ID M8A8Q5_TRIUA Unreviewed; 525 AA.
AC M8A8Q5;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:EMS56869.1};
GN ORFNames=TRIUR3_11383 {ECO:0000313|EMBL:EMS56869.1};
OS Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS56869.1};
RN [1] {ECO:0000313|EMBL:EMS56869.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23535596; DOI=10.1038/nature11997;
RA Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA Wang D., Zhang A., Wang J.;
RT "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL Nature 496:87-90(2013).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR000350-3};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR000350-3};
CC -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00007532,
CC ECO:0000256|RuleBase:RU003691}.
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DR EMBL; KD152767; EMS56869.1; -; Genomic_DNA.
DR AlphaFoldDB; M8A8Q5; -.
DR STRING; 4572.M8A8Q5; -.
DR eggNOG; KOG1335; Eukaryota.
DR OMA; EHHLKSM; -.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016668; F:oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor; IEA:InterPro.
DR Gene3D; 3.30.390.30; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
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; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR22912:SF204; DIHYDROLIPOYL DEHYDROGENASE; 1.
DR PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 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|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003691};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU003691}.
FT DOMAIN 25..374
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 393..504
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 495
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 49
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 144..146
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 181..188
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 240
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 313
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 365..368
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 40..45
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 525 AA; 56263 MW; 71A02599CCF5EAD2 CRC64;
MNMTSGTAKS VKETIIPAGI ILFPGLKTAI IEGDVVGGTC VNRGCVPSKA LLAVSGRMRE
LHDEHHMKSL GLQVSSTGYD RQAVADHANN LASKIRSNLT NSMKAMGVDI LTGFGKIVGK
QRVRYGKVGF PEKEITAKNI IIATGSVPFV PKGIEIDGKT VFTSDHALKL ESVPDWIAIV
GSGYIGLEFS DVYTALGSEI LTHIQLQKVL EDSVRYCSKM FGPNAAYSYT ILIEQVTFVE
ALDQLMPGFD PEIAKLAQRV LINTRKIDYH TGVFASKITP AKDGKPVLIE LIDAKTKEHK
ETLEVDAALI ATGRAPFTSG LGLENINVVT QRGFIPVDER MQVTDADGNV VPNLFCIGDA
NGKLMLAHAA SAQGISVVEQ ISGRDHILNH LSIPAACFTH PEISMVGLTE PQAREKADNE
GFEVSVVKTS FKANTKALAE NEGDGIAKMI YRPDTGEILG VHILGLHAAD LIHEASNAIA
LGTRLQELKL AVHAHPTLSE VLDELFKAAK VNSGVSHSVN EPVAA
//
