ID A0A0H2S894_9AGAM Unreviewed; 711 AA.
AC A0A0H2S894;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SCHPADRAFT_817148 {ECO:0000313|EMBL:KLO20149.1};
OS Schizopora paradoxa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Hymenochaetales; Schizoporaceae; Schizopora.
OX NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO20149.1, ECO:0000313|Proteomes:UP000053477};
RN [1] {ECO:0000313|EMBL:KLO20149.1, ECO:0000313|Proteomes:UP000053477}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUC8140 {ECO:0000313|EMBL:KLO20149.1,
RC ECO:0000313|Proteomes:UP000053477};
RG DOE Joint Genome Institute;
RA Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT wood degrader in East Asia.";
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};
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DR EMBL; KQ085883; KLO20149.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H2S894; -.
DR STRING; 27342.A0A0H2S894; -.
DR InParanoid; A0A0H2S894; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000053477; 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; 3.30.700.40; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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:UP000053477}.
FT DOMAIN 18..465
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 137..335
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 628..703
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 711 AA; 77802 MW; 34479EDEB4DED267 CRC64;
MLFTGPSSDV LSSERRPLFD KILIANRGEI ACRVIRTAKK LGIKTVAVYS EVDRNALHVL
QADEAYCIGP APSSESYLRV DKIIEICHRT GAQAVHPGYG FLSENAGFAQ RLSDEGITFI
GPSPTSIRSM GSKSESKDIM ISAGVPCVPG YHGSEQSIEK LVEEAEQIGF PVLIKAVMGG
GGKGMRIVHN ASELPDALES AKREAIKSFG DDRVLVEKYI IRPRHVEVQV FGDQHGNVVS
LWERDCSVQR RHQKIIEEAP APGLSTELRS DLCSKAVAAA KAVNYLGAGT VEFILDNDTD
KFYFMEMNTR LQVEHPVTEM ITGQDLVQWQ LEVAVGNSLP LKQTEIPMLG HSFEARIYAE
NPRNNFLPDV GPLLHVSTPT TSPSVRLEEG FRQGHDVEVF YDPLIAKLVV HGRDRTEALR
ILRKALEEYH IVGVSTNVEF LRTLAGNGQF IEGNVETGFI QKYHDDLFPS HPAPSPETLA
QAALHVVLRE NQVGSGPYSP WTSLGPLRFG GDVYERIITF KSEQGSTATH PAVHVKFVRP
GVFDIEVSDP ANTSRTEFRS VTTSRLSSSA LASTFDGRRL RSTIVSEKPP ATGLTGEEKL
HVFHEHSGER TTLVIPAPAW LQARSSALQE AQSQGGIRAP MPSLVVDVRV EIGQTIEAGQ
AVVVLESMKT ETVLRAAVAG VVRSINCKKG EMVEEGRELV LIEAEEDADG K
//
