ID R4Z2V2_9ACTN Unreviewed; 495 AA.
AC R4Z2V2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Putative glutathione oxidoreductase {ECO:0000313|EMBL:CCM65058.1};
GN ORFNames=BN381_500016 {ECO:0000313|EMBL:CCM65058.1};
OS Candidatus Microthrix parvicella RN1.
OC Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC Microthrixaceae; Microthrix.
OX NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM65058.1, ECO:0000313|Proteomes:UP000018291};
RN [1] {ECO:0000313|EMBL:CCM65058.1, ECO:0000313|Proteomes:UP000018291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN1 {ECO:0000313|EMBL:CCM65058.1,
RC ECO:0000313|Proteomes:UP000018291};
RX PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT based on genomic and metagenomic analyses.";
RL ISME J. 7:1161-1172(2013).
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:CCM65058.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CANL01000046; CCM65058.1; -; Genomic_DNA.
DR AlphaFoldDB; R4Z2V2; -.
DR STRING; 1229780.BN381_500016; -.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_2_0_11; -.
DR Proteomes; UP000018291; 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: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.
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:UP000018291}.
FT DOMAIN 16..332
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 352..457
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 62
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 184..191
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 274
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 315
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 53..58
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 495 AA; 52593 MW; 53D2D5152B77769A CRC64;
MCTPGERVGV QMSETFDLIV IGAGMAGVAA AEKCASRGWR VAIVDALPYG GTCALRGCDP
KKILRRGAEV IDAARLMRGK GIDDDGLSIN WTDLMTHKHG FTDPVPQAME RGLRSSGVET
LHGTAAFTDP NRIVVDGAAY ESQRFLIAAG AKPRPMDFPG AEHLIDSTEF LNLAERPRRV
LFVGGGFISF EFAHIAARAG SAPVIIDRGE RPLKGFDPDL VAQLVKRSTD TGITVKSKTA
ITSIEPADSG YLVTVEQAGH DEIHQTDLVV HGAGRVPELS RLDLDAAGIA HSTKGVTVAG
HLQSTTNPAV FAAGDSADTP GLALTPVAVF EGKVAASNMI NDTTTVPDYT GVPTTVFTIP
ELARVGLLEH EAVARDIDVD VRYNDTSGWY SNYRIGETTA AAKILIDRST DRIVGAHLLG
PGYAELINIL GLAMKADLTS RQLKSMTASY PSVSSDLGSM LCASDQQRVR TAQSCERVDR
LVVELPPAPT PDTKP
//
