ID E4VBS1_BIFBI Unreviewed; 534 AA.
AC E4VBS1;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0000313|EMBL:EFR51036.1};
GN ORFNames=BBNG_01584 {ECO:0000313|EMBL:EFR51036.1};
OS Bifidobacterium bifidum NCIMB 41171.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=398513 {ECO:0000313|EMBL:EFR51036.1, ECO:0000313|Proteomes:UP000002776};
RN [1] {ECO:0000313|EMBL:EFR51036.1, ECO:0000313|Proteomes:UP000002776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 41171 {ECO:0000313|EMBL:EFR51036.1,
RC ECO:0000313|Proteomes:UP000002776};
RG The Broad Institute Genome Sequencing Platform;
RA Goulas T., Tzortzis G., Gibson G.R., Ward D., Mehta T., Young S., Jaffe D.,
RA Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA Birren B.;
RT "Annotation of Bifidobacterium bifidum strain NCIMB 41171.";
RL Submitted (AUG-2008) 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}.
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DR EMBL; DS990230; EFR51036.1; -; Genomic_DNA.
DR AlphaFoldDB; E4VBS1; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_2_11; -.
DR Proteomes; UP000002776; 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}.
FT DOMAIN 16..337
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 364..471
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT REGION 487..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 462
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 63
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 189..196
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 286
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 327
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 54..59
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 534 AA; 57184 MW; B8A825726F3DE28D CRC64;
MTSTSSTDVP SAISADALII GFGKGGKTLA AKLASTGRTV IVAEASADMY GGTCINIGCL
PSKSLILSAD RARREGANRT AETREAAFEA AIREKRRITA MLRDRNYHKL ADQDNITVIT
GRARFTGAHS AEITTADGPV AVAADMMFIN TGATPHIPDI PGIRTTPGVY TSTGLMDVDE
LPQRLVIIGA GFIGLEFASM FADFGTAVTV LQHSDEFLPR EDEDVAAAIR AQLESQGVRF
LFGADTKAIT SADDGIRLSV SMRGTSDVGS EARLCLSTDA VLVATGRTPN VEGLNLEAAG
VELTERGAVK VDDLLRTTAD GIWALGDVNG GPQHTYISLD DYRVVWSQLN GSARPYTLSD
RRNVPSSTFL HTPYSRVGLN EREAKAAGLD YVVKRLPVAT VPKAQVMRRP EGMMKALVEN
GTDRILGAML LAAESHEVIN IVKLAMDMGA PASTLRDMMF THPTMAEALN DLFAQRSRIA
LVRDTFAQRP TNRGSPPWIG GEPLGLSASQ PAVTPRGGDG RRPWRPGQHT WRAR
//
