ID Q2U8M9_ASPOR Unreviewed; 597 AA.
AC Q2U8M9;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAE62086.1};
GN ORFNames=AO090701000364 {ECO:0000313|EMBL:BAE62086.1};
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE62086.1, ECO:0000313|Proteomes:UP000006564};
RN [1] {ECO:0000313|EMBL:BAE62086.1, ECO:0000313|Proteomes:UP000006564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007164; BAE62086.1; -; Genomic_DNA.
DR RefSeq; XP_001823219.1; XM_001823167.1.
DR AlphaFoldDB; Q2U8M9; -.
DR STRING; 510516.Q2U8M9; -.
DR EnsemblFungi; BAE62086; BAE62086; AO090701000364.
DR GeneID; 5995276; -.
DR KEGG; aor:AO090701000364; -.
DR VEuPathDB; FungiDB:AO090701000364; -.
DR HOGENOM; CLU_013748_3_3_1; -.
DR OMA; LPGAQIY; -.
DR OrthoDB; 1328249at2759; -.
DR Proteomes; UP000006564; Chromosome 5.
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; 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; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR PANTHER; PTHR18968:SF166; 2-HYDROXYACYL-COA LYASE 2; 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.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000006564};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 14..128
FT /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02776"
FT DOMAIN 205..339
FT /note="Thiamine pyrophosphate enzyme central"
FT /evidence="ECO:0000259|Pfam:PF00205"
FT DOMAIN 406..557
FT /note="Thiamine pyrophosphate enzyme TPP-binding"
FT /evidence="ECO:0000259|Pfam:PF02775"
SQ SEQUENCE 597 AA; 63421 MW; C3EACDE95F06E72E CRC64;
MAGFALNDHN GELNGGDLLA QTLKHLGVEV AFGLHGGHLD AFLQGCEASQ IRLIDTRHET
VAVQAAESYA KFSKKIGVCF ITANSGFSNG IPGLATALAD RSPILCITSS PPTRDAENNS
LQGIIDQVVV SRPLTKFAYR MTNPEDTPRI VKYAMGVALS GAPGPVLLDF PVDVLFTPVH
KPLISWGSVS SPFPYGPGPH TAAIEGTVEL LNAAKRPVII LGTGGNSKEA AESLMKLSET
CHMPIFDTTK CKISFFPSQF ALNGGASSAL ALLPHVGIQR PDLILLLGAR TGMFLGGRSG
AIIPDKDCKL VQVDVDGAEI GRTLPVDLGA ICDVTQFAAG LNRHFETASF QGSVDTKWVD
DVLGLKSLPS PYEQQAEVQP SGRLHPYHAL KHLLTFVPKE SIIILDGGEA PLWAGEMIST
CSPSAIVKSS GGLGFLGNGF GYALGAAVAC PDQTVINLHG DGSAGFHFMD LDTYKRHNLN
IMTIVVNNYC WGMSSNGQDL IYGTKTPTRP VSHLSPVTDY SLVAKALGNA SAKIQSIDDM
SPAFVKLLDQ SGPTCIELVV DDKPIHPITV SMVGQTDEPG MVVVPYYDNV PRAYYKS
//
