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Database: UniProt
Entry: A0A1S3V5Y0_VIGRR
LinkDB: A0A1S3V5Y0_VIGRR
Original site: A0A1S3V5Y0_VIGRR 
ID   A0A1S3V5Y0_VIGRR        Unreviewed;       736 AA.
AC   A0A1S3V5Y0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial isoform X2 {ECO:0000313|RefSeq:XP_014513758.1};
GN   Name=LOC106772100 {ECO:0000313|RefSeq:XP_014513758.1};
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
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; Vigna.
OX   NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014513758.1};
RN   [1] {ECO:0000313|RefSeq:XP_014513758.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_014513758.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   RefSeq; XP_014513758.1; XM_014658272.2.
DR   AlphaFoldDB; A0A1S3V5Y0; -.
DR   GeneID; 106772100; -.
DR   OrthoDB; 1129179at2759; -.
DR   Proteomes; UP000087766; Chromosome 8.
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: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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000087766}.
FT   DOMAIN          37..483
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          156..354
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          658..734
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   736 AA;  81007 MW;  32A4E7D2A6CE0C22 CRC64;
     MASLALIRRK IIITRTTLSH WHVCTRAFSN ADSNNNRIEK ILVANRGEIA CRIMRTARRL
     GIQTVAVYSD ADRDSLHVAS ADEAIRIGPP PARLSYLNGT TIVDAAIRSG AQAIHPGYGF
     LSESAVFAKL CEDSGLTFIG PPASAIRDMG DKSASKRIMG AAGVPLVPGY HGDDQDIERM
     KLEADKIGYP VLIKPTHGGG GKGMRIVHSP EEFVESFLAA QREAAASFGV NTILLEKYIT
     RPRHIEVQIF GDKHGNVLHL NERDCSVQRR HQKIIEEAPA PNISADFRAH LGQAAVSAAK
     AVNYYSAGTV EFIVDTVSDE FYFMEMNTRL QVEHPVTEMI VGQDLVEWQI LVANGEALPL
     NQSQVPISGH AFEARIYAEN VQKGFLPATG VLHHYHVPVS SEVRVETGVK QGDTVSMHYD
     PMIAKLVVWG DNRASALVKL KDSLSKFQVA GLPTNVSFIL KLANHGAFAN GNVETHFIDN
     YKEDLFGDGN NSVSDKEAYE AARHNASLVA ACLIEKEHFV SSRNPPGGGS LLPIWYSSPP
     FRVHHQAKRK MELEWENEYD SGSSKTMKLT ITCQPAGRYL IETEENGSPV LDVKASYVKD
     RHFRVEAGGV INDVNVAVYS KDQTRHIHIW QGSHHHYFRE KLGLDLSEDG ELQHKPKVET
     SANPRGTVVA PMAGLVVKVL VENKTRVEEG QPVLVLEAMK MEHVVKAPSS GYVHELQVTV
     GEQVSDGSVL FRVKDQ
//
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