ID A0A0D4C1V5_9MICC Unreviewed; 166 AA.
AC A0A0D4C1V5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=UM93_15635 {ECO:0000313|EMBL:AJT42558.1};
OS Psychromicrobium lacuslunae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Psychromicrobium.
OX NCBI_TaxID=1618207 {ECO:0000313|EMBL:AJT42558.1, ECO:0000313|Proteomes:UP000061839};
RN [1] {ECO:0000313|EMBL:AJT42558.1, ECO:0000313|Proteomes:UP000061839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IHBB 11108 {ECO:0000313|EMBL:AJT42558.1,
RC ECO:0000313|Proteomes:UP000061839};
RX PubMed=25908143;
RA Kiran S., Swarnkar M.K., Pal M., Thakur R., Tewari R., Singh A.K.,
RA Gulati A.;
RT "Complete Genome Sequencing of Protease-Producing Novel Arthrobacter sp.
RT Strain IHBB 11108 Using PacBio Single-Molecule Real-Time Sequencing
RT Technology.";
RL Genome Announc. 3:0-0(2015).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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DR EMBL; CP011005; AJT42558.1; -; Genomic_DNA.
DR RefSeq; WP_045076429.1; NZ_CP011005.1.
DR AlphaFoldDB; A0A0D4C1V5; -.
DR STRING; 1618207.UM93_15635; -.
DR KEGG; ari:UM93_15635; -.
DR PATRIC; fig|1618207.4.peg.3182; -.
DR HOGENOM; CLU_029507_2_2_11; -.
DR OrthoDB; 9785502at2; -.
DR Proteomes; UP000061839; Chromosome.
DR GO; GO:0004602; F:glutathione peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd00340; GSH_Peroxidase; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000889; Glutathione_peroxidase.
DR InterPro; IPR029759; GPX_AS.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR11592; GLUTATHIONE PEROXIDASE; 1.
DR PANTHER; PTHR11592:SF40; THIOREDOXIN_GLUTATHIONE PEROXIDASE BTUE; 1.
DR Pfam; PF00255; GSHPx; 1.
DR PIRSF; PIRSF000303; Glutathion_perox; 1.
DR PRINTS; PR01011; GLUTPROXDASE.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00460; GLUTATHIONE_PEROXID_1; 1.
DR PROSITE; PS51355; GLUTATHIONE_PEROXID_3; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000499};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000499};
KW Reference proteome {ECO:0000313|Proteomes:UP000061839}.
FT DOMAIN 1..165
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 40
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 166 AA; 18287 MW; 14512822F0E850DE CRC64;
MTGSEASLYS IPLTLNDGTE TDFGRFQGKT VMVVNVASQC GFTPQYAGLE ALYEKYRAQG
FEVLGVPCNQ FAGQEPGTDE DIQEFCSRNF GVTFTLSKKA DVRGKDQHPL YAELTKFKNG
ILPGLIKWNF EKFLISSEGK VVARFAPNVE PDAEEITSAI ERELAA
//
