ID Q6VQZ6_SPHPI Unreviewed; 448 AA.
AC Q6VQZ6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 03-MAY-2023, entry version 94.
DE SubName: Full=ORFG {ECO:0000313|EMBL:AAR05955.1};
GN Name=orfG {ECO:0000313|EMBL:AAR05955.1};
OS Sphingomonas paucimobilis (Pseudomonas paucimobilis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=13689 {ECO:0000313|EMBL:AAR05955.1};
RN [1] {ECO:0000313|EMBL:AAR05955.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B90A {ECO:0000313|EMBL:AAR05955.1};
RX PubMed=15060023; DOI=10.1128/JB.186.8.2225-2235.2004;
RA Dogra C., Raina V., Pal R., Suar M., Lal S., Gartemann K.H., Holliger C.,
RA van der Meer J.R., Lal R.;
RT "Organization of lin genes and IS6100 among different strains of
RT hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for
RT horizontal gene transfer.";
RL J. Bacteriol. 186:2225-2235(2004).
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; AY331258; AAR05955.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6VQZ6; -.
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..447
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 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; 48829 MW; EE394413E23CBD6B CRC64;
MLTYDYDLFV IGAGSGGVRA ARVSAAYGAR VAVAEEHRVG GTCVIRGCVP KKLLVYGSHF
AEDLQDARRF GWKVPDCEFD WSALRDNVLA EVSRLEGLYT ETLGNNKVEI IRERATVAGP
HEVLLGSGQT ITAGKILIAT GAWPIVPHFP GAEHGITSNE VFHLDTFPKR VVIAGAGYIA
NEFAGIFHQF GAHVTLVNRT DVILRGYDEQ IRDRLLQISM TKGIEFKFHV AFEKVDKQPD
GSLLVHMTGH EPIPADMLLF ATGRRPHTEN LGLETADVAL DAKGAIKVDD DNRSSCASIY
AVGDVTNRVQ LTPVAIREGQ AFADTVFGNN PRRVDYGCIP SAVFSHPPMA GVGMTEAEAR
NKLGEVKVYT SDFRAMKNVL ADRHERALYK LVVHPETDVV VGIHMIGPDA PEILQAAAIA
VKARLTKAQF DDTVALHPSM AEELVLMR
//
