ID S3D8H0_GLAL2 Unreviewed; 560 AA.
AC S3D8H0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Thiamin diphosphate-binding fold (THDP-binding) {ECO:0000313|EMBL:EPE28281.1};
GN ORFNames=GLAREA_09401 {ECO:0000313|EMBL:EPE28281.1};
OS Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE28281.1, ECO:0000313|Proteomes:UP000016922};
RN [1] {ECO:0000313|EMBL:EPE28281.1, ECO:0000313|Proteomes:UP000016922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT the fungus Glarea lozoyensis.";
RL BMC Genomics 14:339-339(2013).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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DR EMBL; KE145368; EPE28281.1; -; Genomic_DNA.
DR RefSeq; XP_008084189.1; XM_008085998.1.
DR AlphaFoldDB; S3D8H0; -.
DR STRING; 1116229.S3D8H0; -.
DR GeneID; 19468449; -.
DR KEGG; glz:GLAREA_09401; -.
DR eggNOG; KOG4166; Eukaryota.
DR HOGENOM; CLU_013748_3_2_1; -.
DR OMA; ANWYARH; -.
DR OrthoDB; 2089851at2759; -.
DR Proteomes; UP000016922; 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:UP000016922};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 7..118
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 196..323
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 391..540
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 560 AA; 60839 MW; DB7BE400DF3CC1B6 CRC64;
MSSDEAKVAS IIVDSLYNAG VRLVFGIPGA KIDAIFDTLS DHPEIHLVVC RHEQNAAMMA
QAVGRITGTP GVCIATSGPG AGNLTTGLLT ATTEGDPVVA LVGSVPRAMS SKHTHQSMAA
LDVLSPVSKK AVNVDVEDQA AETILAAFRN ASTSPRGASV VSIPMDVAAG KSSIKAFPSE
AFPSPPLGPA PKASLEKVSR MIEEARLPVL FLGMRASSIK VVTAVRQFLE KHPMPVVETF
QAAGAIPKEQ RHLFFGRVGL FRNQTGDRLL AKSDLILTVG YDPTEYNANQ WNPSGDLKII
HMDYTACDYE QYYRPAVELL GSLVENMTYL KDSLKSVTNA SSSDFCKGLT HDFFAWQSRK
ELRRESGLIH PLHFISLLQN NVSIDTTVIS DVGTVYIWMM RFFFSYKPRT LLCSNGQQTL
GIGLPWAIGA SLIQSPPCSQ KVVSMSGDGG FMFSSQELST AVLQGCNITH FIWNDEAYNM
VEFQEEMKYG RSSGIKLGGV DFAKFAESFG AKGFKINDSS ELESVMKEAL AHKGVALVDV
KIDYTDVREL AKELIKEDFN
//
