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Database: UniProt
Entry: A0A225AMH1_9EURO
LinkDB: A0A225AMH1_9EURO
Original site: A0A225AMH1_9EURO 
ID   A0A225AMH1_9EURO        Unreviewed;       584 AA.
AC   A0A225AMH1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OKL56136.1};
GN   ORFNames=UA08_08739 {ECO:0000313|EMBL:OKL56136.1};
OS   Talaromyces atroroseus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Trachyspermi.
OX   NCBI_TaxID=1441469 {ECO:0000313|EMBL:OKL56136.1, ECO:0000313|Proteomes:UP000214365};
RN   [1] {ECO:0000313|EMBL:OKL56136.1, ECO:0000313|Proteomes:UP000214365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 11181 {ECO:0000313|EMBL:OKL56136.1,
RC   ECO:0000313|Proteomes:UP000214365};
RA   Rasmussen K.B., Rasmussen S., Petersen B., Sicheritz-Ponten T.,
RA   Mortensen U.H., Thrane U.;
RT   "Talaromyces atroroseus IBT 11181 draft genome.";
RL   Submitted (JUN-2015) 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:OKL56136.1}.
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DR   EMBL; LFMY01000016; OKL56136.1; -; Genomic_DNA.
DR   RefSeq; XP_020116257.1; XM_020263636.1.
DR   AlphaFoldDB; A0A225AMH1; -.
DR   STRING; 1441469.A0A225AMH1; -.
DR   GeneID; 31008495; -.
DR   OrthoDB; 2089851at2759; -.
DR   Proteomes; UP000214365; Unassembled WGS sequence.
DR   GO; GO:0003984; F:acetolactate synthase activity; IEA:InterPro.
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   GO; GO:0034077; P:butanediol metabolic process; 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; IPR012782; Acetolactate_synth_catblc.
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   NCBIfam; TIGR02418; acolac_catab; 1.
DR   PANTHER; PTHR18968:SF129; ACETOLACTATE SYNTHASE; 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:UP000214365};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT   DOMAIN          21..134
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          213..347
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          413..564
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   584 AA;  63783 MW;  0710EB14E69332B0 CRC64;
     MALVRNYRAT IFPAETMSNR NLAHVIVDSL ANAGVKIVFG IPGAKVDGVF DALRDHPSIK
     LIVCRHEQNA AFMAAAVGRL TGLPGVCLVT SGPGTSNLVT GLATATTEGD PVLAIAGTVS
     RLQAARHTHQ SLDVNKVLEG VCKSVIQVGV EDQVSEVIAN AFRQARRFPQ GATAVALPMD
     IIKSTSVGVP PFPALSFESP GYGSSNAKLG KIAVDKLLGS KYPVILLGMR SADPSVVHAV
     RRMIMNHTLP VVETFQAAGA ISEDLLNRYY GRVGLFRNQP GDKILARADL IITVGYDPYE
     YDAETWNVDN PTTIHNIIHV DYTDARVSQH YMPQVELVGN PADIIDEMAS SIQAFKPKFW
     SGAEDALENI RQEIDKWQST ATANIILDGP VQPTHFVYQL RHYLPKDTVV AVDVGTVYIY
     MMRYFQIYSP RHLLCSNGQQ TLGVGLPWAI AASLTQEPKP CSKKVVSISG DGGFMFSSQE
     LATAVQQKCN ITHFIWNDSA YNMVEFQEEA KYGRSSGIKL GGIDFVKFAE AFEGAKGYRV
     TTTGELKSVM KEALEFQGVA VVDVRIDYSK SHELMKNIIP KDYR
//
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