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Database: UniProt
Entry: A0A3M9YH86_9PEZI
LinkDB: A0A3M9YH86_9PEZI
Original site: A0A3M9YH86_9PEZI 
ID   A0A3M9YH86_9PEZI        Unreviewed;       727 AA.
AC   A0A3M9YH86;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   13-SEP-2023, entry version 12.
DE   RecName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial {ECO:0008006|Google:ProtNLM};
GN   ORFNames=D7B24_000650 {ECO:0000313|EMBL:RNJ59933.1};
OS   Verticillium nonalfalfae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ59933.1, ECO:0000313|Proteomes:UP000267145};
RN   [1] {ECO:0000313|EMBL:RNJ59933.1, ECO:0000313|Proteomes:UP000267145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ59933.1,
RC   ECO:0000313|Proteomes:UP000267145};
RA   Stajich J.E., Kasson M.T.;
RT   "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RNJ59933.1}.
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DR   EMBL; RBVV01000011; RNJ59933.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9YH86; -.
DR   STRING; 1051616.A0A3M9YH86; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000267145; Unassembled WGS sequence.
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; 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; 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   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; PS50968; BIOTINYL_LIPOYL; 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}.
FT   DOMAIN          35..485
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          151..351
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          643..718
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   727 AA;  78953 MW;  30F5437FF8A2AE68 CRC64;
     MRSMKAKHRL ARPLPRLLST AATGVSASAA PQITPITSLL IANRGEIALR IHKTADRLGI
     RTTTLYTDPD ASSQHAACSP HSLSLGNPKA YLDGDRIISL AKQHGIQALH PGYGFLSENP
     AFASRCEKEG IVFVGPPAKA MHDMGDKARS KEIMTAAGVP CVPGYHGADQ EEAQLLQHAR
     EVRFPVLLKS VKGGGGKGMR IVLTEDEFPA QLRSARLEAK ASFGDGGEVM LVEKYIVRPR
     HVEVQVFADK HGNCVALGER DCSVQRRHQK ILEESPAPCL DEATRLDLWD KARKAASAVD
     YVGAGTVEFI LDRDTGEFYF MEMNTRLQVE HPVSEMVTGT DLVEWQLNIA AGEKLPMTQE
     EISEAISQRG AAIEARIYAE SPEKGFMPDS GKLVHLTTPA TDPDVRIDAG FVQGDTVSEA
     YDGMIAKLIV RGRDRETAIR RLELALRDYE VVGLSTNIEF LKRMCRSPAF IEGDVETGFI
     EKWKDELFAP RVITDEVFVQ AALGSLTAQL ASEAPHGGSL GFGAPNTATE RSFALKVLDA
     YSKQDGEVVQ VTVSQTSPGM FSATVTRKGA EPEVIEKIAC TSSTPKSLAT KLTTFFPGER
     IHSTVVRTTP NATETQDSKV VVFQHGVRTE LALLPPKWFE KALGLKEIAA SVVAPMPCKV
     LRNEVAEDEV VKKGAPLVVI ESMKMETVIR SPQDGVVKKL AHKEGDICKA GTVLVLFEEE
     AAANEAS
//
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