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Database: UniProt
Entry: I1JF82_SOYBN
LinkDB: I1JF82_SOYBN
Original site: I1JF82_SOYBN 
ID   I1JF82_SOYBN            Unreviewed;       735 AA.
AC   I1JF82;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   ORFNames=GLYMA_02G145300 {ECO:0000313|EMBL:KRH71391.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847 {ECO:0000313|EnsemblPlants:KRH71391};
RN   [1] {ECO:0000313|EMBL:KRH71391.1, ECO:0000313|EnsemblPlants:KRH71391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82 {ECO:0000313|EnsemblPlants:KRH71391};
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH71391.1};
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [2] {ECO:0000313|EnsemblPlants:KRH71391}
RP   IDENTIFICATION.
RC   STRAIN=Williams 82 {ECO:0000313|EnsemblPlants:KRH71391};
RG   EnsemblPlants;
RL   Submitted (FEB-2018) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:KRH71391.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Callus {ECO:0000313|EMBL:KRH71391.1};
RA   Schmutz J., Cannon S., Schlueter J., Ma J., Mitros T., Nelson W., Hyten D.,
RA   Song Q., Thelen J., Cheng J., Xu D., Hellsten U., May G., Yu Y.,
RA   Sakurai T., Umezawa T., Bhattacharyya M., Sandhu D., Valliyodan B.,
RA   Lindquist E., Peto M., Grant D., Shu S., Goodstein D., Barry K.,
RA   Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N., Joshi T.,
RA   Libault M., Sethuraman A., Zhang X., Shinozaki K., Nguyen H., Wing R.,
RA   Cregan P., Specht J., Grimwood J., Rokhsar D., Stacey G., Shoemaker R.,
RA   Jackson S.;
RT   "WGS assembly of Glycine max.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CM000835; KRH71391.1; -; Genomic_DNA.
DR   AlphaFoldDB; I1JF82; -.
DR   SMR; I1JF82; -.
DR   STRING; 3847.I1JF82; -.
DR   EnsemblPlants; KRH71391; KRH71391; GLYMA_02G145300.
DR   Gramene; KRH71391; KRH71391; GLYMA_02G145300.
DR   HOGENOM; CLU_000395_3_1_1; -.
DR   InParanoid; I1JF82; -.
DR   OMA; LVKWQLM; -.
DR   Proteomes; UP000008827; Chromosome 2.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR005481; BC-like_N.
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; IPR016185; PreATP-grasp_dom_sf.
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; PF00289; Biotin_carb_N; 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; SSF52440; PreATP-grasp domain; 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|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000008827}.
FT   DOMAIN          36..482
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          155..353
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          657..733
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   735 AA;  81110 MW;  36FD356C7619B666 CRC64;
     MASLALLRRK LIITRTTLSY SHVRARAFSA GNNKHRIEKI LVANRGEIAC RITRTARRLG
     IQTVAVYSDA DRDSLHVATA DEAIRIGPPP ARLSYLNGAS IVDAAIRSGA QAIHPGYGFL
     SESADFAKLC EESGLTFIGP PASAIRDMGD KSASKRIMGA AGVPLVPGYH GYDQDIEKMK
     LEADRIGYPV LIKPTHGGGG KGMRIVHTPD EFVESFLAAQ REAAASFGVN TILLEKYITR
     PRHIEVQIFG DKHGNVLHLY ERDCSVQRRH QKIIEEAPAP NISADFRAQL GVAAVSAAKA
     VNYYNAGTVE FIVDTVSDEF YFMEMNTRLQ VEHPVTEMIV GQDLVEWQIL VANGEALPLS
     QSQVPLSGHA FEARIYAENV QKGFLPATGV LHHYHVPVSS AVRVETGVKE GDKVSMHYDP
     MIAKLVVWGE NRAAALVKLK DSLSKFQVAG LPTNVNFLQK LANHRAFANG NVETHFIDNY
     KEDLFVDANN SVSVKEAYEA ARLNASLVAA CLIEKEHFIL ARNPPGGSSL LPIWYSSPPF
     RIHHQAKRRM ELEWDNEYGS GSSKIMKLTI TYQPDGRYLI ETEQNGSPVL EVKSTYVKDN
     YFRVEAAGVI NDVNVAVYSK DQIRHIHIWQ GSCHHYFREK LGLELSEDEE SQHKPKVETS
     ANPQGTVVAP MAGLVVKVLV ENKTRVEEGQ PVLVLEAMKM EHVVKAPSSG YVHGLQLMVG
     EQVSDGSVLF SVKVR
//
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