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Database: UniProt
Entry: E9GFK7_DAPPU
LinkDB: E9GFK7_DAPPU
Original site: E9GFK7_DAPPU 
ID   E9GFK7_DAPPU            Unreviewed;       553 AA.
AC   E9GFK7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
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   ORFNames=DAPPUDRAFT_303340 {ECO:0000313|EMBL:EFX81653.1};
OS   Daphnia pulex (Water flea).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC   Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX   NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX81653.1, ECO:0000313|Proteomes:UP000000305};
RN   [1] {ECO:0000313|EMBL:EFX81653.1, ECO:0000313|Proteomes:UP000000305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21292972; DOI=10.1126/science.1197761;
RA   Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA   Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA   Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA   Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA   Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA   Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA   Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA   Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA   Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA   Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA   Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA   Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT   "The ecoresponsive genome of Daphnia pulex.";
RL   Science 331:555-561(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; GL732542; EFX81653.1; -; Genomic_DNA.
DR   AlphaFoldDB; E9GFK7; -.
DR   STRING; 6669.E9GFK7; -.
DR   EnsemblMetazoa; EFX81653; EFX81653; DAPPUDRAFT_303340.
DR   KEGG; dpx:DAPPUDRAFT_303340; -.
DR   eggNOG; KOG0540; Eukaryota.
DR   HOGENOM; CLU_018822_0_1_1; -.
DR   InParanoid; E9GFK7; -.
DR   OMA; AYLPIMS; -.
DR   UniPathway; UPA00363; UER00861.
DR   Proteomes; UP000000305; Unassembled WGS sequence.
DR   GO; GO:1905202; C:methylcrotonoyl-CoA carboxylase complex; IBA:GO_Central.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0006552; P:leucine catabolic process; IBA:GO_Central.
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:UP000000305}.
FT   DOMAIN          39..296
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          296..545
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
SQ   SEQUENCE   553 AA;  59825 MW;  D22547A2F24BDE30 CRC64;
     MKRLVPVSSR NYYANDNVVS IGTDQDRNSD TFQDNYNRMA VLVSQLKANI QRVQEGGGAK
     ATQRHKSRGK LLARERVEAL IDPSSPFLEF SQLAGKDLYG SDEVPAGGVI TGIGRIMGNE
     CVIVANDATV KGGSYYPITV KKHLRAQEIA EQNCLPCVYL VDSGGANLPH QAEIFPDREH
     FGRIFYNQAN MSAKGISQIA VVLGSCTAGG AYVPAMADES IIVRKQGTIF LAGPPLVKAA
     TGEEISAEEL GGADLHCSKS GVTDHYAVDD LHALHLARRA VGNLNLVKKP DISVAPPEEP
     LYPADDIYGI VGDNVKKNYD IREVIARIVD ASRFDEFKAK YGETLVTGFA RIHGYPVGII
     ANNGVLFAES SMKGAHFVEL CCQRHIPLIF LQNITGFMVG REAEAGGIAK HGAKLVTAVA
     CAQVPKLTVL VGGSYGAGNY GMCGRAYSPR FLYMWPNSRI SVMGGEQAAG VLAQISQEQR
     KREGKQWTAE EEKALKDPIL KKYDVEGSPY YSSARLWDDG VIDPADTRKV LALSLSAALN
     APIPSTKFGI FRM
//
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