ID A0A1A9F287_9GAMM Unreviewed; 245 AA.
AC A0A1A9F287;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Glutathione peroxidase {ECO:0000313|EMBL:ANG64275.1};
GN ORFNames=A8C75_18555 {ECO:0000313|EMBL:ANG64275.1};
OS Marinobacterium aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG64275.1, ECO:0000313|Proteomes:UP000078070};
RN [1] {ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA Baek K., Yang S.-J.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANG64275.1, ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|EMBL:ANG64275.1,
RC ECO:0000313|Proteomes:UP000078070};
RX PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA Bae S.S., Jung J., Chung D., Baek K.;
RT "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT isolated from estuary sediment.";
RL Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
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DR EMBL; CP015839; ANG64275.1; -; Genomic_DNA.
DR RefSeq; WP_067385744.1; NZ_CP015839.1.
DR AlphaFoldDB; A0A1A9F287; -.
DR STRING; 1821621.A8C75_18555; -.
DR KEGG; mars:A8C75_18555; -.
DR OrthoDB; 9800621at2; -.
DR Proteomes; UP000078070; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011906; Glutaredoxin_dom.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02190; GlrX-dom; 1.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:ANG64275.1};
KW Peroxidase {ECO:0000313|EMBL:ANG64275.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078070}.
FT DOMAIN 3..167
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 49
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 245 AA; 27034 MW; 33459171D38150C4 CRC64;
MQHKEGQRVP QVTFRTRVGN DWQDLTSDEI FAGKNVILFA LPGAFTPTCS TTHLPRYNEL
APVFQANGVD SIICLSVNDA FVMNAWAEDQ KLAHIQVLPD GNGEFSDGMG MLVDKADLGF
GKRSWRYSML VKDGVIDKMF IEPDLPGDPF EVSDADTMLN YINPQAQQPK RVTIITKPGC
PHCTRAKKVL SEHEFRYEEI VLGQGGVSYS SLTAISGRGT TPQVYIDGLH VGTADELEQW
LAANA
//
