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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//