ID Q1ZQ73_PHOAS Unreviewed; 193 AA.
AC Q1ZQ73;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Glutathione peroxidase {ECO:0000256|RuleBase:RU000499};
GN ORFNames=VAS14_01861 {ECO:0000313|EMBL:EAS64424.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS64424.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS64424.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS64424.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC -!- SIMILARITY: Belongs to the glutathione peroxidase family.
CC {ECO:0000256|ARBA:ARBA00006926, ECO:0000256|RuleBase:RU000499}.
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:EAS64424.1}.
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DR EMBL; AAOJ01000003; EAS64424.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1ZQ73; -.
DR eggNOG; COG0386; Bacteria.
DR HOGENOM; CLU_029507_1_3_6; -.
DR Proteomes; UP000001603; Unassembled WGS sequence.
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:SF44; GLUTATHIONE PEROXIDASE; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..193
FT /note="Glutathione peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004198585"
FT DOMAIN 24..192
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 72
FT /evidence="ECO:0000256|PIRSR:PIRSR000303-1"
SQ SEQUENCE 193 AA; 21410 MW; FBD43210303926BE CRC64;
MQVVSSNHFI LRLILLVSSI FFTSLVTTSA NASSCPTLYQ APLKKLNSDE YYDICQQLTG
KVVLVVNTAS QCGFTPQFKQ LEELYKTYKD SGLVVIGFPS NDFKQDRGSE QQTANICYSN
YGVTFPMMTK TSVKGSRANS LYKHLIAQSG KSVGWNFQKY LLNKQGQVVG VFPSSLSPTS
NEMVAAIKQQ LKM
//
