ID Q2SN86_HAHCH Unreviewed; 728 AA.
AC Q2SN86;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Probable mercuric reductase {ECO:0000313|EMBL:ABC27888.1};
DE EC=1.16.1.1 {ECO:0000313|EMBL:ABC27888.1};
GN OrderedLocusNames=HCH_01003 {ECO:0000313|EMBL:ABC27888.1};
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC27888.1, ECO:0000313|Proteomes:UP000000238};
RN [1] {ECO:0000313|EMBL:ABC27888.1, ECO:0000313|Proteomes:UP000000238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC27888.1,
RC ECO:0000313|Proteomes:UP000000238};
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(2005).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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; CP000155; ABC27888.1; -; Genomic_DNA.
DR RefSeq; WP_011394963.1; NC_007645.1.
DR AlphaFoldDB; Q2SN86; -.
DR STRING; 349521.HCH_01003; -.
DR KEGG; hch:HCH_01003; -.
DR eggNOG; COG0398; Bacteria.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_6; -.
DR OrthoDB; 9800167at2; -.
DR Proteomes; UP000000238; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016152; F:mercury (II) reductase activity; IEA:UniProtKB-EC.
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; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR InterPro; IPR032816; VTT_dom.
DR PANTHER; PTHR43014; MERCURIC REDUCTASE; 1.
DR PANTHER; PTHR43014:SF2; MERCURIC REDUCTASE; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR Pfam; PF09335; SNARE_assoc; 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|RuleBase:RU003691};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003691}; Membrane {ECO:0000256|SAM:Phobius};
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:UP000000238};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 53..76
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 88..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 70..184
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 239..556
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 578..685
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 728 AA; 79493 MW; 3887E54B09E0B8BB CRC64;
MKAKRLGLLL LLALLIGAFF LFDFNRYFSL EYFAEQREAI SAYTTANPLT AAAIYFIVYV
VVTGLSLPAA TVLTLVGGAV FGLFEGTLLV SFASVIGSTI AFLVSRLSLR DWVQDKFGDS
LQAINAGVER EGAMYLFGLR LVPLFPFFVI NLVMGLTPVK ARTFFWVSQL GMLPGTIVYV
NAGTQLGQVQ SASGILTPGL IASFVLLGIF PFIARRILDA LKSRKALAGV DKPAHFDRNL
VVIGAGAAGL VTSYIAAAVK AKVTLIEKHK VGGDCLNTGC VPSKALIRSA KIANYVERAS
EFGVQVSSPE INFAAVMERV QSVIKQVEPH DSVQRYTSLG VECLEGEATI LDPYRVKVNG
QVLTTRNIVI ATGARPFVPP IPGLDLVEYY TSDTIWSLRD KPERLLVIGG GPIGCELSQA
FHRLGVKVTQ LDMSPRLMPR EDTDVSAAVE ARFRNEGIDL RLGYSAKAFK RNASGASLLI
CEKDGEEVEL TFDKVLLAVG RRANTSNLGL DKLGIGVNKD GTLQVNEFLQ TEIPTVFAAG
DVAGPYQFTH TAAHQAWYAA VNSLFGVLRK FRADYRVIPW ATFTDPEVAR VGLNEQDAIA
RNIPYEVTRY GIDDLDRAIA DSEAHGFIKV LTVPGKDKIL GATIVGHHAG ELITEYITAM
KHGIGLNKIL GVIHIYPTLS ETNKYAAGEW KRAHAPQKTL QWLEKWHRWR RKSETDMNSA
LGRSNNEV
//
