hydroxy-3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC   -!- SUBUNIT: Probably a dodecamer composed of six biotin-containing
CC       alpha subunits and six beta subunits. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
DR   EMBL; AAFI02000100; EAL63756.1; -; Genomic_DNA.
DR   RefSeq; XP_637277.1; XM_632185.1.
DR   ProteinModelPortal; Q54KE6; -.
DR   SMR; Q54KE6; -.
DR   STRING; 44689.DDB0230065; -.
DR   PaxDb; Q54KE6; -.
DR   PRIDE; 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   eggNOG; COG4770; LUCA.
DR   InParanoid; Q54KE6; -.
DR   KO; K01968; -.
DR   OMA; DYDPMLA; -.
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   Proteomes; UP000002195; Unassembled WGS sequence.
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   InterPro; IPR011761; ATP-grasp.
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; Complete proteome; Ligase; Mitochondrion;
KW   Nucleotide-binding; Reference proteome; Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion. {ECO:0000255}.
FT   CHAIN         ?    699       Methylcrotonoyl-CoA carboxylase subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000327665.
FT   DOMAIN       30    475       Biotin carboxylation.
FT   DOMAIN      148    345       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   DOMAIN      624    699       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   ACT_SITE    320    320       {ECO:0000250}.
FT   BINDING     144    144       ATP. {ECO:0000250}.
FT   BINDING     228    228       ATP. {ECO:0000250}.
FT   BINDING     263    263       ATP. {ECO:0000250}.
FT   MOD_RES     665    665       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-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
//
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