ID A0A0D6AI94_9CHRO Unreviewed; 475 AA.
AC A0A0D6AI94;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE SubName: Full=Mercuric ion reductase {ECO:0000313|EMBL:BAQ62538.1};
GN ORFNames=GM3708_2944 {ECO:0000313|EMBL:BAQ62538.1};
OS Geminocystis sp. NIES-3708.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Geminocystis.
OX NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ62538.1, ECO:0000313|Proteomes:UP000060542};
RN [1] {ECO:0000313|EMBL:BAQ62538.1, ECO:0000313|Proteomes:UP000060542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ62538.1,
RC ECO:0000313|Proteomes:UP000060542};
RA Hirose Y.;
RT "Geminocystis sp. NIES-3708 complete genome sequence.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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; AP014815; BAQ62538.1; -; Genomic_DNA.
DR RefSeq; WP_066348333.1; NZ_AP014815.1.
DR AlphaFoldDB; A0A0D6AI94; -.
DR STRING; 1615909.GM3708_2944; -.
DR KEGG; gee:GM3708_2944; -.
DR PATRIC; fig|1615909.3.peg.2992; -.
DR OrthoDB; 9807946at2; -.
DR Proteomes; UP000060542; Chromosome.
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 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 InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR PANTHER; PTHR43014; MERCURIC 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000060542}.
FT DOMAIN 5..317
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 337..440
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT BINDING 51
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 139..141
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 176..183
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 262
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT BINDING 302
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-3"
FT DISULFID 42..47
FT /note="Redox-active"
FT /evidence="ECO:0000256|PIRSR:PIRSR000350-4"
SQ SEQUENCE 475 AA; 52263 MW; 0835FD5984489EE2 CRC64;
MTREYDLVII GGGSGGLVIA SAAAQLKAKV ALVEKHRLGG DCLWYGCIPS KSLIHASRVA
YQVKNSHNFG IYNDNLEIKF AEAINHVQKV ISTIEPNDSP ERFRGLGVDV IFGNGKFIDE
NTFEVSGKQL KPRNFVISTG SSPEIPEIEG LSAAGFITNE QVFSLTHLPE SIIIMGGGAI
ACELGQALKR LGAEITIIAS KSQLLPKEDL EASKIIENQF IEEGIRIIKS AKAEKVKIID
GKKVVFVNGE KLIAEEILVS IGRIPNIQSL DLKKAKVQYN HQGIKVNNKL QTSNKKIYSC
GDVIGGYQFT HVAGYEATII LQNALFFPTK NVDYRVISWA TFTSPELARV GINESQAREI
YGDNIIILKL EMKEVDRAQT AKNIKGFCKI ITTLKGDILG ATIIGESAGE LIHEIVLAMK
NNLKVTSLSG IHIYPTLSEI NSKTALLFVK QKYAQNQGLQ NLLTKFFNFR RWLGF
//
