ID Q2C0P8_9GAMM Unreviewed; 242 AA.
AC Q2C0P8;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 67.
DE SubName: Full=Putative peroxiredoxin/glutaredoxin family protein {ECO:0000313|EMBL:EAR54589.1};
GN ORFNames=SKA34_00135 {ECO:0000313|EMBL:EAR54589.1};
OS Photobacterium sp. SKA34.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=121723 {ECO:0000313|EMBL:EAR54589.1, ECO:0000313|Proteomes:UP000005284};
RN [1] {ECO:0000313|EMBL:EAR54589.1, ECO:0000313|Proteomes:UP000005284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA34 {ECO:0000313|EMBL:EAR54589.1,
RC ECO:0000313|Proteomes:UP000005284};
RA Hagstrom A.J., Ferriera S., Johnson J., Kravitz S., Halpern A.,
RA Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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:EAR54589.1}.
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DR EMBL; AAOU01000028; EAR54589.1; -; Genomic_DNA.
DR RefSeq; WP_006643557.1; NZ_AAOU01000028.1.
DR AlphaFoldDB; Q2C0P8; -.
DR PeroxiBase; 4803; PHspPrxGrx.
DR HOGENOM; CLU_072440_2_2_6; -.
DR OrthoDB; 9800621at2; -.
DR Proteomes; UP000005284; Unassembled WGS sequence.
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; IPR011767; GLR_AS.
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; PS00195; GLUTAREDOXIN_1; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Redox-active center {ECO:0000256|ARBA:ARBA00023284}.
FT DOMAIN 4..168
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 50
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 242 AA; 26669 MW; 5B4E73486D0538C0 CRC64;
MFASKEGQAV PQVTFHTRKG DQWVDVTTED LFANKTVVVF SLPGAFTPTC SSSHLPRYNE
LASVFAENGV DDILCVSVND TFVMNAWKAD QDAENITFIP DGNGEFTKGM DMLVEKDDLG
FGARSWRYSM LVKNGVVEKM FVENEEPGDP FKVSDADTML KYIAPEQKLQ ESITVFSKPG
CPFCVKAKQN LIDKGLQYEE IILGKDATTV SLRAITGRST VPQVFIGGKH IGGSEELETY
LG
//
