ID Q6AQZ1_DESPS Unreviewed; 716 AA.
AC Q6AQZ1;
DT 13-SEP-2004, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2004, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Related to mercuric reductase {ECO:0000313|EMBL:CAG35233.1};
GN OrderedLocusNames=DP0504 {ECO:0000313|EMBL:CAG35233.1};
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35233.1, ECO:0000313|Proteomes:UP000000602};
RN [1] {ECO:0000313|Proteomes:UP000000602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602};
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(2004).
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; CR522870; CAG35233.1; -; Genomic_DNA.
DR RefSeq; WP_011187749.1; NC_006138.1.
DR AlphaFoldDB; Q6AQZ1; -.
DR STRING; 177439.DP0504; -.
DR KEGG; dps:DP0504; -.
DR eggNOG; COG0398; Bacteria.
DR eggNOG; COG1249; Bacteria.
DR HOGENOM; CLU_016755_1_0_7; -.
DR OrthoDB; 9786429at2; -.
DR Proteomes; UP000000602; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:UP000000602};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 5..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 198..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..182
FT /note="VTT"
FT /evidence="ECO:0000259|Pfam:PF09335"
FT DOMAIN 237..560
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 582..690
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
SQ SEQUENCE 716 AA; 78726 MW; 68EFC0600DE44094 CRC64;
MKKYLIVGTV IALVSAYYFF GLDSYLSLQA IKTRQVQLES WRNAEPILAG LSFFGLYAVV
ASLSLPGAGV LTVAAGAIFG LIWGVLIVSF ASTLGASLAF LLSRFLLREI VQSRFQDRLH
AVNRGMEEEG AFYLFTLRLV PIFPFFVINL LMGLTSIRLR TFAWVSQLGM LVGTIVYVNA
GTQLAQVESL GGILSTRLLF SFALLGIFPL ICKRGIAWFK GRRLYAKWLR PARFDRNLIV
IGAGAAGLVS AYIATTLKAK VTLVEAAEMG GDCLNYGCVP SKALIKSAKV AHHIRNGDKY
GLDAVELSFS FRRVMARVHR IIATIEPHDS VERYTDLGVE VLCGYARLLD PWTVEVKLKS
GETRRLTSRA VIIATGAGPF IPPLPGLDAV DYLTNETLWN AFANLDEAPR RLLVLGGGPI
GCELSQALAR LGSEVWQIQR GARLLPREDA DAAAIVEASL GADGVHVLTG HTALRCERAG
EEKYIVVEHE GQELRLAFDA LICAVGRVAR LKGYGLEELG IPVKRTVLTN EYLQTLYPNI
FAAGDVAGPY QFTHTAAHQA WYAVVNALFG GIKKFKVDYS VIPWTTFVDP EVARVGLNEQ
EAAERGVDVE VTRYDLDDLD RAITDGVREG FIKILTVPNK DRILGVTIVG EHAGDLLAEF
VLAMKHGLGL NKILSTIHTY PTLAEANKYA AGGWKRKHLP RRLLAWAERY HSWRRL
//
