ID F5RA13_METUF Unreviewed; 211 AA.
AC F5RA13;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=Peroxidase {ECO:0000313|EMBL:EGK72616.1};
GN ORFNames=METUNv1_01091 {ECO:0000313|EMBL:EGK72616.1};
OS Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Sterolibacteriaceae; Methyloversatilis.
OX NCBI_TaxID=1000565 {ECO:0000313|EMBL:EGK72616.1, ECO:0000313|Proteomes:UP000005019};
RN [1] {ECO:0000313|EMBL:EGK72616.1, ECO:0000313|Proteomes:UP000005019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5
RC {ECO:0000313|Proteomes:UP000005019};
RX PubMed=21725020; DOI=10.1128/JB.05331-11;
RA Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT representative of the order Rhodocyclales.";
RL J. Bacteriol. 193:4541-4542(2011).
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. Prx6 subfamily.
CC {ECO:0000256|ARBA:ARBA00025719}.
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:EGK72616.1}.
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DR EMBL; AFHG01000034; EGK72616.1; -; Genomic_DNA.
DR RefSeq; WP_008059599.1; NZ_AFHG01000034.1.
DR AlphaFoldDB; F5RA13; -.
DR STRING; 1000565.METUNv1_01091; -.
DR eggNOG; COG0450; Bacteria.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000005019; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03016; PRX_1cys; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ.
DR InterPro; IPR019479; Peroxiredoxin_C.
DR InterPro; IPR045020; PRX_1cys.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR43503; MCG48959-RELATED; 1.
DR PANTHER; PTHR43503:SF4; PEROXIREDOXIN-6; 1.
DR Pfam; PF10417; 1-cysPrx_C; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR PIRSF; PIRSF000239; AHPC; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant {ECO:0000256|ARBA:ARBA00022862};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:EGK72616.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005019}.
FT DOMAIN 3..159
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 45
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 211 AA; 23597 MW; 7F75A7700BDBFB3F CRC64;
MTIRLGDIAP DFEQDSSAGR IRFHEWLGNS WGVLFSHPAD FTPVCTTELG LTAKLKGEFD
KRGVKAIALS VDPVDSHHKW IADINDTQNT TVNFPIIADG DRKVSELYDM IHPNANATLT
VRSLFIIDPN KKVRLIITYP ASTGRNFDEV LRVIDSLQLT DKHSVATPGN WKHGDDVVIV
PSLQDPDEIA RRFPAGYKAV RPYLRLTPQP K
//
