ID   A3IJB7_9CHRO            Unreviewed;       395 AA.
AC   A3IJB7;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 80.
DE   SubName: Full=Mercuric reductase {ECO:0000313|EMBL:EAZ93899.1};
GN   ORFNames=CY0110_18927 {ECO:0000313|EMBL:EAZ93899.1};
OS   Crocosphaera chwakensis CCY0110.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Aphanothecaceae; Crocosphaera; Crocosphaera chwakensis.
OX   NCBI_TaxID=391612 {ECO:0000313|EMBL:EAZ93899.1, ECO:0000313|Proteomes:UP000003781};
RN   [1] {ECO:0000313|EMBL:EAZ93899.1, ECO:0000313|Proteomes:UP000003781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCY0110 {ECO:0000313|EMBL:EAZ93899.1,
RC   ECO:0000313|Proteomes:UP000003781};
RA   Stal L., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EAZ93899.1}.
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DR   EMBL; AAXW01000002; EAZ93899.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3IJB7; -.
DR   eggNOG; COG1249; Bacteria.
DR   Proteomes; UP000003781; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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   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   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        55..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..235
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          260..360
FT                   /note="Pyridine nucleotide-disulphide oxidoreductase
FT                   dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF02852"
SQ   SEQUENCE   395 AA;  45433 MW;  4192FAFBF7D61D9A CRC64;
     MKQWKNKVKQ DIKELTNREK LAKLGVDIIE ESGEFCRLPK LGFVLKTRTL RSRRYLLAIS
     SLAITPQIPG LAEVGYVIPE TLDIDQLPQN IVILCQTYLG IELAQLLNRL GKKITLIIEN
     SNILLQEDKD IIQLIQAILE AENIKLLINS SITQVRKIEG KKWIQAGNKA IETNEIIVVN
     QRILNTNRLN LEGVKVEIEN NKIKTNNKLQ TTNPNIYACG RAMGQYSLSN IAQYEASIAI
     KNTIFYPIFK VNYDYHPIRM LTNPIFSRVG LTETQAQQQY KNDIIIIKQN YKTLVKATVL
     DETTGFCKLI TRRNGLILGC HIIGNNSDEI INIVAYAIKN KIKIQEIAKL FPPYGTISEI
     LFKISRQWQE KKNREKKLLN NCLETLLFWR RKWSQ
//