ID A0A2P5IFQ4_9PEZI Unreviewed; 733 AA.
AC A0A2P5IFQ4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 28-JUN-2023, entry version 15.
DE SubName: Full=Methylcrotonoyl-CoA carboxylase subunit alpha {ECO:0000313|EMBL:POS81313.1};
GN ORFNames=DHEL01_v200289 {ECO:0000313|EMBL:POS81313.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS81313.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS81313.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS81313.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-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:POS81313.1}.
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DR EMBL; MAVT02000011; POS81313.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5IFQ4; -.
DR STRING; 158607.A0A2P5IFQ4; -.
DR InParanoid; A0A2P5IFQ4; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000094444; 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:UP000094444}.
FT DOMAIN 37..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 648..723
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT REGION 15..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 733 AA; 80021 MW; 020E18D8A69CC026 CRC64;
MRSIKTAHRR LPLRPASRAF LSTSTSSSQT SNSNVTPITS VIIANRGEIA LRVQRTASKL
GIRTTTLYTD VDRNAQHTTA TPYSLSLPNY LDGDRIIALA RQHGIQALHP GYGFLSENAA
FAQKCHDAGI VFVGPPASAM ADMGDKARSK EIMTAAGVPC VPGYHGTEQA VDALQAHAVQ
IGFPVLLKSV KGGGGKGMRI VDSEADFPAQ LRSARAEARA SFGEGGEVML VEKYVVRPRH
VEVQVFADKL GNCVALGERD CSVQRRHQKI LEESPAPLLD DATRKDLWAK ARTAALAVGY
VGAGTVEFIL DRDTGRFYFM EMNTRLQVEH PVSEMVTGTD LVEWQFRVAA GEALPLTQDE
IEARIEERGA AIEARIYAES PEKDFMPDSG KLVHLVTPTT DEDVRIDAGF IEGDTVSSAY
DGMISKLIVR GKDREAAIRR LELALREYEV VGLSTNIEFL KRLCRSQAFI DGDVETGFIK
KHGDELFKPR QIDNEVFVQA ALGLLTAQLQ SDIPRSGPHG EVLGFGPEST STGERNYVFK
CIDNYSSQEG EVVQAKITQL GKNLFSAAVS RKGQEQPQVF ENLICEPITS SIAQPNHSRT
AVRTFFPLER LDTTVVSDPT NSHKLSIFQH GLKTELLLQQ PSWYDKALGL QDVAASVVAP
MPCKILRNEV SEGESVEKGA PLVVIESMKM ETVIRSPQSG IIKKLAHKEG DICKAGTVLV
VFDEAEEAHN ASS
//
