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Database: UniProt
Entry: A0A0F8XH77_9EURO
LinkDB: A0A0F8XH77_9EURO
Original site: A0A0F8XH77_9EURO 
ID   A0A0F8XH77_9EURO        Unreviewed;      3312 AA.
AC   A0A0F8XH77;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Pyruvate decarboxylase {ECO:0000256|ARBA:ARBA00014422};
DE            EC=4.1.1.1 {ECO:0000256|ARBA:ARBA00013202};
GN   ORFNames=ARAM_005024 {ECO:0000313|EMBL:KKK22942.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK22942.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK22942.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK22942.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
RL   Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2-oxocarboxylate + H(+) = an aldehyde + CO2;
CC         Xref=Rhea:RHEA:11628, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:35179; EC=4.1.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001041};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family.
CC       {ECO:0000256|ARBA:ARBA00007812}.
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:KKK22942.1}.
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DR   EMBL; JZBS01001391; KKK22942.1; -; Genomic_DNA.
DR   STRING; 308745.A0A0F8XH77; -.
DR   OrthoDB; 1331544at2759; -.
DR   Proteomes; UP000034291; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016757; F:glycosyltransferase 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   CDD; cd02005; TPP_PDC_IPDC; 1.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 1.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR001296; Glyco_trans_1.
DR   InterPro; IPR012110; PDC/IPDC-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   InterPro; IPR047214; TPP_PDC_IPDC.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF11; PYRUVATE DECARBOXYLASE; 1.
DR   Pfam; PF00534; Glycos_transf_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   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034291};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        803..832
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        844..863
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        892..911
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        917..937
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        949..967
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        973..990
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1227..1248
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1254..1273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1285..1304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1310..1330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1719..1737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2470..2629
FT                   /note="Glycosyl transferase family 1"
FT                   /evidence="ECO:0000259|Pfam:PF00534"
FT   DOMAIN          2762..2847
FT                   /note="Thiamine pyrophosphate enzyme N-terminal TPP-
FT                   binding"
FT                   /evidence="ECO:0000259|Pfam:PF02776"
FT   DOMAIN          2934..3047
FT                   /note="Thiamine pyrophosphate enzyme central"
FT                   /evidence="ECO:0000259|Pfam:PF00205"
FT   DOMAIN          3131..3279
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   3312 AA;  374103 MW;  EA73077837E0E5B0 CRC64;
     MLYLIGRTVY QHWRTRHELS EVPTAIVRYI ERLKAETQKL SPERPELTEP KTFGVYLGSF
     SNPPTEDQAR LLSQWDTVVL DPLQYGVLDA LARSYTATHV LARLDVRQVI SSEPSSHNED
     VIRAICTLTE TLVTYLKRPE DRQSPFTGVL LADCHDHFQP VVLNEVVQFI NALGLDVWLE
     LSPPNYISER QSRDIDMARI RGVVYRNGTI LPNGDRRNYF QMAAMRTVMR VVAAQKPIGG
     STLAMWDAVD DSVEITHDVL HRSSKWCNYN SAMSWIAPQA ALTDARIASG KTIVQEPIGA
     MMWLKGADAL EAHDIWRKNE KVSPTSSHGN DNLYDSLQYL VPNLKQKLAL YPPQEKPAAD
     GQVFVVDGLQ WPSLNEPLVA NPFSRSPDGD EYTGFGCFQI GLDCTAKDIA DLLQAQRHIR
     DLELSDKLKV EELRRIAKQL KELRDSQLPG LEGAKAAQEL CDLLFICDGT DNDPVRVYSG
     LHSGFRTGME TQIWGMAEQQ PGVGVLNIYL SGKAEDRTGT ILHTYMSSRG YSRFQCFMAE
     VSLATANGTL SEKWQLPERI VNDLQQLTPT EALLWLRRLS LTLCQECADL TAKVRACCEY
     QLMQVQSLAQ FRTLSSSEYL SGKISPEEIV SSRLAWYRDQ GCWAPDEAAS KALFMEIDAR
     LPQILISSDA TTLGQLEKVM YKVMQPGKID ASADMLALAV FCAFRRLALD EIYLEVLDRN
     PLPNRHTVQA ACFAEMYALG ARCDMFFDMT PKLLGKIIAA RYQAYYKVHQ PPRREEIFTE
     LPTAYASMDI DLDPKGDQFK VPFYYRITFL GIFAFPALID ITMLTTVGRG LYLTTFMSDI
     DKTLATTALM IALLVCGGFG SWISSGGTYY LYAMAFPAMG MFVMTRFIAG LAVAFAAGII
     AMIAIGCVKG FAAGVLFFLY FFFLSTYLMV LSVLSIYQLP GFEFQSGRTV IITCIPILFI
     SPIVTLWVNH DSVIYLCVLG VFLTSLLLGA RRVIAQWNTW YLHIPRVTDG EVVNWYINNK
     ISPDSAEAKD VATSSVPRKA LVESVQKERK RPFWSKATAD PFVRKMAEGY SATMFLLVWY
     CRYSRTKMPL PYSPTWNLQL KAAVDTMGDM QKGLKLHSAF LHWRHTGADV WCGILYFVIA
     LMDKWTALFT GEALVGLSTA SSSEFRLSVG FGLGYYLAGA VILDAVSQPL WTAAHKRTSE
     AVSSLDSLRV VTTNNYKMRK ALYFKNLTKF FFLHIWGTAV TLALMWTFED SRKATIMYLA
     YIGAYSGLLW YQYNRIFTGP EAARCLALGS IVGLITGIVL HVAIPPFTWS SVIGLSAGTW
     TAAIYSLIMA NVGLPQFKRK AAAADKLSND LTVDPQVSYT SSSLEPYLDL SQTTLTQTFD
     NIDALAEDLR YRLDPSSHPG SEVKEILLSN CGSKKSALVR AAFPEAEKLL HDVVRLWQSG
     QTVIEFVSAE HLLHKEQRIR AVSRRTGDQL LIFVIIGPGL VGQDWTTNIR RNCRTIAEAI
     IQATAEARLG YSQDHSMMAE LLVAEHRNDF ELAVPEGIKY QLERSPAECA RVANHGRRTF
     LRHLLLGIDC DLEWDNLPET ARSFLVRRCS GKPGRVTAEE LRWLQDRVGA QDLQDVGEYV
     ARYNLGVAMS TSVNYFAQRW MEHDDYPDYP VFMDSTYEKP IHSLLPPPIS TNLSFSEALR
     LSFTRVIQTL KTCLKFVVIS LVADPEYQRE LNYIMRGQPL FFAWPVTILL NTIWSYVKFL
     QRIIFPFVLL HGRKNVSELY KNTKGWKTVI EKDRIVIDSL SGVTTCFFRP QPDGSPRLYQ
     YLGNHKQEPT DQAQLIAINT YTDKIVLRRR EEYKGQKLVN DYTYEYAEGG KRFRGKKLPI
     QRQCTAGELE GQVVQYDESG YIISGSAMQG VNPVHFKYGF RKNAKFDDEL LRAEYVFPHI
     QIKVAWCMPP PTRPERLDKW IPYPRVSEAT FIQDSDVHHA KWTYDHKFHP DIATTLNGEP
     VPTPAMIHED WFHVLDKPTK GSFLHDNPLF FFRSIKTNFI TRFLGLNVKC RPIPTSRART
     HLWKTWKGSK EFDAVTTTWL DELLLRSERL LRPYWLNRDF GRLDAAGDYL DAQVDTILAR
     VDIDPEVSSW TPSAFKISDL YSFGIGGDAR INTRTLSTQL QDTDTQLHVL AMDTATWPNE
     PGGVSACRRD MVNDLKGIRW HIISENANDY GVPKFQIERN VQSLTVLPQW GLDFLNPTHG
     VFQNSLDSAV VERSYDTRDE DIEKHFLPIL TKLVRCARTT NLTRQHIEEA TNALVDLNTY
     FVSGRSWNDV WMSDTVKRTW RELWLSENVE DAAPVSEWWD VEHPTLLQLD TALDMWHRYL
     FIFSIPVPER IPDVFQVSHH FTGATYGVLC KAKRKCALHV WDHCVSFREM TVFLSSAVSF
     DSTFVNTTLI SLGHLACVLI EHHADVVLPC AEYFNPGWEV ELGTAEGALQ HRRAFSRKID
     PVVNGITNME KYKPIEAIKT KTPTVVMLSH IRYVKDIKTA IMATDLIVNK WGFTDYRLHI
     YGDMERAPAY ASECQEVIAS KGLREHVVLK GLGNPSVVLQ DAWLFMNSSI SEGLPLAMGE
     AALTGAPVVC TDVGASFCVV TDRATGKKFS EVVAPNDYDS LARAQLRVLA LLENWSPFAE
     DKEGEVVPKL EFRPTPEQVQ AISQRMYDKA EQRRRFGMLG RSNVLNSFSS HRYLREHEQM
     LWLGKYQSHS YIARSAVASS NSSGVLVKEK KTGSQIYINL PNTPNSVEDL MPPTSWRAQR
     DYNLRLLDYV APSRLHWVGN CNELNAGYAA DGYSRIKGIG ALVTTFGVGE LSAVNAIAGA
     YAERAPVVHI VGTPLRESQE SRALIHHTFS DGEYGRFDRM QEHITVAQSI LTDHRTAPAE
     IDRVLRECLL HSRPVRITIP DDMVALRVPT ITLETKLRVP LPVHQPQIEE KALRAVLDRI
     YNAKSPMILV DGESRSARIL DEVDYLVKST EWPTFTSGFG KSLIDESLPN VYGVFTPPRK
     EFVDSCDLVL CFGPHFSNTN TFIFQTLPTD PEATVLVNHA SVQVGGEIFR DLPANYFLPQ
     LIGQLDLSKI AKPTPKLVHP KSVERPTGSN TDLVTHNSGF WSRISSFFRE GDIILAETGT
     AGYGANEFFL PPKTRLFKPV TWLSIGYMLP ATLGASLAQR DLIARSEYYD LLEARTILFI
     GDGSFQLTTQ ELATIIHKKL NVIIFLLNND GYTIERCIHG RNQVYNDITP WRYLKAPEFY
     GAPTEGEYAA HTWQVRTWGD LEKALTDEKM LNGKGVRMVE VFMEKLDAPL PLLGVLDMQI
     QRERERETAA GQ
//
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