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Database: UniProt
Entry: C7JH93_ACEP3
LinkDB: C7JH93_ACEP3
Original site: C7JH93_ACEP3 
ID   C7JH93_ACEP3            Unreviewed;       112 AA.
AC   C7JH93;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Glutaredoxin {ECO:0000256|PIRNR:PIRNR005894};
GN   OrderedLocusNames=APA01_12000 {ECO:0000313|EMBL:BAH99347.1};
OS   Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Acetobacter.
OX   NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH99347.1, ECO:0000313|Proteomes:UP000000948};
RN   [1] {ECO:0000313|EMBL:BAH99347.1, ECO:0000313|Proteomes:UP000000948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX   PubMed=19638423; DOI=10.1093/nar/gkp612;
RA   Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA   Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT   "Whole-genome analyses reveal genetic instability of Acetobacter
RT   pasteurianus.";
RL   Nucleic Acids Res. 37:5768-5783(2009).
CC   -!- SIMILARITY: Belongs to the glutaredoxin family. Monothiol subfamily.
CC       {ECO:0000256|ARBA:ARBA00009630, ECO:0000256|PIRNR:PIRNR005894}.
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DR   EMBL; AP011121; BAH99347.1; -; Genomic_DNA.
DR   RefSeq; WP_003630611.1; NC_013209.1.
DR   AlphaFoldDB; C7JH93; -.
DR   STRING; 634452.APA01_12000; -.
DR   GeneID; 78168510; -.
DR   KEGG; apt:APA01_12000; -.
DR   PATRIC; fig|634452.3.peg.1266; -.
DR   eggNOG; COG0278; Bacteria.
DR   HOGENOM; CLU_026126_2_1_5; -.
DR   OMA; TKLMPQC; -.
DR   BioCyc; APAS634452:APA01_RS06065-MONOMER; -.
DR   Proteomes; UP000000948; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0015036; F:disulfide oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03028; GRX_PICOT_like; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR002109; Glutaredoxin.
DR   InterPro; IPR033658; GRX_PICOT-like.
DR   InterPro; IPR014434; Monothiol_GRX.
DR   InterPro; IPR004480; Monothiol_GRX-rel.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR00365; Grx4 family monothiol glutaredoxin; 1.
DR   PANTHER; PTHR10293; GLUTAREDOXIN FAMILY MEMBER; 1.
DR   PANTHER; PTHR10293:SF72; MONOTHIOL GLUTAREDOXIN-S14, CHLOROPLASTIC; 1.
DR   Pfam; PF00462; Glutaredoxin; 1.
DR   PIRSF; PIRSF005894; Monothiol_GRX; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714, ECO:0000256|PIRSR:PIRSR005894-2};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR005894-2};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR005894-
KW   2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR005894-2}.
FT   DOMAIN          18..82
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000259|Pfam:PF00462"
FT   BINDING         31
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR005894-2"
SQ   SEQUENCE   112 AA;  12517 MW;  6B95DE98E3008C95 CRC64;
     MTDTAQQRIK QDIEANPVML FMKGDADFPQ CGFSARVVQI LQHLGVPFKT ENVLADPAIR
     QGIKDFSNWP TIPQLYVKGE FIGGCDIVTE MYQSGELQNL FKEKNIPCNA PA
//
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