ID O86924_9SPHN Unreviewed; 448 AA.
AC O86924;
DT 01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1998, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE SubName: Full=ORF 4 protein {ECO:0000313|EMBL:CAA12270.1};
GN Name=ORF 4 {ECO:0000313|EMBL:CAA12270.1};
OS Sphingomonas sp. RW5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=74360 {ECO:0000313|EMBL:CAA12270.1};
RN [1] {ECO:0000313|EMBL:CAA12270.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RW5 {ECO:0000313|EMBL:CAA12270.1};
RX PubMed=9696766;
RA Werwath J., Arfmann H.A., Pieper D.H., Timmis K.N., Wittich R.M.;
RT "Biochemical and genetic characterization of a gentisate 1, 2-dioxygenase
RT from Sphingomonas sp. strain RW5.";
RL J. Bacteriol. 180:4171-4176(1998).
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; AJ224977; CAA12270.1; -; Genomic_DNA.
DR AlphaFoldDB; O86924; -.
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 GO; GO:0045454; P:cell redox homeostasis; 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; IPR046952; GSHR/TRXR-like.
DR InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR42737; GLUTATHIONE REDUCTASE; 1.
DR PANTHER; PTHR42737:SF2; GLUTATHIONE 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.
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 6..319
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 339..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 52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 175..182
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 304
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 448 AA; 48326 MW; 2F7E7539AC574118 CRC64;
MSDYDYDLIV IGAGSGGVRA ARVAAAHGAR VAIVEEYRVG GTCVIRGCVP KKLLIYGAHF
AEDLRDARQF GWQVPDCQFD WPTLRDNVLA EVDRLEGLYR NTLGSHGVTI LPGRGTIIGP
HGVRIAGGQD VTSRMILVAT GARPLLPSFD GAEHGISSNE AFHLDDVPRR IAIVGGGYIA
NEFAGIFNEL GSAVTVINRS GQLLRGYDHS VRDRLVEIST RKGIAFRFDA SFEKVIKLAD
GSLSVQLAGE DAFSVDCLMF AIGRVPNSSD LGLEEQGVEI DPLGAIIVDD DGRSTVGSIF
AVGDVTNRIQ LTPVAIREGQ AFADTQFGGK PHRVDYRHVP SAVFSHPPIA FVGLTEQQAR
DQVGEVKIYT SDFRPMKNVL AKRDERALYK MICDADTDRI LGLHMIGPDA PEILQAAAIA
VKAGLSKAAF DETIALHPTM AEELVLLR
//
