ID G4U860_NEUT9 Unreviewed; 608 AA.
AC G4U860;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 36.
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:carbon dioxide ligase subunit beta {ECO:0000256|ARBA:ARBA00031237};
GN ORFNames=NEUTE2DRAFT_154810 {ECO:0000313|EMBL:EGZ78393.1};
OS Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ78393.1, ECO:0000313|Proteomes:UP000008513};
RN [1] {ECO:0000313|EMBL:EGZ78393.1, ECO:0000313|Proteomes:UP000008513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT "Massive changes in genome architecture accompany the transition to self-
RT fertility in the filamentous fungus Neurospora tetrasperma.";
RL Genetics 189:55-69(2011).
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 EMBL; GL890999; EGZ78393.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U860; -.
DR STRING; 510952.G4U860; -.
DR eggNOG; KOG0540; Eukaryota.
DR HOGENOM; CLU_018822_0_1_1; -.
DR UniPathway; UPA00363; UER00861.
DR Proteomes; UP000008513; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
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:UP000008513}.
FT DOMAIN 99..356
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50980"
FT DOMAIN 363..596
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
FT REGION 45..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 608 AA; 65825 MW; 891A5351FC12A8B4 CRC64;
MSFSSASRRE VLLFSKQLSR TASTSPRSAS LPLHPRNLGL LLHSNQQQPQ QSHRQQSVLQ
QQRRSVATFT TPHQANAISV LKSDVDTDSP EFKENERLMG EAMARLEELT RKVHQGGPQK
AREKHLLRKK MLPRDRITAL IDPGTTFLEL SPLAGHELYP EADVPAGGII TGVGVVEGVT
CVIVANDSTV KGGTYYPITV KKHLRAQEVA KENNLPCIYL VDSGGANLPH QSDVFPDREH
FGRIFFNQAR MSSQGIPQIA VVMGPCTAGG AYVPAMSDES IIVQEQGHIF LAGPPLVKAA
TGEVVSPEEL GGGAMHSSVS GVTDYLAVDD AHAIVLARRS IANLNWPRGS STGAVTPADF
EQKFEEPLYS ADELLGIAST NLRKPLPIHE VIARIVDGSA FAEFKRDYGT TLVTGFAKIY
GHRVGIVANN GILFSSSALK GAHFIELCAQ RGIPLVFLQN ISGFMVGRDA EREGIAKNGA
KLVTAVACAD VPKFTVVVGG SYGAGNYGMC GRAYSPRFLW MWPNARIGVM GSEQLAKVME
TVGTKADPEL QDRIERESDA VFSSARLWDD GVIPPQHTRR YLGLGLRAAL GGRNEQAPRG
TKFGVFRM
//
