ID A0A0N0GNI5_9NEIS Unreviewed; 243 AA.
AC A0A0N0GNI5;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Glutathione amide-dependent peroxidase {ECO:0000313|EMBL:KPC52862.1};
DE EC=1.11.1.17 {ECO:0000313|EMBL:KPC52862.1};
GN Name=garA {ECO:0000313|EMBL:KPC52862.1};
GN ORFNames=WG78_10245 {ECO:0000313|EMBL:KPC52862.1};
OS Amantichitinum ursilacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Amantichitinum.
OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC52862.1, ECO:0000313|Proteomes:UP000037939};
RN [1] {ECO:0000313|EMBL:KPC52862.1, ECO:0000313|Proteomes:UP000037939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC52862.1,
RC ECO:0000313|Proteomes:UP000037939};
RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT chitin-degrading bacterium.";
RL Submitted (JUL-2015) 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:KPC52862.1}.
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DR EMBL; LAQT01000008; KPC52862.1; -; Genomic_DNA.
DR RefSeq; WP_053937708.1; NZ_LAQT01000008.1.
DR AlphaFoldDB; A0A0N0GNI5; -.
DR STRING; 857265.WG78_10245; -.
DR PATRIC; fig|857265.3.peg.2104; -.
DR OrthoDB; 9800621at2; -.
DR Proteomes; UP000037939; 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; 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:KPC52862.1};
KW Peroxidase {ECO:0000313|EMBL:KPC52862.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037939}.
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 243 AA; 26439 MW; ACD1FB0E8FE9A8BA CRC64;
MLQSREGQRV PNVTFRIREG NDWKDVTTDE LFKGKNVVLF SLPGAFTPTC SSTHLPRYNE
LAPAFKQHGI DAILCVSVND TFVMNEWAKD QESANITMIP DGNGEFTEGM GMLVDKAGLG
FGKRSWRYSM LVKDGVVDKM FIEPEKDGDP FEVSDADTML DYVAPGAKKP DQVVVFTKVG
CGFCAKAKEQ LSAAGYDFVE VPLDNKVRGK VLGALAGKVT APQVFVNGKL IGGSEEVAKF
VAA
//
