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Database: UniProt
Entry: X0YDV3_9ZZZZ
LinkDB: X0YDV3_9ZZZZ
Original site: X0YDV3_9ZZZZ 
ID   X0YDV3_9ZZZZ            Unreviewed;       367 AA.
AC   X0YDV3;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Dihydrolipoyl dehydrogenase {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=S01H4_13124 {ECO:0000313|EMBL:GAG54079.1};
OS   marine sediment metagenome.
OC   unclassified sequences; metagenomes; ecological metagenomes.
OX   NCBI_TaxID=412755 {ECO:0000313|EMBL:GAG54079.1};
RN   [1] {ECO:0000313|EMBL:GAG54079.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Expedition CK06-06 {ECO:0000313|EMBL:GAG54079.1};
RX   PubMed=24624126; DOI=10.3389/fmicb.2014.00080;
RA   Kawai M., Futagami T., Toyoda A., Takaki Y., Nishi S., Hori S., Arai W.,
RA   Tsubouchi T., Morono Y., Uchiyama I., Ito T., Fujiyama A., Inagaki F.,
RA   Takami H.;
RT   "High frequency of phylogenetically diverse reductive dehalogenase-
RT   homologous genes in deep subseafloor sedimentary metagenomes.";
RL   Front. Microbiol. 5:80-80(2014).
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:GAG54079.1}.
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DR   EMBL; BART01005792; GAG54079.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0YDV3; -.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   PANTHER; PTHR22912:SF151; DIHYDROLIPOYL DEHYDROGENASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR22912; DISULFIDE OXIDOREDUCTASE; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
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.
PE   4: Predicted;
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          3..227
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          247..352
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:GAG54079.1"
SQ   SEQUENCE   367 AA;  38562 MW;  2C7520C1B01AB3A4 CRC64;
     RKGLTGLIQS HKVKILKGRA IVAARKQVKI ETDFAATEIQ ADKIILATGS EPIEIPAVPF
     DSQTVISSKE ALALQQIPES MVIVGGGIIG CEMACVYAAV GTKVTIVEAL SRLIPMEDEW
     VGRLMAREFK KLGIDSLTSQ KVTSVNKAGG LAKVTLESGQ TIGAEKVLVS VGRRPVADKE
     TVQALNLEMS GPVIKVNEKM QTNVPGLYAV GDAVGTTYSA HGAFAEAEVA AVNATGGDGK
     IADYSLVPRV VYTFPEIASV GKTEEACKSE GLDVSVGRSF FKANGRSAAH NETVGEIRVV
     KDNSTKKIIG VTMVGAEAAE LIAAARALIG STEKITEISF PHPTVSEVLK EAVEDAFGLS
     LHNPPKA
//
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