ID A0A364LCU4_9EURO Unreviewed; 952 AA.
AC A0A364LCU4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=methylisocitrate lyase {ECO:0000256|ARBA:ARBA00012260};
DE EC=4.1.3.30 {ECO:0000256|ARBA:ARBA00012260};
GN ORFNames=BHQ10_009646 {ECO:0000313|EMBL:RAO73634.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO73634.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO73634.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO73634.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000256|RuleBase:RU003932}.
CC -!- SIMILARITY: Belongs to the isocitrate lyase/PEP mutase superfamily.
CC Isocitrate lyase family. {ECO:0000256|ARBA:ARBA00005704}.
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:RAO73634.1}.
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DR EMBL; MIKG01000025; RAO73634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364LCU4; -.
DR STRING; 1196081.A0A364LCU4; -.
DR OrthoDB; 1052588at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0004451; F:isocitrate lyase activity; IEA:InterPro.
DR GO; GO:0046421; F:methylisocitrate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 1.20.120.1240; Dynamin, middle domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR006254; Isocitrate_lyase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR PANTHER; PTHR11566; DYNAMIN; 1.
DR PANTHER; PTHR11566:SF21; DYNAMIN-1-LIKE PROTEIN; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR Pfam; PF00463; ICL; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU003932};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003932};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363}.
FT DOMAIN 194..483
FT /note="Dynamin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51718"
FT DOMAIN 865..952
FT /note="GED"
FT /evidence="ECO:0000259|PROSITE:PS51388"
FT REGION 713..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 952 AA; 105812 MW; 4F94DEA46390A1D8 CRC64;
MAILEIDLDA KQAAFEKEVD EVEAWWKIPQ HAGLKRAPTF PDAVYVSGAI YGTTRVMEPG
IDHADYPWDT VPKIIDQIHH SQMWNDQRQR HLRLSRPKEE RAQMAHVAYM APIIEDSDTG
FGGSTSTIKM ATAFVEVGVA MIHVNDLASG MKRFTIGQAG FGLRQFSMAS LGDDLLVTVN
KLQDLVFNTI GNDSLDLPQI VVVGSQSSGK SSVLENIVGR DFLPRGSGIV TRRPLILQLI
NVSDEEDDSN DAAVNIPHTA NSVAAHGEWA EFHHLPGRKF EDFAQVKQEI ENETARIAGS
NKGINRQPIN LKIFSPHVLN LTLVDLPGLT KVPIGDQPSD IEKQTRTLIS EYIAKPNSII
LAVSPANVDL VNSEALKLAR HVDPMGRRTI GVLTKLDLMD HGTNALDILS GRVYPLKLGF
IGVVNRSQQD IQSGKSLSEA LKAEADFFRH HPAYRNMAIR CGTQFLAKTL NSTLMAHIRD
RLPDIKARLN TLMGQTQQEL ASYGNKQFSG KEHRGSLILQ LMTRFASSFI SSIDGTSSEI
STKELCGGAR IYYIFNSVFG HSLETIDPTH NLTVYDIRTA IRNSTGPRPS LFVPELAFDL
LVKPQIKLLE IPSQRCVELV YEELIKICHT CGSQELSRFP RLQGKLIEVV SDLLRERLGP
CSNYVESLIA IQRAYINTNH PNFLGAAAAM SSVVQNKQEQ EKKAILAEER KKREKRRLKE
VAETNGVTEE DEEHAESRSR NLPIRGAAAG SRTMSPHVET GMNGSPPVFG AANTARDSFL
NYFFGKDGMP SSGPLPQPTQ AGQGRRVGHT IEPSISQSIR RSEARSPVIP QEDYSAPVSD
YGRDIAQFPT ENVEPNLTDR EIMETELIRR LISSYFNIVR ETIADQVPKA VMHLLVNHSK
DVVQNRLVSE LYKEELFGDL LYEDDGIKAE REKCERLLET YKEAAKIVGE VL
//