ID A0A067TCC6_GALM3 Unreviewed; 661 AA.
AC A0A067TCC6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Thiamine pyrophosphate enzyme TPP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=GALMADRAFT_245691 {ECO:0000313|EMBL:KDR77534.1};
OS Galerina marginata (strain CBS 339.88).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Strophariaceae; Galerina.
OX NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR77534.1, ECO:0000313|Proteomes:UP000027222};
RN [1] {ECO:0000313|Proteomes:UP000027222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA Hibbett D.S., Grigoriev I.V.;
RT "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT white-rot/brown-rot paradigm for wood decay fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812}.
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DR EMBL; KL142376; KDR77534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067TCC6; -.
DR STRING; 685588.A0A067TCC6; -.
DR HOGENOM; CLU_013748_4_0_1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000027222; 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:UP000027222}.
FT DOMAIN 7..131
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 475..656
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 661 AA; 70667 MW; 30ECBF4DA6DB78B4 CRC64;
MPTSTYTTST LFLRTLARAG ITHAFVNWGS DHPALLEDLE RQRVEARAKG ETLDEGGTEP
RIVTCPNEMV ALSAAQGFAQ VTGKPAAVIV HVDVGTQALA GAVHNVDRSR TPVLIYAGAS
AISQEGEHKG SRNEWIMWIQ DIPDQPAIVR QYMRHTAQIG SAKTVDKTVK RALQIANSDP
KGPVYLWARR EVMEEEVDIA AVEAITNTTG WPTIEPTALS PSATARIADA LLKASSPLII
TSNIGRSPSA VPALISLASL LSIPVLSSCP PCVNLPFSHP SYIGVTFLAP DTHWEKLQGV
DVILVLECDL PWIPGNEKPQ EDTRVFVVDG GDPLKSNVGH WHVDAEMICR ADGGIASKQI
EDALRGMGVR PAGERWELDA SLDGLALEEK ANFRKEVLEK NHARLVSQLD EAEMSPSTVQ
SITAGEPPDI VRYSVANIIG ALRRSFNALT PSKGANILVL NESISNYPAV WGHLRPETLG
SVISSGGSSL GWALGAAVGA SLGARTIGAD DGVPGGRGKG YDLIVAVVGD GSFMFGVPSS
AYWMARRYET PFLTIVLNNG GWKSPKLSML GVHPVGHGSR ASGAELSVGF GPDTPDFLQI
AVAASAGWAW GAKVGGHMPR SVCENRKERP LRELQEVMEK AVKIVLEEKR CAVVECVLMS
I
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