(data stored in SCRATCH zone)

SWISSPROT: Q3IIA8_PSEHT

ID   Q3IIA8_PSEHT            Unreviewed;       453 AA.
AC   Q3IIA8;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 97.
DE   SubName: Full=Glutathione reductase {ECO:0000313|EMBL:CAI85458.1};
DE            EC=1.8.1.7 {ECO:0000313|EMBL:CAI85458.1};
GN   Name=gor {ECO:0000313|EMBL:CAI85458.1};
GN   OrderedLocusNames=PSHAa0360 {ECO:0000313|EMBL:CAI85458.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85458.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85458.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- SIMILARITY: Belongs to the class-I pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000256|RuleBase:RU003691}.
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DR   EMBL; CR954246; CAI85458.1; -; Genomic_DNA.
DR   RefSeq; WP_011327071.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIA8; -.
DR   STRING; 326442.PSHAa0360; -.
DR   EnsemblBacteria; CAI85458; CAI85458; PSHAa0360.
DR   GeneID; 32567129; -.
DR   KEGG; pha:PSHAa0360; -.
DR   eggNOG; ENOG4105DC8; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276712; -.
DR   KO; K00383; -.
DR   OMA; KCAIIEA; -.
DR   OrthoDB; POG091H0239; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005623; C:cell; IEA:GOC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004362; F:glutathione-disulfide reductase activity; IEA:UniProtKB-EC.
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; -; 1.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer.
DR   InterPro; IPR006322; Glutathione_Rdtase_euk/bac.
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   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; Q3IIA8.
DR   SWISS-2DPAGE; Q3IIA8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   FAD {ECO:0000256|RuleBase:RU003691};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003691};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003691,
KW   ECO:0000313|EMBL:CAI85458.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843}.
FT   DOMAIN        6    319       FAD/NAD-binding_dom. {ECO:0000259|Pfam:
FT                                PF07992}.
FT   DOMAIN      342    452       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
SQ   SEQUENCE   453 AA;  48750 MW;  FD295FC4716F36E7 CRC64;
     MAQHFDYIAI GGGSGGIASA NRAAMRGAKV ALIEAKHMGG TCVNVGCVPK KVMWHGAQVA
     EAINLYAPDY GFNVEVKGFD WGKLVESREA YIGRIHKGYD NGLANNGVTV IKGFAKFVDN
     KTVEVDGEHY TADHILIAVG GRPSIPNIEG AEHGIDSNGF FELKEQPKRV AVIGAGYIAV
     ELAGVLHSLG TDTHLFVRKH APLRNFDPYI IDTLVEVMAK EGPTLHTESV PHKLVKEDDG
     SVTLHLDNGK SHNVDQVIWA IGREPTTNAI NIAAAGVEVN SKGFVKVDEY QNTTAKNVYA
     VGDIIENGIE LTPVAVKAGR TLSERLFNKE LPDDLKMDYS LVPTVVFSHP PIGTIGLTEQ
     EAISQYGAEN VKVYQSAFAA MYTAVTQHRQ PCKMKLVCAG PDEKVVGLHG IGFAVDEMIQ
     GFAVAMKMGA TKADFDAVVA IHPTGSEEFV TMR
//

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