ID C5FVB5_ARTOC Unreviewed; 712 AA.
AC C5FVB5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:EEQ33849.1};
GN ORFNames=MCYG_06668 {ECO:0000313|EMBL:EEQ33849.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ33849.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; DS995706; EEQ33849.1; -; Genomic_DNA.
DR RefSeq; XP_002844704.1; XM_002844658.1.
DR AlphaFoldDB; C5FVB5; -.
DR STRING; 554155.C5FVB5; -.
DR GeneID; 9227102; -.
DR VEuPathDB; FungiDB:MCYG_06668; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_1_1; -.
DR OMA; FVEICSH; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000002035; 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:UP000002035}.
FT DOMAIN 37..485
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 153..351
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 626..704
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 712 AA; 77303 MW; BC5D738870E0C9FB CRC64;
MSFLLRASAS RIPQRALFAA PSLRHSSSTA TGKGTTSLHS ILIANRGEIA LRVGRTAGQH
GIRVTTLYTD PDAHAQHALS SPFAFNLGET SAYLDGDRII EIAKREGCKG IHPGYGFLSE
NAGFAKKCTD AGLIFIGPPP SAIDAMGDKS RSKEIMTAAG VPCVPGYHGT NQDVNFLAAE
AEKIKYPVLI KAVKGGGGKG MRIARSAAEF QDQLKSAKSE AMSSFGDDTM LIEKYIITPR
HIEVQVFADQ HGNSVALGER DCSVQRRHQK VLEESPAPHL PEATRKDLWA KARDAALAVG
YEGAGTVEFI FDNDTGEFFF MEMNTRLQVE HPVTEMVTGQ DLVHWQLLVA EGAPLPLTQE
EVEAKMATMG HAIEARIYAE NPEQNFVPDS GKLIHVRTPQ PTEDVRIDAG FVAGDEVSSH
YDPMISKLIV RGADRTEALR NLSMALEQYE VAGPITNIEF LKRVCKSPDF VAGEVETGYI
EKHREELFAK APVEPELWAQ VALSTFISGT SLSNPVGNTG AGVGFSPGYQ QRQFTFVEAT
APNTPEATPA TVQIHQTGPS SYDVTVNNEK TFSNVTASLS ADGKALTSFF PHTRLDTTVI
RDEDSITAFQ HGRQYRLKVP RAKWMEKALG IKELANSVLA PMPCKILRVE VAEGAVVEKD
QPLVVIESMK METVIRSPIK GVVEKIVHKQ GDICKAGTAL VEFAAEPKAP ES
//