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Database: UniProt
Entry: U3KCS1_FICAL
LinkDB: U3KCS1_FICAL
Original site: U3KCS1_FICAL 
ID   U3KCS1_FICAL            Unreviewed;       577 AA.
AC   U3KCS1;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=methylcrotonoyl-CoA carboxylase {ECO:0000256|ARBA:ARBA00026116};
DE            EC=6.4.1.4 {ECO:0000256|ARBA:ARBA00026116};
DE   AltName: Full=3-methylcrotonyl-CoA carboxylase 2 {ECO:0000256|ARBA:ARBA00031404};
DE   AltName: Full=3-methylcrotonyl-CoA carboxylase non-biotin-containing subunit {ECO:0000256|ARBA:ARBA00031109};
DE   AltName: Full=3-methylcrotonyl-CoA:carbon dioxide ligase subunit beta {ECO:0000256|ARBA:ARBA00031237};
GN   Name=MCCC2 {ECO:0000313|Ensembl:ENSFALP00000012825.1};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000012825.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000012825.1, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000012825.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00029358};
CC   -!- PATHWAY: Amino-acid degradation; L-leucine degradation; (S)-3-hydroxy-
CC       3-methylglutaryl-CoA from 3-isovaleryl-CoA: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00025711}.
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DR   RefSeq; XP_005061119.1; XM_005061062.1.
DR   STRING; 59894.ENSFALP00000012825; -.
DR   Ensembl; ENSFALT00000012875.2; ENSFALP00000012825.1; ENSFALG00000012282.2.
DR   Ensembl; ENSFALT00000028305.1; ENSFALP00000028832.1; ENSFALG00000012282.2.
DR   Ensembl; ENSFALT00000043383.1; ENSFALP00000030905.1; ENSFALG00000012282.2.
DR   GeneID; 101821035; -.
DR   KEGG; fab:101821035; -.
DR   CTD; 64087; -.
DR   eggNOG; KOG0540; Eukaryota.
DR   GeneTree; ENSGT00940000155949; -.
DR   HOGENOM; CLU_018822_0_1_1; -.
DR   OMA; AYLPIMS; -.
DR   OrthoDB; 5474505at2759; -.
DR   UniPathway; UPA00363; UER00861.
DR   Proteomes; UP000016665; Chromosome Z.
DR   GO; GO:0002169; C:3-methylcrotonyl-CoA carboxylase complex, mitochondrial; IEA:Ensembl.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:Ensembl.
DR   GO; GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR034733; AcCoA_carboxyl_beta.
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; ACETYL, PROPIONYL, PYRUVATE, AND GLUTACONYL CARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22855:SF13; METHYLCROTONOYL-COA CARBOXYLASE BETA CHAIN, MITOCHONDRIAL; 1.
DR   Pfam; PF01039; Carboxyl_trans; 1.
DR   SUPFAM; SSF52096; ClpP/crotonase; 2.
DR   PROSITE; PS50989; COA_CT_CTER; 1.
DR   PROSITE; PS50980; COA_CT_NTER; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT   DOMAIN          63..320
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          320..569
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  62490 MW;  F935527FD54F67AB CRC64;
     MEERSRGAAG RGESPSARAW PSLRAEPSGT GERRGLPRRG CLGAVRSACQ LLLPVRLENY
     ERMKALVTEL QEQAEKIRLG GGEKARKLHT SRGKLLPRER IDKLIDPGSP FLEFSQFAGH
     QLYGNEEVPA GGIITGIGRV SGTECLIVAN DATVKGGTYY PITVKKHLRA QEIAMQNHLP
     CLYLVDSGGA NLPRQAEVFP DRDHFGRIFY NQAVMSSQGI PQIAVVMGSC TAGGAYVPAM
     ADESIIVGKQ GTIFLGGPPL VKAATGEQVS AEDLGGADLH CRKSGVTDHY ALDDNHALHL
     ARKVVRSLNL QKKVDVTIEP SEEPLFPADE IYGIVGDQLK RNFDVKEVIA RIVDGSRFDE
     FKALYGDTLV TGFARIFGYP VGIIGNNGVL FSESAKKGTH FIQLCCQRNI PIVFLQNITG
     FMVGREYEAG GIAKDGAKMV TAVACANVPK ITVIIGGSYG AGNYGMCGRA YSPRFLYMWP
     NARISVMGGE QAATVLATIA KDQKAREGKQ LSEADEAALK EPIIRRFEEE GNPYYSSARL
     WDDGIIDPAD TRLVLGLSLS AALNAPTKKT EFGVFRM
//
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