ID C5E2G8_LACTC Unreviewed; 443 AA.
AC C5E2G8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=KLTH0H04840p {ECO:0000313|EMBL:CAR30229.1};
GN OrderedLocusNames=KLTH0H04840g {ECO:0000313|EMBL:CAR30229.1};
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR30229.1, ECO:0000313|Proteomes:UP000002036};
RN [1] {ECO:0000313|EMBL:CAR30229.1, ECO:0000313|Proteomes:UP000002036}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC {ECO:0000313|Proteomes:UP000002036};
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000256|ARBA:ARBA00010701}.
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DR EMBL; CU928180; CAR30229.1; -; Genomic_DNA.
DR RefSeq; XP_002556091.1; XM_002556045.1.
DR AlphaFoldDB; C5E2G8; -.
DR STRING; 559295.C5E2G8; -.
DR ESTHER; lactc-c5e2g8; Acidic_Lipase.
DR GeneID; 8294405; -.
DR KEGG; lth:KLTH0H04840g; -.
DR eggNOG; KOG2624; Eukaryota.
DR HOGENOM; CLU_010974_5_0_1; -.
DR InParanoid; C5E2G8; -.
DR OMA; GYPYEKY; -.
DR OrthoDB; 5474043at2759; -.
DR Proteomes; UP000002036; Chromosome H.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR025483; Lipase_euk.
DR PANTHER; PTHR11005; LYSOSOMAL ACID LIPASE-RELATED; 1.
DR PANTHER; PTHR11005:SF103; STEROL ESTERASE TGL1; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF000862; Steryl_ester_lip; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 106..408
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 201
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 374
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
FT ACT_SITE 403
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR000862-1"
SQ SEQUENCE 443 AA; 51361 MW; F78250CB96ACA615 CRC64;
MCGRMESLWN FCLSLCLRIP MWIYNHCILP LICVLPFFQK YKTFNYSYHN RLVKEVVHAN
DILDIAMAHG FDVQEHLVRT QDGYLLTVHR VLGKKSEVYR SQAKKPVVYF HHGLLTNSEL
FLLGQTSDKC LPFLLVERGY DVWLGNNRGN KYSRKHINLS SRSAKFWDFS LDEYAIFDIP
NTISYILNLT GLEKLTYIGF SQGSSQAFAA FSINPQLRDK IQLFVGLSPA MIPRSLSHPV
AKFLVTCPPE LLYFIFGTRA ILPSVVFWQR LFGPINYMKI VDWSLVYLFN WKSEHISSAQ
KQVGYTHMFS PSSVKSVAHW FQIIHNKRFQ MFQEDISKIY SSVPSLHRKL HRCAPFPVQV
IENMPMMLLY GDQDILIDME TTKQNLVRNL SDLTLVELPG YEHMDTLWAE NVVEEVFNPI
LKKIDQIHAE KPYQNGLEVT ASA
//
