ID A0A0D6P6D3_9PROT Unreviewed; 458 AA.
AC A0A0D6P6D3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase dimerisation region {ECO:0000313|EMBL:GAN77217.1};
GN ORFNames=Asru_0257_09 {ECO:0000313|EMBL:GAN77217.1};
OS Acidisphaera rubrifaciens HS-AP3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidisphaera.
OX NCBI_TaxID=1231350 {ECO:0000313|EMBL:GAN77217.1, ECO:0000313|Proteomes:UP000032680};
RN [1] {ECO:0000313|EMBL:GAN77217.1, ECO:0000313|Proteomes:UP000032680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS-AP3 {ECO:0000313|EMBL:GAN77217.1,
RC ECO:0000313|Proteomes:UP000032680};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidisphaera rubrifaciens HS-AP3.";
RL Submitted (NOV-2012) 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 -!- 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:GAN77217.1}.
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DR EMBL; BANB01000257; GAN77217.1; -; Genomic_DNA.
DR RefSeq; WP_048861214.1; NZ_BANB01000257.1.
DR AlphaFoldDB; A0A0D6P6D3; -.
DR OrthoDB; 9764616at2; -.
DR Proteomes; UP000032680; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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 PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 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.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Flavoprotein {ECO:0000256|PIRSR:PIRSR000350-3};
KW NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000032680}.
FT DOMAIN 5..320
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 343..447
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 50
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 176..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 199
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 307
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 41..46
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 458 AA; 49033 MW; 5F3FAB40B853CE0F CRC64;
MTDFDAIIIG AGQAGPSLAF RLAGAGMKVA VIERHLIGGS CVNTGCTPTK ALVASAYVAR
IARRAGEYGL LVGGDIGIDM RQVKARMDAI VAASRNGLTS ALESAPNIML YRGHARFASP
QVVTVAGEQL RAGQIFINVG GRAVVPPMPG INEVPYLTNS SMMNVDFLPP HLIIIGGSYI
GLEFGQMYRR FGSQVTIIEM GPRLVRHEDE DVSAAIKSIL ELEGIEVRLN AECVSLAKRG
DEIIAKVDCT AGAPEIVGSH LLLAVGRRPN TDDLDLDIAG VRCDERGYIV VDDRLQTTAP
GIWALGDCNG RGAFTHTAYN DFEIVAAQLL DRDPRSLGER ITAYALYTDP PLARVGMTLA
QARPSGRRVL AGDRPMTRVA RAVERGETQG FMRILVDGDS KEILGASLLG TGCDEAVHAI
LDLMYARVPY TVMQRAMHIH PTVSELLPTI LGGLRPVV
//
