ID A0A0D1XEG9_9PEZI Unreviewed; 708 AA.
AC A0A0D1XEG9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV09_07925 {ECO:0000313|EMBL:KIW00571.1};
OS Verruconis gallopava.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW00571.1, ECO:0000313|Proteomes:UP000053259};
RN [1] {ECO:0000313|EMBL:KIW00571.1, ECO:0000313|Proteomes:UP000053259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW00571.1,
RC ECO:0000313|Proteomes:UP000053259};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Ochroconis gallopava CBS43764.";
RL Submitted (JAN-2015) 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; KN847562; KIW00571.1; -; Genomic_DNA.
DR RefSeq; XP_016210440.1; XM_016361758.1.
DR AlphaFoldDB; A0A0D1XEG9; -.
DR STRING; 253628.A0A0D1XEG9; -.
DR GeneID; 27315898; -.
DR VEuPathDB; FungiDB:PV09_07925; -.
DR HOGENOM; CLU_000395_3_3_1; -.
DR InParanoid; A0A0D1XEG9; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000053259; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053259}.
FT DOMAIN 34..482
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 150..348
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 626..701
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 708 AA; 77828 MW; 72057FCA149EEF12 CRC64;
MMLRRGPRLP RSLRAFPASF RKLSTVPKAG ETKSLSSILI ANRGEIALRV NRTAADYGIR
TTTIYTNPDA NSQHALSSPF TVNLGEPSAY LDGDRIIQVA KEQGCQAIHP GYGFLSENPS
FARKCTEAGL TFIGPPWEAI EAMGSKSRSK DIMNAAGVPC IPGYHGENQD PEYLKQQAAN
IGYPVLLKAV KGGGGKGMRI VQTPAEFMDQ LASAKSEARN SFGDEVMLVE KYITKPRHIE
VQVFADKHGN CVALGERDCS IQRRHQKILE ESPAPHLQED IRQDLWEKAR AAALAVGYEG
AGTVEFIFDN DTNEFFFMEM NTRLQVEHPV TEMVTGEDLV RWQFIVAEGG ELPLTQEQIH
DRIKERGHAI EARIYAENPD MNFMPDSGKL LHMKLPATNA DVRIDAGFVA GDEVSSHYDP
MIAKLIVRGP TREAALQKMR AALESYEIAG PVTNIEFLKR CCVSPAFVAG DVETGYIQKY
KEELFERKPV PEEAWAQAAI GLLFEETSVQ NASMTNSLLG PTFQSRAFHL TELASDGKGA
PQSTTVEITE KPSPAAGTSR VFSVKINNKT FDSVTVTGNA TKFSSSFPHT RISTTLIRSD
DTVTLFHLGA QIRLKLSPAP WMQKALGVRD VANSVLAPMP CKVLRVDVKP GDSVKKDQPL
VVIESMKMET VIRSPVDGVV RRVVHNAGDM CKAGTALVEF EEQEEHAS
//
