ID K5YU05_9BACT Unreviewed; 458 AA.
AC K5YU05;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Pyridine nucleotide-disulfide oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1077_03325 {ECO:0000313|EMBL:EKN06519.1};
OS Parabacteroides johnsonii CL02T12C29.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=999419 {ECO:0000313|EMBL:EKN06519.1, ECO:0000313|Proteomes:UP000001218};
RN [1] {ECO:0000313|EMBL:EKN06519.1, ECO:0000313|Proteomes:UP000001218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL02T12C29 {ECO:0000313|EMBL:EKN06519.1,
RC ECO:0000313|Proteomes:UP000001218};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Zitomersky N.L., Coyne M.J.,
RA Comstock L.E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Parabacteroides johnsonii CL02T12C29.";
RL Submitted (FEB-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 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:EKN06519.1}.
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DR EMBL; AGZP01000030; EKN06519.1; -; Genomic_DNA.
DR RefSeq; WP_008158293.1; NZ_JH976468.1.
DR AlphaFoldDB; K5YU05; -.
DR PATRIC; fig|999419.3.peg.3397; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_2_10; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000001218; 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:UP000001218}.
FT DOMAIN 4..318
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 347..453
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 444
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-2"
FT BINDING 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 177..184
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 200
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 269
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 310
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 43..48
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 458 AA; 50103 MW; C68084BD26049ECE CRC64;
MKKYDAIIIG FGKGGKTLAA DLGSRGWTVA VVERSKEMYG GTCINIGCIP TKTLVHLSKV
AQYSHFTTFE QYADAFHKAI EEKRKITAAL RQKNFENLDS KETVTVYTGV ASFLSPTEVE
VKTDRETIVL QAGKIFINTG ASTIVPNIKG IEGNPFVYTS TSIMELDRLP RRLAIVGGGY
IGLEFASIFA NFGSDVTVLE GGDKFIPRED RDIADAVKTV LEKKGISIRL NAVVQEIGHD
VGKATVVYRD ALTGDTEQID ADAILLATGR RPNTEGLNLQ AAGVKLTERG AIEVDDRLHT
SADNIWAIGD VRGGLQFTYL SLDDYRIIRD ELFGDGKRNT GDREAVAYSV FIDPPLSHVG
LNEEQALRTG RNIKVSKVMA ASMPRTRTIG QPEGLLKTVV DADTNQILGA TLFCAESSEI
INLVSLAMRT DNDYVLLRDN IFTHPSMSES LNDLFNIK
//
