ID A0A135UHX1_9PEZI Unreviewed; 708 AA.
AC A0A135UHX1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Thiamine pyrophosphate enzyme {ECO:0000313|EMBL:KXH59984.1};
GN ORFNames=CSAL01_11981 {ECO:0000313|EMBL:KXH59984.1};
OS Colletotrichum salicis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH59984.1, ECO:0000313|Proteomes:UP000070121};
RN [1] {ECO:0000313|EMBL:KXH59984.1, ECO:0000313|Proteomes:UP000070121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH59984.1,
RC ECO:0000313|Proteomes:UP000070121};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:KXH59984.1}.
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DR EMBL; JFFI01001443; KXH59984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A135UHX1; -.
DR STRING; 1209931.A0A135UHX1; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000070121; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004737; F:pyruvate decarboxylase activity; IEA:UniProtKB-EC.
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; IPR012000; Thiamin_PyroP_enz_cen_dom.
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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000070121};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 107..239
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 311..417
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 517..702
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
FT REGION 54..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 76258 MW; 13A72B17A258EBF5 CRC64;
MPFRQLPVPM ARCLRSFGPA GGRPGRLVRF NQTLAPSIAV VGGPARQLAG FSSAAPLHRS
GGSTSPSSSH AGAGIKPTTS RPLVKDEFKA TIEQARNLSS KSTEMHTASF AFFEALWDAG
VTHCFVNLGS DHPSIIEAMV KGQRERKGNF PRIITCPNEM VAMSMADGYA RLTGKPQCVI
VHVDVGTQGL GAAVHNASCG RAPILVFAGL SPFTIEGEMR GSRTEYIHWI QDVPDQKQIV
SQYCRYSGEL KTATNVKQMV NRALQFSKSD PQGPVYLCGA REVMEAEVEP YSIRQEDWDP
VELGGLPKNA VNKIAEALAG AKEPLIVTGF GGRDHRFPGA LVELANTVKG LRVVDTGGSD
MCFPADHPGW LGLRFGIEDA VNTADVIVVL DCDVPWINTL CHPKKDAKIF HIDVDPLKQQ
MPVFYIAAQS RYRASSLLSI EQITAHLKGQ YATQLESAEA KEREAKVKES HKQLLAKIEE
KAQPKADGEF GTGHLTRSLK KLCPEDTIWA IEAVTNTIFV HDNLQPTLPG SWINCGGGGL
GWSGGGALGI KLATDFENGG NNKGKFVVQI VGDGTFLFSV PGSVYWIAKR YNIPILTIIL
NNKGEWSINL SGDFETKADM KAGWNAPRRS LLLVHPDGEG SRATNEEINI SFDPAPDYAG
IAKAAAGGDL FAARVDKAAD LDSVLKKAIE TVQGGQPAVL DIKVALGF
//