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Database: UniProt
Entry: D1NXB9_9GAMM
LinkDB: D1NXB9_9GAMM
Original site: D1NXB9_9GAMM 
ID   D1NXB9_9GAMM            Unreviewed;        87 AA.
AC   D1NXB9;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Glutaredoxin, GrxA family {ECO:0000313|EMBL:EFB74058.1};
GN   Name=grxA {ECO:0000313|EMBL:EFB74058.1};
GN   ORFNames=PROVRUST_04547 {ECO:0000313|EMBL:EFB74058.1};
OS   Providencia rustigianii DSM 4541.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Providencia.
OX   NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB74058.1, ECO:0000313|Proteomes:UP000005512};
RN   [1] {ECO:0000313|EMBL:EFB74058.1, ECO:0000313|Proteomes:UP000005512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB74058.1,
RC   ECO:0000313|Proteomes:UP000005512};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the glutaredoxin family.
CC       {ECO:0000256|ARBA:ARBA00007787}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFB74058.1}.
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DR   EMBL; ABXV02000002; EFB74058.1; -; Genomic_DNA.
DR   RefSeq; WP_006812644.1; NZ_GG703817.1.
DR   AlphaFoldDB; D1NXB9; -.
DR   STRING; 500637.PROVRUST_04547; -.
DR   GeneID; 76391187; -.
DR   eggNOG; COG0695; Bacteria.
DR   HOGENOM; CLU_026126_7_3_6; -.
DR   Proteomes; UP000005512; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd02066; GRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR011767; GLR_AS.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR014025; Glutaredoxin_subgr.
DR   InterPro; IPR011902; GRXA.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR02183; GRXA; 1.
DR   PANTHER; PTHR45694:SF28; GLUTAREDOXIN 1; 1.
DR   PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PRINTS; PR00160; GLUTAREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00195; GLUTAREDOXIN_1; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          4..69
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
SQ   SEQUENCE   87 AA;  10016 MW;  025A3CB62540039F CRC64;
     MYTVIFGRPG CPYCVRAKEL AEKLKNERDD FDYRYVDIQA EGISKEDLSK TVGKTVETVP
     QIFIDEKHIG GCTDFEAYAK ENLNLYK
//
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