ID A0A2B7ZEY9_9EURO Unreviewed; 726 AA.
AC A0A2B7ZEY9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 28-JUN-2023, entry version 14.
DE SubName: Full=3-methylcrotonyl-CoA carboxylase alpha subunit {ECO:0000313|EMBL:PGH31753.1};
GN ORFNames=GX50_05476 {ECO:0000313|EMBL:PGH31753.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH31753.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH31753.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH31753.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) 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:PGH31753.1}.
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DR EMBL; PDND01000116; PGH31753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZEY9; -.
DR STRING; 73230.A0A2B7ZEY9; -.
DR VEuPathDB; FungiDB:EMCG_01079; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000226031; 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:UP000226031}.
FT DOMAIN 42..490
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 158..356
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 638..714
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 726 AA; 78877 MW; 31FDDB40ADB1C19A CRC64;
MSFISRLPST TSRLGTRVAV LKSTATAVRA NSSLSGAPEN KALNSILIAN RGEIALRVGR
TASQHGIRVT TLYTDPDARA QHALSSPFAF NLGETSAYLD GDRIIEIAKK EGCQGIHPGY
GFLSENSAFA QKCTQAGLVF IGPPPKAIEA MGDKSRSKEI MTAAGVPCVP GYHGENQNMD
FLEAEAEKIK FPVLIKAVKG GGGKGMRIAS TKETFRDQLI SAKSEAMNSF GNDTMLVEKY
VTTPRHIEVQ VFADKHGNCV ALGERDCSIQ RRHQKILEES PAPHLPEATR KDIWDKARAA
ALAVGYEGAG TVEFIFDNDT GEFFFMEMNT RLQVEHPVTE MVTGQDLVHW QILVAEGAPL
PLTQDEIEAI MATKGHAIEA RIYAENPDQG FVPDSGRLLH VRTPTATEDV RIDAGFVAGD
EVSSHYDPMI SKLIVRGSNR TEALRNLTVA LEQYEVAGPI TNIEFLKRVC KSPDFVAGNV
ETGYIDKHRA ELFAKEPVED ELLAQVALSC LLSDSNGMKT ATGPGGAAVG FSPAYQQRQF
AFVEAAVQTP SEASGGAAPY NVHIQQTGEI TFNIVVNGTS FENVKVQQQQ QESNVVTSFF
PHTRLDTTVI RDEDTITAFQ RGRQYRLKIP RAKWMEKALG IKDTANSVLA PMPCKILRVE
VAEGATVVKD QPLVVIESMK METVIRSPQD GKIEKIVHKA GDICKAGTAL VEFAEAASDA
EKKTSS
//
