GenomeNet

Database: UniProt
Entry: R1DDE4_EMIHU
LinkDB: R1DDE4_EMIHU
Original site: R1DDE4_EMIHU 
ID   R1DDE4_EMIHU            Unreviewed;       505 AA.
AC   R1DDE4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
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};
DE   Flags: Fragment;
GN   ORFNames=EMIHUDRAFT_450910 {ECO:0000313|EMBL:EOD21074.1},
GN   EMIHUDRAFT_455777 {ECO:0000313|EMBL:EOD33473.1};
OS   Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC   Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC   Noelaerhabdaceae; Emiliania.
OX   NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD33473.1};
RN   [1] {ECO:0000313|EMBL:EOD33473.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD33473.1};
RG   DOE Joint Genome Institute;
RA   Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA   Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA   Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA   Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA   Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA   Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA   Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA   Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA   Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA   Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA   Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA   Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA   Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT   "Genome variability drives Emilianias global distribution.";
RL   Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000013827}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX   PubMed=23760476; DOI=10.1038/nature12221;
RA   Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA   Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA   Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA   Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA   Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA   Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA   Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA   Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA   Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA   Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA   Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA   Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA   Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA   van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA   Wurch L.L.;
RT   "Pan genome of the phytoplankton Emiliania underpins its global
RT   distribution.";
RL   Nature 499:209-213(2013).
RN   [3] {ECO:0000313|EnsemblProtists:EOD21074}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (NOV-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KB865995; EOD21074.1; -; Genomic_DNA.
DR   EMBL; KB864424; EOD33473.1; -; Genomic_DNA.
DR   RefSeq; XP_005773503.1; XM_005773446.1.
DR   RefSeq; XP_005785902.1; XM_005785845.1.
DR   STRING; 2903.R1DDE4; -.
DR   PaxDb; 2903-EOD21074; -.
DR   EnsemblProtists; EOD21074; EOD21074; EMIHUDRAFT_450910.
DR   EnsemblProtists; EOD33473; EOD33473; EMIHUDRAFT_455777.
DR   GeneID; 17266621; -.
DR   GeneID; 17278743; -.
DR   KEGG; ehx:EMIHUDRAFT_450910; -.
DR   KEGG; ehx:EMIHUDRAFT_455777; -.
DR   eggNOG; KOG0540; Eukaryota.
DR   HOGENOM; CLU_018822_0_1_1; -.
DR   OMA; MCNTEEE; -.
DR   UniPathway; UPA00363; UER00861.
DR   Proteomes; UP000013827; 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:UP000013827}.
FT   DOMAIN          45..302
FT                   /note="CoA carboxyltransferase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50980"
FT   DOMAIN          305..505
FT                   /note="CoA carboxyltransferase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50989"
FT   NON_TER         505
FT                   /evidence="ECO:0000313|EMBL:EOD33473.1"
SQ   SEQUENCE   505 AA;  52641 MW;  5151B221E0E6066A CRC64;
     MKTLRSTVVR AAGSRLLSAR AAAASVLDGA VDTSSASFLA NAARMDEQLI EVRSATAVAH
     EGGGPRARAL HTARGKMLAR QRVEALLDPG SPFLELSPLA GHDLYGDEAV PSGGVVTGVG
     SVSGRLVMIV ANDATVKGGT YYPITVKKHL RAQEVAAQNR LPCVYLVDSG GANLPRQADV
     FPDKEHFGRI FFNQARMSAA GVPQLALVCG SCTAGGAYVP AMADEAVIVR GNGTIFLGGP
     PLVKAATGEE VTAEELGGAD VHCKTSGVTD HYALDEPHGL RLARQMVASL PPSQGGSLPR
     ADARPPLFDP AELRGLVPAD SRQPLPMRRV LARVLDGSEL SEFKAEYGST LITGFGSVHG
     YRVGVVANDG VLFSESAQKG AHFVQLCAQR GIPLLFVQNI TGFMVGKAAE HEGIAKHGAK
     LVNAVATANV PKLTVVVGGS FGAGNYGMCG RAYSPRFMFM WPNSRIGVMG GEQAAGVLCQ
     VKEAQAARAG TPLDAPGLEK YRESI
//
DBGET integrated database retrieval system