(data stored in SCRATCH zone)

SWISSPROT: A0KR16_AERHH

ID   A0KR16_AERHH            Unreviewed;       449 AA.
AC   A0KR16;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 93.
DE   SubName: Full=Glutathione-disulfide reductase {ECO:0000313|EMBL:ABK37668.1};
DE            EC=1.8.1.7 {ECO:0000313|EMBL:ABK37668.1};
GN   Name=gor {ECO:0000313|EMBL:ABK37668.1};
GN   OrderedLocusNames=AHA_0019 {ECO:0000313|EMBL:ABK37668.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK37668.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK37668.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK37668.1; -; Genomic_DNA.
DR   RefSeq; WP_011704063.1; NC_008570.1.
DR   RefSeq; YP_854548.1; NC_008570.1.
DR   STRING; 380703.AHA_0019; -.
DR   EnsemblBacteria; ABK37668; ABK37668; AHA_0019.
DR   GeneID; 4490531; -.
DR   KEGG; aha:AHA_0019; -.
DR   PATRIC; fig|380703.7.peg.18; -.
DR   eggNOG; ENOG4105DC8; Bacteria.
DR   eggNOG; COG1249; LUCA.
DR   HOGENOM; HOG000276712; -.
DR   KO; K00383; -.
DR   OMA; KCAIIEA; -.
DR   BioCyc; AHYD380703:G1G7B-19-MONOMER; -.
DR   Proteomes; UP000000756; 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: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; -; 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; A0KR16.
DR   SWISS-2DPAGE; A0KR16.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000756};
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   ECO:0000313|EMBL:ABK37668.1};
KW   Redox-active center {ECO:0000256|RuleBase:RU003691};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000756}.
FT   DOMAIN        6    317       Pyr_redox_2. {ECO:0000259|Pfam:PF07992}.
FT   DOMAIN      338    448       Pyr_redox_dim. {ECO:0000259|Pfam:
FT                                PF02852}.
FT   NP_BIND     173    180       NAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   ACT_SITE    438    438       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000350-2}.
FT   BINDING      51     51       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     261    261       NAD; via amide nitrogen.
FT                                {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   BINDING     302    302       FAD. {ECO:0000256|PIRSR:PIRSR000350-3}.
FT   DISULFID     42     47       Redox-active. {ECO:0000256|PIRSR:
FT                                PIRSR000350-4}.
SQ   SEQUENCE   449 AA;  48483 MW;  02271451E68E4995 CRC64;
     MAQHFDYIAI GGGSGGIASA NRAAMYGKKV ALIEAKELGG TCVNVGCVPK KAMWYAGQIA
     DALKYGADYG FDTTLNHFNW AKLVESRQAY IGRIHQSYQN VLGKNQITVI KGFARFVSSN
     TIEVNGEQYS ADHILIATGG RPEVPAIPGA ELGIDSDGFF ELQSQPKRVA VVGAGYIAVE
     IAGVMQALGS ETHLVVRKHA PLRNFDPMIH ETLVEIMAQE GPKLHTHAIP KAVVKNADES
     LTLQLEDGRH LTVDCLIWAI GRVPATDNLN LAAAGIELDE QGFIPTDKFQ NTAVANVYAV
     GDNTGRIQLT PVAVAAGRRL SERLFNNKPG EHLNYDLVPT VVFSHPPIGT IGLTEPEAIA
     EYGEGQVKVY RSQFTAMYSA LTQHRQPTRM KLVCVGPEEK VVGLHGIGFA MDEILQGFGV
     AMKMGATKAD FDNCVAIHPT SAEEFVTMR
//

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