ID J7QM94_METSZ Unreviewed; 279 AA.
AC J7QM94;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:CCJ06298.1};
GN OrderedLocusNames=BN69_0847 {ECO:0000313|EMBL:CCJ06298.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ06298.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ06298.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ06298.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|PIRSR:PIRSR006816-2};
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DR EMBL; HE956757; CCJ06298.1; -; Genomic_DNA.
DR AlphaFoldDB; J7QM94; -.
DR STRING; 187303.BN69_0847; -.
DR KEGG; msc:BN69_0847; -.
DR PATRIC; fig|187303.17.peg.927; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_1_5; -.
DR Proteomes; UP000005263; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR CDD; cd06221; sulfite_reductase_like; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR43513:SF1; ANAEROBIC SULFITE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2}.
FT DOMAIN 12..107
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 243
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 248
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 251
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 259
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 279 AA; 30592 MW; 70370DEC82122597 CRC64;
MLKACAPLSY PMAPSMTPVT RFTRESADVF TFDLLPERAT PFAPGQFNML YAFGVGEIPI
SISGDSQAPE RLTHTIRAVG PVSAALGKLK AGDQVGLRGP FGVGWPVEEA KGFDVLLIGG
GIGLAPLRPA IYWLLRHRAA YGRVGVLYGA RTPEDLIFRD ELEEWRKTPD FQLRVAVERA
GPDWTGDVGY VTPLLSKLRY EPADAIAMIC GPEVMIRATA LALEDAGVAD SRIFISMERN
MKCAIGHCGH CQFGPLFICK DGPVHRYDRV RDLLAYREL
//
