(data stored in SCRATCH zone)

SWISSPROT: A8FPI2_SHESH

ID   A8FPI2_SHESH            Unreviewed;       451 AA.
AC   A8FPI2;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   08-MAY-2019, entry version 80.
DE   SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:ABV34755.1};
GN   OrderedLocusNames=Ssed_0142 {ECO:0000313|EMBL:ABV34755.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34755.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34755.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34755.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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|RuleBase:RU003691}.
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DR   EMBL; CP000821; ABV34755.1; -; Genomic_DNA.
DR   RefSeq; WP_012004281.1; NC_009831.1.
DR   STRING; 425104.Ssed_0142; -.
DR   EnsemblBacteria; ABV34755; ABV34755; Ssed_0142.
DR   KEGG; sse:Ssed_0142; -.
DR   eggNOG; ENOG4105DC8; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276712; -.
DR   KO; K00383; -.
DR   OMA; KCAIIEA; -.
DR   OrthoDB; 267896at2; -.
DR   BioCyc; SSED425104:G1G9Y-151-MONOMER; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 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; IPR006322; Glutathione_Rdtase_euk/bac.
DR   InterPro; IPR001100; Pyr_nuc-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR012999; Pyr_OxRdtase_I_AS.
DR   PANTHER; PTHR42737; PTHR42737; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PIRSF; PIRSF000350; Mercury_reductase_MerA; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR01421; gluta_reduc_1; 1.
DR   PROSITE; PS00076; PYRIDINE_REDOX_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPI2.
DR   SWISS-2DPAGE; A8FPI2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   FAD {ECO:0000256|PIRSR:PIRSR000350-3, ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW   NAD {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Nucleotide-binding {ECO:0000256|PIRSR:PIRSR000350-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003691};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002015}.
FT   DOMAIN        6    319       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      340    450       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     174    181       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    440    440       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      51     51       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     115    115       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000350-
FT                                3}.
FT   BINDING     262    262       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     303    303       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     42     47       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   451 AA;  48528 MW;  0CAE2BC2D99EDCF2 CRC64;
     MAQHFDYICL GAGSGGIASA NRAAMRGAKV LLIEAKALGG TCVNVGCVPK KVMWYGAQVA
     EALHLYAKDY GFDVTVNKFD WNTLVASRDA YIERIHGSYD RGLENNKVTL VRGYGRFVNE
     RTIEVDGQEY TADHILIATG GSPSIPNIPG AEHGIDSDGF FELRAQPKRV AVIGAGYIAV
     ELAGVLHSLG SETHLFVRKH APLRSFDPML SEALMESMAT DGPTLHTHST PESVIKNSDG
     SLTLKLENGE SFEVDTLIWA IGRKPSTGNI GLENTQVKLN DKGYVVVDEQ QNTTNPGIYC
     VGDIIEGGVE LTPVAVKAGR LLSERLFNGM TDAKMDYTLI PTVVFSHPAI GTMGLSEPEA
     IAQYGTDQVK CYNSGFTSMY TAVTAHRQAC KMKLVCAGPD EKVVGIHGIG FGMDEILQGF
     GVAMKMGATK KQFDSVVAIH PTGAEEFVTM R
//

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