ID A0A1Y1ZSU8_9PLEO Unreviewed; 1325 AA.
AC A0A1Y1ZSU8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0000256|RuleBase:RU003692};
DE EC=1.8.1.4 {ECO:0000256|RuleBase:RU003692};
GN ORFNames=BCR34DRAFT_623909 {ECO:0000313|EMBL:ORY13298.1};
OS Clohesyomyces aquaticus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Lindgomycetaceae; Clohesyomyces.
OX NCBI_TaxID=1231657 {ECO:0000313|EMBL:ORY13298.1, ECO:0000313|Proteomes:UP000193144};
RN [1] {ECO:0000313|EMBL:ORY13298.1, ECO:0000313|Proteomes:UP000193144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115471 {ECO:0000313|EMBL:ORY13298.1,
RC ECO:0000313|Proteomes:UP000193144};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + NAD(+) = H(+) +
CC N(6)-[(R)-lipoyl]-L-lysyl-[protein] + NADH; Xref=Rhea:RHEA:15045,
CC Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10475, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83100; EC=1.8.1.4;
CC Evidence={ECO:0000256|RuleBase:RU003692};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU003692};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|RuleBase:RU003692};
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC {ECO:0000256|RuleBase:RU003692}.
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003692}.
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:ORY13298.1}.
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DR EMBL; MCFA01000043; ORY13298.1; -; Genomic_DNA.
DR STRING; 1231657.A0A1Y1ZSU8; -.
DR OrthoDB; 5473641at2759; -.
DR Proteomes; UP000193144; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR Gene3D; 1.25.40.180; -; 1.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR006258; Lipoamide_DH.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR NCBIfam; TIGR01350; lipoamide_DH; 1.
DR PANTHER; PTHR22912:SF217; DIHYDROLIPOYL DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF02847; MA3; 1.
DR Pfam; PF02854; MIF4G; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR PROSITE; PS51366; MI; 1.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003692};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003692};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003692};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003692};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003692};
KW Reference proteome {ECO:0000313|Proteomes:UP000193144}.
FT DOMAIN 589..724
FT /note="MI"
FT /evidence="ECO:0000259|PROSITE:PS51366"
FT REGION 1..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..263
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1325 AA; 145170 MW; FD056427E2ADAEEB CRC64;
MRQPPFGGPK LPKELRDQFG DPANSHRNGR GRNGPVNRKD RRKAERVEKK TQRKRPKTRN
GGFAPPKASD PSEGEDDGFS DEELPPPKIH PRKQEAPQPL KGILKKSRPE SGLEASSRRL
QSPSPPPRVS RAVKDRLAQD DAEIKALEKR LGIKSKKSKS LDDDGLDDLF ADLGALGSDE
DAPATGPKKR KLAEDDAWLA SKRRKALGEA GPGSSDDDSD TEDSMDIGSE EETELDEDLD
SELDQGLDEN SEEGSDFDSF EEDEPPEPRV RENPYVAPVT STTPQPAKYT PPSLRGPPSS
DAEALTRLRR QIQGLLNKLS EANMLTILRD VEQIYQNNAR GYVNTTFVDL LIGLLTADTT
LPDTFLILHA GFIAAIYKVI GTDFGAQMVE RIVTEFDKHY ETDKIGAGKQ TANLMSLVAE
LYSFQILGSN LIFDYIKLFL GELSEINTEL LLRIIRISGS QLRQDDPTSL KDIVLLLQKQ
VSKVGEDKLP VRTKFMIETI NSLKNNRMKT GMAASTIQLG TLNTRNLKGT EPLRIGLTDI
QDAEKKGKCI APDNKDKNGE QKTLSPEDVE EDGQVDLLQL AREQRMNTDV RRAIFVTIMS
AADFKDAHLR LMKLNLKKAQ EIEIPRVIVH CAGCEKSYNP YYTLIARKFC SEHRLRKCFQ
FALWDVFKSL GEKKDDDDDG VSEDEGDSVN EDLSLRRLVN LGKLYGTLIA NGGLPITSLK
ILNFAYLQPK TRTLVEILLV TAILQSQKGA KEERNEKALL EIFIKTGAEP QMITGLQYFL
KKVVSKSDLG TTRSEKEAIK WACKTANGLL TKVMATSTPV PRAAPRSLLR PVRGAQSTFR
ASNIYFQDRL RRGYASEAEE KDLVIIGGGV AGYVAAIKAG QAGLKVACIE KRGSLGGTCL
NVGCIPSKSL LNNSHLYHQI LHDTKNRGID VGEVTLNLAN MMKAKETSVS GLTKGIEFLF
KKNNVEYIKG TGAFQDEHTI AVNLIDGGEA SVRGKNIFIA TGSEATPFPG LTIDEKKVIT
STGAIALQEV PKKMVVIGGG IIGLEMGSVW SRLGAEVTVV EFLGQIGGPG MDAEIAKMTQ
KMLTKQGMKF KLNTKVTNGD DSSEGVKINV EASKGGKEEV LDADVVLVAI GRRPYTSGLG
LENIGIETDS KGRLEIDQEY RTKIPHIRVI GDVTFGPMLA HKAEEEGVAA VEFLTKGYGH
VNYGAIPSVM YTHPEVAWVG QNEQELKTAG VKYKAGTFPF SANSRAKTNL DTEGIVKILS
DAETDRILGV HIVGPNAGEM IAEGTLAIEY GASSEDIART SHAHPTLSEA FKEAAMATYD
KAIHY
//
