ID N1PGG2_DOTSN Unreviewed; 602 AA.
AC N1PGG2;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EME41477.1};
GN ORFNames=DOTSEDRAFT_73779 {ECO:0000313|EMBL:EME41477.1};
OS Dothistroma septosporum (strain NZE10 / CBS 128990) (Red band needle blight
OS fungus) (Mycosphaerella pini).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Dothistroma.
OX NCBI_TaxID=675120 {ECO:0000313|EMBL:EME41477.1, ECO:0000313|Proteomes:UP000016933};
RN [1] {ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23209441; DOI=10.1371/journal.pgen.1003088;
RA de Wit P.J.G.M., van der Burgt A., Oekmen B., Stergiopoulos I.,
RA Abd-Elsalam K.A., Aerts A.L., Bahkali A.H., Beenen H.G., Chettri P.,
RA Cox M.P., Datema E., de Vries R.P., Dhillon B., Ganley A.R.,
RA Griffiths S.A., Guo Y., Hamelin R.C., Henrissat B., Kabir M.S.,
RA Jashni M.K., Kema G., Klaubauf S., Lapidus A., Levasseur A., Lindquist E.,
RA Mehrabi R., Ohm R.A., Owen T.J., Salamov A., Schwelm A., Schijlen E.,
RA Sun H., van den Burg H.A., van Ham R.C.H.J., Zhang S., Goodwin S.B.,
RA Grigoriev I.V., Collemare J., Bradshaw R.E.;
RT "The genomes of the fungal plant pathogens Cladosporium fulvum and
RT Dothistroma septosporum reveal adaptation to different hosts and lifestyles
RT but also signatures of common ancestry.";
RL PLoS Genet. 8:E1003088-E1003088(2012).
RN [2] {ECO:0000313|EMBL:EME41477.1, ECO:0000313|Proteomes:UP000016933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NZE10 / CBS 128990 {ECO:0000313|Proteomes:UP000016933};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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}.
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DR EMBL; KB446542; EME41477.1; -; Genomic_DNA.
DR AlphaFoldDB; N1PGG2; -.
DR STRING; 675120.N1PGG2; -.
DR EnsemblFungi; EME41477; EME41477; DOTSEDRAFT_73779.
DR eggNOG; KOG1185; Eukaryota.
DR HOGENOM; CLU_013748_3_3_1; -.
DR OMA; PGPYGCL; -.
DR OrthoDB; 2020042at2759; -.
DR Proteomes; UP000016933; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblFungi.
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; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000016933};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 15..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 201..330
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 407..576
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 602 AA; 64152 MW; EA9EE6E52E9C522F CRC64;
MPSGEYAVAG GGTYGAKIIA QALHDLGVKV IFGLPGLPVT DIGQEGLYLG MRFISFRNEQ
AAVYAATAYG YLTGKPGVCI SVGGPGVFHV MAGIPHATAN SWPLLVLSGS SETHNAGKDA
FQEVDAISLI SPLAKFAGRP PSADLIPKFI KDAYRAAWFG RPGPAFVDLP ANLILGTFDV
PRNKLPALTE APLSVAPPKK IQDVASVIKS AKAPLIVIGK GAAYAQAEKQ IIEFVDKTGI
PFVPTPMGKG VVADSHASNF SAARSTALRE SDVILVLGAK LNWILSFGLP PKWSPHAKII
QIDITADELG KNGGHPTLSL VGDVALCVEQ ISRTLGSWKW PGVKDSAFSK SLQAAKDRNE
AKALAKTKSG KVPMPFEKAF EIIKAALNDL SNPSEGDIVY VSEGANAMDI SRSVFTMEHP
RIKLDAGTYA TMGVGLGYCI AAHTAYNLTH EGHAGGSGKK KVVAIEGDSA FGFSAMEVET
MARFQMDVLI FVMNNSGLYR GDTDAEDKWE ERRRNTVEGT TTDGKGLTAW SLGYQTKYEK
IAEMAGGIGI CARTAEELME ATRRGFEAKV PVVVNVIIDP QSDLPMDFSW LDMVPKKKEA
KL
//
