ID S7QJX1_GLOTA Unreviewed; 814 AA.
AC S7QJX1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=3-methylcrotonyl-CoA carboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=GLOTRDRAFT_134779 {ECO:0000313|EMBL:EPQ60006.1};
OS Gloeophyllum trabeum (strain ATCC 11539 / FP-39264 / Madison 617) (Brown
OS rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Gloeophyllales; Gloeophyllaceae; Gloeophyllum.
OX NCBI_TaxID=670483 {ECO:0000313|EMBL:EPQ60006.1, ECO:0000313|Proteomes:UP000030669};
RN [1] {ECO:0000313|EMBL:EPQ60006.1, ECO:0000313|Proteomes:UP000030669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11539 {ECO:0000313|EMBL:EPQ60006.1,
RC ECO:0000313|Proteomes:UP000030669};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; KB469296; EPQ60006.1; -; Genomic_DNA.
DR RefSeq; XP_007860504.1; XM_007862313.1.
DR AlphaFoldDB; S7QJX1; -.
DR STRING; 670483.S7QJX1; -.
DR GeneID; 19303168; -.
DR KEGG; gtr:GLOTRDRAFT_134779; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_3_1; -.
DR OMA; FINKPKH; -.
DR OrthoDB; 1459320at2759; -.
DR Proteomes; UP000030669; 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; PS00866; CPSASE_1; 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:UP000030669}.
FT DOMAIN 86..570
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 205..403
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 732..808
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 814 AA; 87378 MW; 835E7F2AC6C6557D CRC64;
MKPATRPSAI RRVNVGGGSI QPARAFTNSQ LRPRLPRVSE QNVSLEGRIG MSGLRKSSPF
PGSSTQARAL ATAAEGTVSL RTRKPHFDKI LIANRGEIAC RVIRTAKKLG IKTVAVYSDV
DADSMHVKMA DEAYCIGPAP SAESYLRIEK IIDVCRRSGA QAVHPGYGFL SENAKFAERL
SEEGIVFIGP PASAIVSMGS KSESKNIMIA AGVPCVPGYH GNNQDPDFLL EEAKRIGFPV
LIKATHGGGG KGMRAVDSPS AFSDALASAK RESAKSFGDD TVLIERYITR PRHVEVQVFA
DTQGGVVSLW ERDCSVQRRN QKIIEEAPAP GLSPELRADL SAKAVAAARA VNYVGAGTVE
FIFDNDTQEF YFMEMNTRLQ VEHPVTEMIT GLDLVEWQLE VAAGNPLPLS QSAIPLHGHA
FEARIYAENP RNNFLPDSGR LLYLSTPQPT CAFAPAVVPA LREEEAALYP TLSTFTSTST
SLTGEGAPAV RIEQGFGSGA QIGVFYDPMI AKLVVHGRDR TEALRVLRKA LEEYKVVGVS
TNVEFLRILA SHGAFIDGEV ETGFIPKHFE ELFPNVGEPE PEVLAQAALF AALRTQLRGN
GMSASPWVSL TSRRFGGDTA GRIITLQNEG ENAEPITVHV VPQPGGVFDV TVQTASSQTE
FRGMSARLVS LTELASTVNG QSSNTTIVAQ PPPPNVPPSS SPNTMERLHI FHNGRKSTLV
LPSPKWLLSL GGDVLNAAKG ALRAPMPSLV VEVRVGVGER VEEGQAVVVL ESMKTETVLR
AGVAGVVRAV GCKKGEMVEE GRELVDIEED AEGK
//
