ID A0A397HA23_9EURO Unreviewed; 1554 AA.
AC A0A397HA23;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
GN ORFNames=CDV56_106433 {ECO:0000313|EMBL:RHZ58524.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ58524.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ58524.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ58524.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|RuleBase:RU361139}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|RuleBase:RU361139};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU361139};
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:RHZ58524.1}.
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DR EMBL; NKHU02000067; RHZ58524.1; -; Genomic_DNA.
DR STRING; 41047.A0A397HA23; -.
DR VEuPathDB; FungiDB:CDV56_106433; -.
DR OrthoDB; 1833413at2759; -.
DR Proteomes; UP000215305; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.30.70.930; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR029756; MTH1187/YkoF-like.
DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR002767; Thiamine_BP.
DR NCBIfam; TIGR00106; MTH1187 family thiamine-binding protein; 1.
DR NCBIfam; TIGR03182; PDH_E1_alph_y; 1.
DR PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1.
DR Pfam; PF00676; E1_dh; 1.
DR Pfam; PF13489; Methyltransf_23; 1.
DR Pfam; PF01910; Thiamine_BP; 1.
DR SUPFAM; SSF89957; MTH1187/YkoF-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361139};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU361139};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 78..371
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT DOMAIN 402..485
FT /note="Thiamine-binding protein"
FT /evidence="ECO:0000259|Pfam:PF01910"
FT REGION 890..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1554 AA; 176989 MW; 770348BDC0FBD2F0 CRC64;
MLSRNLRLKE SLPWVSSTLF CVKRRFLAQV VNVPNIPTED DKPFDVPISE DSFETYHFDH
PPYTVGTTKR QLKDLYRDML MIRRMELAAD KLYKEKKIRG FCHLSTGQEA VAVGIENGIS
KEDKLITAYR SHGFTFTRGA SIKSIIGELL GRQDGISHGK GGSMHMFCES FFGGNGIVGA
HVPVGAGIAF AQQYNDSDNV TIDVYGDGAA NQGQVHEAFN MAKLWNLPVL FGCENNQYGM
GTSAERASAM TDYYKRGLYI PGLRVNGMDV LAVMAAVKHG KEFIRAGNGP LVYEFVTYRY
AGHSMSDPGV AYRTREELKA ERAKDPVSTF RGKLIDWGVL TEDEAKTIDK NVREKVNHEV
AEAEKMPEPE PRLDVLFQDI YVRGSEPGQR RGPLATPARC TADFSLIPIG TQNASFSQQI
ADIQRLLTQA SQQTGLKYQL NPTGTTVEGP WDQVVQVIGF AHTLIHQEGV PRIQTDIRIT
TSDTQSLTAS VTDYPTENGR RYHKYHEGSY VYPNDEQELD RLDMQHHMIK LVNDGRLFFA
PIHSPKRILD IGTGSGIWPI EMASIFPEAE ITGTDLSPVQ PTEVPDNVHF LVDDATEEDW
LWDADHFDLI HTAHMIGSFP SFKDVLRKGF KHLKPGGYME CHEFDPKLKC DDGTMPPENP
DGFCEYALHD WVDLNVRSSQ VADPPRQFRI AHRIARWMKE VGFVDVQERI SKVPTNPWSD
DPHLRTIGTW NETNWLEALS GWSYKPLLAL GWSKPEIEVF LVNVRRSIQN RDVHSYMDFY
VVTGGHSSIA LECPRCLMSL GRHAYRHAIQ PSSTHLIDYV WISEELLAST FRRFATSQRR
YESRVPGPLE ARRRLAKRRN TALAGIAGSG PLEDIACLFG RNGREHMKWT DRQERDVHPE
AHEGSPLYPL SPPEPPLPFY SENIDPSEFN TLSGLPGFPD AAHRVSRGQA LEEFLKSRPS
VTAIGIFMRQ LNFDLQREPA YSRLILKHLL PRSVYNEVAM KKVVEFLDDP YLNTRGAGNY
LCALKHILST AAIFGKQRVF DAVIRSLELG LLHPNELQDI IKTISNVKLK RSHEFTARNS
RFLIRFHREM WDAIGRCDIY RHKDLGKDLV DTWLSILCER KTYDDVILAK DMILATQDPT
SSDSQWVPML IARWLKISAE SRHSTNRHYL KELLGYFHPT ATSKFIIRTT EYLVSTKTDC
LLEWQRRLSE LDKLTSVVSS QTWVDVRAQH TTESLGSTQE TKSTLSFRHQ IILRIWTLRS
LSKYLPQGPL WRRDPRVTDS HITHLFTIYE STLYKGGYED LLSSLMKEIH ALGIPSNGLL
MSVVELKAAK RMTRTQRRTL EKLETTKVSF AEMFSDIHAY NATNTHFFST YEKMARQIDI
TDPSFVKHAI ETARDGNIQR IWTLIRLFRC HTPLKIAISS FWPPVPDPSE KALVRYNPEP
RTALCPDPHL AVEMIHLFAV SLACSRNISP RRAFTLVHWL YDFLMSHNAH VKPSLVRAMY
HAGVLRFRRA GLNVAPTQYA YILDRVKEIE TPEMVQALME PPRVGESRKR SDSV
//
