ID G4T0J8_META2 Unreviewed; 580 AA.
AC G4T0J8;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Pyridine nucleotide-disulphide oxidoreductase family protein {ECO:0000313|EMBL:CCE25602.1};
GN OrderedLocusNames=MEALZ_3946 {ECO:0000313|EMBL:CCE25602.1};
OS Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylotuvimicrobium.
OX NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE25602.1, ECO:0000313|Proteomes:UP000008315};
RN [1] {ECO:0000313|Proteomes:UP000008315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC {ECO:0000313|Proteomes:UP000008315};
RX PubMed=22207753; DOI=10.1128/JB.06392-11;
RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA Trotsenko Y.A., Kalyuzhnaya M.G.;
RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT Methylomicrobium alcaliphilum 20Z.";
RL J. Bacteriol. 194:551-552(2012).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; FO082060; CCE25602.1; -; Genomic_DNA.
DR RefSeq; WP_014150351.1; NC_016112.1.
DR AlphaFoldDB; G4T0J8; -.
DR STRING; 1091494.MEALZ_3946; -.
DR KEGG; mah:MEALZ_3946; -.
DR PATRIC; fig|271065.3.peg.4077; -.
DR HOGENOM; CLU_003291_1_2_6; -.
DR Proteomes; UP000008315; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR43031; FAD-DEPENDENT OXIDOREDUCTASE; 1.
DR PANTHER; PTHR43031:SF7; NITRIC OXIDE REDUCTASE FLRD-NAD(+) REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000008315}.
FT DOMAIN 493..580
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 580 AA; 63996 MW; 2830F1BE0BB18D35 CRC64;
MNKRILIIGG VAGGASCAAR LRRLCEHCEI VIFEMGSYVS FANCGLPYFI GDVIVDEQKL
LVATPELFEK RFNIRVCTDS EVLAIDRTNK SIEVCDLKTG RKRNESYDAL VLSTGSEAVW
PDIDGIDLPG IYVLRTIPDS RKIRGNLANM KSAVVLGAGF LGLELAENLK KRALKVTVLQ
STDQVMPALD KEMARFVAQY LQKNDIDLQL NCQVNRFELN QDQTLTVHRQ DGESIISDAV
MVSVGVKPRT QLARQAGLAI GDLGGIRVDE TMQTSDSHIW AVGDVVEVRN VITGEWQLLP
LAGPANRQGR LAAAAILSNG DQQEIPSTYR GVQGTSVCGL FDLTIASTGV NEKTLQKINY
ENYEKVYLHP GNHVGYYPGA KPIHMKLLYD TSNGKILGAQ ALGESGVARR VDVISAFIQM
GGSVYDLEEA ELCYAPQFGA TKDPVNLAGM IAANQLRGMH PLAKWEELLE THVQVTEDKD
EAAQLLAFIL DDPFTQAQLV DVRTEAEFLQ KHIPNAINIP LDNLRDRLNE LSREREIWVV
CGVGQRAYNA TRILQQNGFR VRNLSGGMQT YETYNGDSEQ
//
