ID A0A177DJZ9_ALTAL Unreviewed; 593 AA.
AC A0A177DJZ9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thiamin diphosphate-binding protein {ECO:0000313|EMBL:OAG19530.1};
GN ORFNames=CC77DRAFT_1009987 {ECO:0000313|EMBL:OAG19530.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG19530.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG19530.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG19530.1,
RC ECO:0000313|Proteomes:UP000077248};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KV441481; OAG19530.1; -; Genomic_DNA.
DR RefSeq; XP_018384951.1; XM_018523621.1.
DR AlphaFoldDB; A0A177DJZ9; -.
DR STRING; 5599.A0A177DJZ9; -.
DR GeneID; 29109215; -.
DR KEGG; aalt:CC77DRAFT_1009987; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1009987; -.
DR OMA; DMCFPGD; -.
DR OrthoDB; 2291769at2759; -.
DR Proteomes; UP000077248; 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; cd02002; TPP_BFDC; 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; 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:UP000077248};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 5..136
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 208..314
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 414..565
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 593 AA; 64603 MW; 2752CE68734B61E5 CRC64;
MVYTASFAFF EALWEYGVSH VFVNLGSDHP SIIEAIVKGQ NEKKGQFPKI ITCPNEMVAL
SMADGYARLT GKPQCVIVHV DVGTQGLGAA VHNASCGRAP VLIFAGLSPF TIEGEMRGSR
TEYIHWIQDV PDQKQIVAQY CRYTGEIKSG KNVKQMVNRA LSFAMSDPKG PVYLYGAREP
MEEDLTPYKL QMDYWQPVEP AALPPKGVKT IAEALVNAQE PLIITGYSGR NHDAVHELVR
LADNVKGIRV LDTGGCDMCF PANHPAWLGL RYGNDPAIKS ADVILVLDCD VPWINTQCHP
KENAKILHID VDPLKQQMPV FYLNAIQRYR ADSYTSLTQL NEYLESQLKE KLSSQLFSQR
WSALQESHKK KLEGIAGEAK VDENGHFSTP YLCSQLKKLC PNDTIWAIEA VTQTGFVADQ
IQATLPGSWI NCGGGGLGWS GGGALGVKLA TDTEGKKQFV CQIVGDGTYL FSVPGSVYWI
AQRYNIPILT VVLNNKGWNA PRRSMLLVHP DGEGSKVSNE ELNISFAPTP DYSGIAKAAS
GGHIWAAHAS TADELSKLLP EAIKSVLSGT SAVLDAHLEG PEGKYGGGKG RLG
//
