ID A0A061DPH8_THECC Unreviewed; 591 AA.
AC A0A061DPH8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Methylcrotonyl-CoA carboxylase alpha chai isoform 2 {ECO:0000313|EMBL:EOX94684.1};
GN ORFNames=TCM_004300 {ECO:0000313|EMBL:EOX94684.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX94684.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX94684.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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DR EMBL; CM001879; EOX94684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061DPH8; -.
DR EnsemblPlants; EOX94684; EOX94684; TCM_004300.
DR Gramene; EOX94684; EOX94684; TCM_004300.
DR Proteomes; UP000026915; Chromosome 1.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
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; IPR045774; MCCA_BT_dom.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF19331; MCCA_BT; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 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; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 1..336
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 8..206
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 514..590
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 591 AA; 65436 MW; EE70D37FD57386DB CRC64;
MGDKSASKRI MGAAGVPLVP GYHGSEQDIE IMKLEADKIG YPILIKPTHG GGGKGMRIVH
SQKDFIDSFL GAQREAAASF GINTILLEKY ITQPRHIEVQ IFGDKYGNVL HLYERDCSVQ
RRHQKIIEEA PAPCVTDEFR SHLGQAAVSA AKAVGYHNAG TVEFIVDTIT GQFYFMEMNT
RLQVEHPVTE MIVGQDLVEW QIRVANGEPL PISQVQVPLS GHSFEARIYA ENVPKGFLPA
TGVLRHYHPV PVSSTVRVET GVEQGDVVSM HYDPMIAKLV VWGENRSAAL VKLKDCLSKF
QVAGVPTNIN FLQKLANHRA FEEGDVETHF IEHHKDDLFV DPNNKEISEE AYDAARLSAN
LVAACLCEEE HSTLKESHPG GPSLLSIWYA HSPFRVNHHA QSTMELEWEN GYDSSSSKPL
MLAITYQRDG NYLIQHIQIG ENSAHSLEVR ASHLGNNSFR VEADGVTMHV SLAVYIKDKM
KHVHIWHGPH HHHFRQKLGL ELSDEDETQH KTSFETTSHP PGTVVAPMAG LVVKVLVEDG
AKVEEGQPVL VLEAMKMEHV VKATSGGYVQ GLKVTAGQQV SDGSVLFRVK E
//
