ID A0A2T9YUE8_9FUNG Unreviewed; 578 AA.
AC A0A2T9YUE8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Pyruvate decarboxylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BB561_001473 {ECO:0000313|EMBL:PVU95977.1};
OS Smittium simulii.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133385 {ECO:0000313|EMBL:PVU95977.1, ECO:0000313|Proteomes:UP000245383};
RN [1] {ECO:0000313|EMBL:PVU95977.1, ECO:0000313|Proteomes:UP000245383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SWE-8-4 {ECO:0000313|EMBL:PVU95977.1,
RC ECO:0000313|Proteomes:UP000245383};
RX PubMed=29764946;
RA Wang Y., Stata M., Wang W., Stajich J.E., White M.M., Moncalvo J.M.;
RT "Comparative Genomics Reveals the Core Gene Toolbox for the Fungus-Insect
RT Symbiosis.";
RL MBio 9:e00636-e00618(2018).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:PVU95977.1}.
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DR EMBL; MBFR01000043; PVU95977.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T9YUE8; -.
DR STRING; 133385.A0A2T9YUE8; -.
DR Proteomes; UP000245383; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd02004; TPP_BZL_OCoD_HPCL; 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; IPR045025; HACL1-like.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR43710; 2-HYDROXYACYL-COA LYASE; 1.
DR PANTHER; PTHR43710:SF2; 2-HYDROXYACYL-COA LYASE 1; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000245383};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 3..117
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 190..317
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 397..560
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 578 AA; 61820 MW; 671C5AF1A03B9E0C CRC64;
MLTGAQLIAS SLKVQGVSVV FGIVGIPVVE IGEACTAAGI RFIAFRNEQA AGYAASAWGY
LTGTPGVCLV VSGPGLVNAL SGIVNANINK WPLVILGGSC ETDLVGYGAF QELDQVGFCK
PHTKYSAKPN SPEQIPYIIE RGFNHAVNGV PGAVYLDFPA DYINAEINTA SVARSTQFVT
KLVSPLQNAV DSAAQLILSA KAPLIIIGKG SAYAACEDRI LELVDLIQAP FLPTPMGKGV
ISDNHALNAS AARSLALASA DVIVILGARL NWILGFGRQF NKSAKIIHAD VDVNEINSSV
PIEVPLVGHL QCTIQMLVQS ISRQLKELPA GIYTTNNTDQ ATAKREYMEA IATKIAQNKQ
RALELVKNRN VMPMTYYTAF NEIKPLLPPN VVFISEGANT MDIARSFFEF ELPRRRLDAG
TYGTMGVGLG YAIAAQIAYP HERVVAVVGD SAFGFSAMEI ETAVRNKLPL IIIVINNSGI
YFGLSRSQFD GCFHSTPDPN APDSMVTQSM IPTTALLPEV AYHDLAIALG GSGYCARTPT
ELNSALTIAL QTNSNTVLIN CLIDPGAKKK LEFNWMKK
//
