ID A0A0J6YUT5_9BACT Unreviewed; 459 AA.
AC A0A0J6YUT5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 28-JUN-2023, entry version 32.
DE SubName: Full=Dihydrolipoyl dehydrogenase {ECO:0000313|EMBL:KMP11049.1};
GN ORFNames=UZ36_05660 {ECO:0000313|EMBL:KMP11049.1};
OS Candidatus Nitromaritima sp. SCGC AAA799-C22.
OC Bacteria; Nitrospinae/Tectomicrobia group; Nitrospinota; Nitrospinia;
OC Nitrospinales; Nitrospinaceae; Candidatus Nitromaritima.
OX NCBI_TaxID=1628279 {ECO:0000313|EMBL:KMP11049.1, ECO:0000313|Proteomes:UP000036407};
RN [1] {ECO:0000313|EMBL:KMP11049.1, ECO:0000313|Proteomes:UP000036407}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC_AAA799_C22 {ECO:0000313|EMBL:KMP11049.1};
RA Ngugi D.K., Blom J., Stepanauskas R., Stingl U.;
RT "Diversification and niche adaptations of Nitrospina-like bacteria in the
RT poly-extreme interfaces of the Atlantis II Deep brine from the Red Sea.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KMP11049.1}.
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DR EMBL; JZKJ01000030; KMP11049.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YUT5; -.
DR PATRIC; fig|1628279.3.peg.884; -.
DR Proteomes; UP000036407; Unassembled WGS sequence.
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; 2.
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; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF4; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE RCLA-RELATED; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PIRSF; PIRSF000350; Mercury_reductase_MerA; 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.
DR PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; NAD {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};
KW Reference proteome {ECO:0000313|Proteomes:UP000036407}.
FT DOMAIN 3..318
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 341..445
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 437
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 136..138
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 173..180
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 263
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 303
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 459 AA; 49462 MW; 8B57C80165E3F62B CRC64;
MDFDVVVIGG GSAGYAAANT AQSAGARVGI VDKGPLGGLC ILRGCMPTKT ILRSSDIIAL
MRRAREFGLS ADNPRADLSA INDRKNRLIK EFADYRIEQL KAPRFTLLEE AAAFISPSEL
KVGGQTLTAK HFIIATGSTI ADFPVAGLAE SGYVTSDDIL KTRTAPGSMI VLGAGPVAVE
LAQFFCRIGT RTTLIQRSGH ILSKGDEDLA RPVEARFREE GMEVFTGTKL LRVEKDGDKR
TVHFTHEGVE KSVTAETILQ ALGRRPNVDG LGLDAARIRT SKGRIDVDAE MRTNVPHIFA
VGDVNGLHEI VHIAIEQGEI AGHNATHPDS PRRCDDRLKT SVTFTDPAVA SVGLSEKECK
AKNISYLSAS HPFGDHGKSM CMGETHGHVK LLCTPDSGEI IGAHIVGPEA GEMIHQMITL
MHYEGTVHDL AQIPHYHPTL SEILTYPAEE LAAQLKQKI
//
