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Database: UniProt
Entry: Q6C6Q2_YARLI
LinkDB: Q6C6Q2_YARLI
Original site: Q6C6Q2_YARLI 
ID   Q6C6Q2_YARLI            Unreviewed;       562 AA.
AC   Q6C6Q2;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   16-AUG-2004, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=YALI0E07315p {ECO:0000313|EMBL:CAG79242.1};
GN   ORFNames=YALI0_E07315g {ECO:0000313|EMBL:CAG79242.1};
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591 {ECO:0000313|EMBL:CAG79242.1, ECO:0000313|Proteomes:UP000001300};
RN   [1] {ECO:0000313|EMBL:CAG79242.1, ECO:0000313|Proteomes:UP000001300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150 {ECO:0000313|Proteomes:UP000001300};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.F., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR   EMBL; CR382131; CAG79242.1; -; Genomic_DNA.
DR   RefSeq; XP_503660.1; XM_503660.1.
DR   AlphaFoldDB; Q6C6Q2; -.
DR   STRING; 284591.Q6C6Q2; -.
DR   EnsemblFungi; CAG79242; CAG79242; YALI0_E07315g.
DR   GeneID; 2912435; -.
DR   KEGG; yli:YALI0E07315g; -.
DR   VEuPathDB; FungiDB:YALI0_E07315g; -.
DR   HOGENOM; CLU_013748_3_3_1; -.
DR   InParanoid; Q6C6Q2; -.
DR   OMA; PGPYGCL; -.
DR   OrthoDB; 2020042at2759; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IBA:GO_Central.
DR   GO; GO:0001561; P:fatty acid alpha-oxidation; IBA:GO_Central.
DR   CDD; cd02004; TPP_BZL_OCoD_HPCL; 1.
DR   CDD; cd07035; TPP_PYR_POX_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR045025; HACL1-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR   PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001300};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          1..116
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          193..323
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          399..536
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   562 AA;  60048 MW;  D536649B6A24A96E CRC64;
     MNGSQVIAES LVQLGVEHIF GIVGIPVIEV ADACIARGIK FIGFRNEQSA SYAASIYGYL
     SGKPGVCLTV GGPGVLHALA GVGNAQSNCF PLLLLAGSVD VHNTHKGGFQ ELDQVAAVTE
     YTKFAARPSS TDALPFLLEK AYRTAYFGRP GATYVDLPAN IIQSKDNDQV SFGVLQRLRN
     VPAPRSAGDP AKIAEAAALI RASKFPLLVI GKGAAYAKAE PTIRRFQEST NIQFLPTPMG
     KGVISDSNPG NMSACRSQAL KNADVVILVG TRLNWILHYG DAPKYSENTK FIHIDVCAEE
     LGNNAGQAEL GILGDASLVI GQLEDVLKGW KSPALAPEIA AKREKNVQNA TKKEADHSVP
     LKYFGVFASI QKTIAEIAKD RKLVIVSEGA NTMDNSRSVF GHVEPRTRLD AGTNATMGVG
     LGYAIAAKAY DPKSLVVAVE GDSAFGFSAI EVETAVRDNL PMVIYVMNNS GIYHGVDPAR
     YTDGQPLPST ALSLDTRYDV LAESLGAKGY FVKNIEELEV ATKSAVQSNR VCVINVIIES
     GKDQKLEFGW MASEKKKEKS KL
//
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