ID J2M9T0_9BURK Unreviewed; 86 AA.
AC J2M9T0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Glutaredoxin {ECO:0000256|RuleBase:RU364065};
GN ORFNames=PMI16_00135 {ECO:0000313|EMBL:EJL94508.1};
OS Herbaspirillum sp. CF444.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Herbaspirillum.
OX NCBI_TaxID=1144319 {ECO:0000313|EMBL:EJL94508.1, ECO:0000313|Proteomes:UP000007296};
RN [1] {ECO:0000313|EMBL:EJL94508.1, ECO:0000313|Proteomes:UP000007296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF444 {ECO:0000313|EMBL:EJL94508.1,
RC ECO:0000313|Proteomes:UP000007296};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- FUNCTION: Has a glutathione-disulfide oxidoreductase activity in the
CC presence of NADPH and glutathione reductase. Reduces low molecular
CC weight disulfides and proteins. {ECO:0000256|ARBA:ARBA00002549,
CC ECO:0000256|RuleBase:RU364065}.
CC -!- SIMILARITY: Belongs to the glutaredoxin family.
CC {ECO:0000256|ARBA:ARBA00007787, ECO:0000256|RuleBase:RU364065}.
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:EJL94508.1}.
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DR EMBL; AKJW01000006; EJL94508.1; -; Genomic_DNA.
DR RefSeq; WP_007875373.1; NZ_AKJW01000006.1.
DR AlphaFoldDB; J2M9T0; -.
DR STRING; 1144319.PMI16_00135; -.
DR PATRIC; fig|1144319.3.peg.132; -.
DR eggNOG; COG0695; Bacteria.
DR OrthoDB; 9814618at2; -.
DR Proteomes; UP000007296; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0015038; F:glutathione disulfide oxidoreductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR CDD; cd03418; GRX_GRXb_1_3_like; 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; IPR011900; GRX_bact.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR NCBIfam; TIGR02181; GRX_bact; 1.
DR PANTHER; PTHR45694; GLUTAREDOXIN 2; 1.
DR PANTHER; PTHR45694:SF18; GLUTAREDOXIN-1; 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 Cytoplasm {ECO:0000256|RuleBase:RU364065};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Electron transport {ECO:0000256|RuleBase:RU364065};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284,
KW ECO:0000256|RuleBase:RU364065}; Transport {ECO:0000256|RuleBase:RU364065}.
FT DOMAIN 5..65
FT /note="Glutaredoxin"
FT /evidence="ECO:0000259|Pfam:PF00462"
SQ SEQUENCE 86 AA; 9601 MW; 732B930863A03389 CRC64;
MTARVVMYST AVCPYCMMAE RLLKSKGIED IEKIRVDLDP QQRDIMMQKT GRRTVPQIYV
GDTHVGGFDD LSALDRAGGL DPLLQA
//
