ID A0A074VPA2_9PEZI Unreviewed; 711 AA.
AC A0A074VPA2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE RecName: Full=3-methylcrotonyl-CoA carboxylase subunit alpha {ECO:0008006|Google:ProtNLM};
GN ORFNames=M437DRAFT_85219 {ECO:0000313|EMBL:KEQ62323.1};
OS Aureobasidium melanogenum CBS 110374.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043003 {ECO:0000313|EMBL:KEQ62323.1, ECO:0000313|Proteomes:UP000030672};
RN [1] {ECO:0000313|EMBL:KEQ62323.1, ECO:0000313|Proteomes:UP000030672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110374 {ECO:0000313|EMBL:KEQ62323.1,
RC ECO:0000313|Proteomes:UP000030672};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KL584835; KEQ62323.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074VPA2; -.
DR STRING; 1043003.A0A074VPA2; -.
DR HOGENOM; CLU_000395_3_1_1; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000030672; 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:UP000030672}.
FT DOMAIN 32..480
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 148..346
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 625..703
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 711 AA; 78083 MW; 799B43D6BEB81529 CRC64;
MFRHTRGHRG LIPAVTKRLK TTTTTQGPER QPLQSILIAN RGEIALRVGK TAAQYGIRTT
TLYTDPDAHS QHALSSPFAV NLSDPSQYLN GDRIIQTARD HGCQAIHPGY GFLSENAAFA
KKCTEAGLKF IGPPWKAIEA MGDKSRSKDI MTSAGVPCIP GYHGTNQDPN FLKDQAAQIG
YPVLLKAVKG GGGKGMRISR SPDDFLDQLA SAKSEAMSSF SDDVMLVEKY ITTPRHIEVQ
VFADKHGNCV ALGERDCSIQ RRHQKILEES PAPHLDEALR QDLWDKARSA ALAVAYEGAG
TVEFIFDNVT GEFFFMEMNT RLQVEHPVTE MVTGEDLVHW QIIVAEGGKL PLTQEEVHER
IKTRGHAIEA RIYAENPDMN FVPDSGKLLH LRTPEITETV RIDAGFAVGD EVTSHYDPMI
AKLIIQGPDR HAALQKMKTA LEEYEIAGPI TNIEFVKRMC VSPKFVAGEV ETGYIEKNKE
ELFRRVEILH ETWTQAAIGL YIGEQGLSGN DSILSSQTIG FNTGLSGPRT FDLVEIPADG
NSSSASSITA HVQHIGPHTF SVSVGDQQAI QVTSKLDPTT NILQSFYPHT RLETRLIRDP
DTNTLILFQQ GRQYRLQLSV PKWAEKALGL KDVANSVLAP MPCKVLRVEV EEGASVMKNQ
ALVVIESMKM ETVIRAPHDG VIAKVVHKAG DLCKAGTALV EFAGEEGDKA A
//
