ID A0A1Z4BZV4_9GAMM Unreviewed; 201 AA.
AC A0A1Z4BZV4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Alkyl hydroperoxide reductase C {ECO:0000256|ARBA:ARBA00017462};
DE EC=1.11.1.26 {ECO:0000256|ARBA:ARBA00013021};
DE AltName: Full=Peroxiredoxin {ECO:0000256|ARBA:ARBA00032077};
GN ORFNames=AADEFJLK_02191 {ECO:0000313|EMBL:POZ51970.1}, CEK71_12350
GN {ECO:0000313|EMBL:ASF46803.1};
OS Methylovulum psychrotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylovulum.
OX NCBI_TaxID=1704499 {ECO:0000313|EMBL:ASF46803.1, ECO:0000313|Proteomes:UP000197019};
RN [1] {ECO:0000313|EMBL:ASF46803.1, ECO:0000313|Proteomes:UP000197019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HV10_M2 {ECO:0000313|EMBL:ASF46803.1,
RC ECO:0000313|Proteomes:UP000197019};
RA Mateos-Rivera A.;
RT "Genome Sequencing of the methanotroph Methylovulum psychrotolerants str.
RT HV10-M2 isolated from a high-altitude environment.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:POZ51970.1, ECO:0000313|Proteomes:UP000237423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sph1 {ECO:0000313|EMBL:POZ51970.1,
RC ECO:0000313|Proteomes:UP000237423};
RA Oshkin I.Y., Miroshnikov K., Belova S.E., Korzhenkov A., Toshchakov S.V.,
RA Dedysh S.N.;
RT "Draft Genome Sequence of Methylobacter psychrotolerans Sph1T, an Obligate
RT Methanotroph from Low-Temperature Environments.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of
CC hydrogen peroxide and organic hydroperoxides to water and alcohols,
CC respectively. Plays a role in cell protection against oxidative stress
CC by detoxifying peroxides. {ECO:0000256|ARBA:ARBA00037420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a hydroperoxide + H(+) + NADH = an alcohol + H2O + NAD(+);
CC Xref=Rhea:RHEA:62628, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.11.1.26;
CC Evidence={ECO:0000256|ARBA:ARBA00000318};
CC -!- SIMILARITY: Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009796}.
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DR EMBL; CP022129; ASF46803.1; -; Genomic_DNA.
DR EMBL; PGFZ01000004; POZ51970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4BZV4; -.
DR KEGG; mpsy:CEK71_12350; -.
DR OrthoDB; 9812811at2; -.
DR Proteomes; UP000197019; Chromosome.
DR Proteomes; UP000237423; Unassembled WGS sequence.
DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro.
DR CDD; cd03015; PRX_Typ2cys; 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; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10681; THIOREDOXIN PEROXIDASE; 1.
DR PANTHER; PTHR10681:SF128; THIOREDOXIN-DEPENDENT PEROXIDE REDUCTASE, MITOCHONDRIAL; 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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000197019}.
FT DOMAIN 3..164
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate; for
FT peroxidase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000239-1"
SQ SEQUENCE 201 AA; 21945 MW; 6BEFC0A5579BE094 CRC64;
MSVLVGKQAP DFTVPAVLGD GQIVDSFSFS EATKGKYAVV FFYPLDFTFV CPSELIALDH
RMEEFTKRGV EVIAVSIDSH FTHNAWRNTP INKGGIGPVR YTMAADLAHS ICKAYDVEAA
APAVAYRGTF LIDQSGLVRY QVVNDLPLGR NMDELLRMVD ALQFHEEHGE VCPAGWTKGD
AGMNASPAGV AEYLDKNADK L
//