ID A0A0F8D318_CERFI Unreviewed; 735 AA.
AC A0A0F8D318;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha mitochondrial {ECO:0000313|EMBL:KKF97112.1};
DE EC=6.4.1.4 {ECO:0000313|EMBL:KKF97112.1};
GN Name=MCCC1 {ECO:0000313|EMBL:KKF97112.1};
GN ORFNames=CFO_g526 {ECO:0000313|EMBL:KKF97112.1};
OS Ceratocystis fimbriata f. sp. platani.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Ceratocystis.
OX NCBI_TaxID=88771 {ECO:0000313|EMBL:KKF97112.1, ECO:0000313|Proteomes:UP000034841};
RN [1] {ECO:0000313|EMBL:KKF97112.1, ECO:0000313|Proteomes:UP000034841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFO {ECO:0000313|EMBL:KKF97112.1,
RC ECO:0000313|Proteomes:UP000034841};
RA Belbahri L.;
RT "Genome sequence of Ceratocystis platani, a major pathogen of plane
RT trees.";
RL Submitted (APR-2015) 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:KKF97112.1}.
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DR EMBL; LBBL01000017; KKF97112.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F8D318; -.
DR Proteomes; UP000034841; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004485; F:methylcrotonoyl-CoA carboxylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:KKF97112.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000034841}.
FT DOMAIN 34..484
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 150..350
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 658..733
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 735 AA; 79701 MW; 41A57974B3D87588 CRC64;
MRSLKSQARR LSLHRSYSPA TTASSSSTAP SITPIASLMI ANRGEIALRI HKTAHRLGIQ
TATVYTDPDA SSQHAAVGNY SFNLGPAKGY LDTEKIIGLA KAHGIQALHP GYGFLSENPA
FAARCEQEGI VFVGPPAQAM ADMGHKARSK EIMESSGVPC VPGYHGPQQG EDQLLGHARK
IGFPVLLKSV RGGGGKGMRI VKTESEFLAQ LRSARAEANA SFGDGGEVML VERYIERPRH
VEVQIFADKY GNCVALGERD CSIQRRHQKI LEESPAPHLD ASTRADLWSK ARTAALAVGY
VGAGTVEFIL DKDSGQFFFM EMNTRLQVEH PVSEMVTGTD LVEWQVRIAS GEKLPLTQSD
IEKNISARGA AIEARIYAEK PEEGFMPDSG KLIHLRTPAT NEDVRIDAGF GEGDVVTEAY
DGMIAKLIVR ADDRTTAIQR LDRALAEYEI VGLGTNIEFL KRLCQSPAFV QGDVETGFIE
KHHDELFAAP LYQDEVFVQG ALALLLSAAD EAQTQSFQTL PGGANLGFGG IANPGEADSI
GTRSFSFKVL DVRNESEVTA VVTLYPTGNR MYDVNVTTNA GNHSDTRSYK SLTTSCALSA
ESSAKADVTT YFPQQRITSK VVTQTQTAAS DQTTVVVFQH GKKHELELLS PTWYDAALGI
KKVSGAVVAP MPCKILKVEV GHGQEVKRGD PLIVIESMKM ETVIKAPHDG RVKRVVYQPG
DICKARSILV EFEDD
//
