ID F8Q0G9_SERL3 Unreviewed; 628 AA.
AC F8Q0G9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EGN97798.1};
GN ORFNames=SERLA73DRAFT_109025 {ECO:0000313|EMBL:EGN97798.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; GL945481; EGN97798.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q0G9; -.
DR STRING; 936435.F8Q0G9; -.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_4_0_1; -.
DR InParanoid; F8Q0G9; -.
DR OMA; DMCFPGD; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
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; IPR029061; THDP-binding.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF164; PYRUVATE DECARBOXYLASE; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 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.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 3..134
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 459..622
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 628 AA; 67272 MW; 28A989873212D338 CRC64;
MYTTSSLFLN TLAQVGITHA FVNWGSDHPA LLEDLERQRV EKGETEPKIV TCPNEMVALS
AAQGYTQVTG KPAAVIVHVD VGTQALAGAV HNVNRGRAPV LIYAGSSPFS AEGELKGSRN
EWIHWMQDVH DQPAILRQYM RYTAQINSPA NLPHLVRRAL QIATSDPKGP VYLWGRREVM
EQEIDEGLLK VPAPMLKWPS VEPCALSHSA AAIIAAALRQ AVNPLLITSH AGRNTNVFTS
LSALCSLIGM PVFVPCPAVL NTPFSYALYV GVGHLAPGTQ TTLLKDADVI LVLDVELPWI
PMNKDSNGDH ERPKEDARVF VIDGGDPLKE NIGMYHVDAE MVCRADAEVA LGQIVEAIQH
SDSTEGVIIA ESAIVQARTR EMEKMHSEWV AKLDKAESFP TSLTSSIPAY TVPQVISALR
RAVISGTPSG GAHTLMLNES ISNYPLVWSH MRPEVLGGMI GSGGSSLGWA LGASVGAFLG
GKVAEKGPGK QGYELVASIV GDGTFLFGVP ASAFWMARKY QTPFLTVILN NGGWKSPKLS
MLGVYPSGHG SKVLGQQLTV GFGPDMPDYA QIAVAASGGW AWGRKVDAST ISEGKNPKDA
LEEVIAEAVR VVVQEGRCAV IDCVLESI
//