(data stored in SCRATCH zone)

SWISSPROT: C8W4X0_DESAS

ID   C8W4X0_DESAS            Unreviewed;       328 AA.
AC   C8W4X0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 73.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01400, ECO:0000256|HAMAP-Rule:MF_01401};
DE   Includes:
DE     RecName: Full=Peptide methionine sulfoxide reductase MsrA {ECO:0000256|HAMAP-Rule:MF_01401};
DE              Short=Protein-methionine-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE              EC=1.8.4.11 {ECO:0000256|HAMAP-Rule:MF_01401};
DE     AltName: Full=Peptide-methionine (S)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE              Short=Peptide Met(O) reductase {ECO:0000256|HAMAP-Rule:MF_01401};
DE   Includes:
DE     RecName: Full=Peptide methionine sulfoxide reductase MsrB {ECO:0000256|HAMAP-Rule:MF_01400};
DE              EC=1.8.4.12 {ECO:0000256|HAMAP-Rule:MF_01400};
DE     AltName: Full=Peptide-methionine (R)-S-oxide reductase {ECO:0000256|HAMAP-Rule:MF_01400};
GN   Name=msrB {ECO:0000256|HAMAP-Rule:MF_01400};
GN   Synonyms=msrA {ECO:0000256|HAMAP-Rule:MF_01401};
GN   OrderedLocusNames=Dtox_0373 {ECO:0000313|EMBL:ACV61322.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61322.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61322.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Has an important function as a repair enzyme for
CC       proteins that have been inactivated by oxidation. Catalyzes the
CC       reversible oxidation-reduction of methionine sulfoxide in proteins
CC       to methionine. {ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionine =
CC         [thioredoxin]-dithiol + L-methionine (S)-S-oxide;
CC         Xref=Rhea:RHEA:19993, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:57844, ChEBI:CHEBI:58772;
CC         EC=1.8.4.11; Evidence={ECO:0000256|HAMAP-Rule:MF_01401,
CC         ECO:0000256|SAAS:SAAS01115769};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:24164, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:45764, ChEBI:CHEBI:50058; EC=1.8.4.12;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01400};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] =
CC         [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein];
CC         Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:44120, ChEBI:CHEBI:50058; EC=1.8.4.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01401,
CC         ECO:0000256|SAAS:SAAS01115765};
CC   -!- SIMILARITY: Belongs to the MsrA Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01401}.
CC   -!- SIMILARITY: Belongs to the MsrB Met sulfoxide reductase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01400}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01400}.
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DR   EMBL; CP001720; ACV61322.1; -; Genomic_DNA.
DR   RefSeq; WP_015756043.1; NC_013216.1.
DR   STRING; 485916.Dtox_0373; -.
DR   EnsemblBacteria; ACV61322; ACV61322; Dtox_0373.
DR   KEGG; dae:Dtox_0373; -.
DR   eggNOG; ENOG4105E0X; Bacteria.
DR   eggNOG; COG0225; LUCA.
DR   eggNOG; COG0229; LUCA.
DR   HOGENOM; HOG000243423; -.
DR   KO; K12267; -.
DR   OMA; YGDFLIL; -.
DR   OrthoDB; 1554384at2; -.
DR   BioCyc; DACE485916:G1GFV-387-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-UniRule.
DR   GO; GO:0030091; P:protein repair; IEA:InterPro.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   Gene3D; 3.30.1060.10; -; 1.
DR   HAMAP; MF_01401; MsrA; 1.
DR   HAMAP; MF_01400; MsrB; 1.
DR   InterPro; IPR028427; Met_Sox_Rdtase.
DR   InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
DR   InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR   InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
DR   InterPro; IPR011057; Mss4-like_sf.
DR   PANTHER; PTHR10173; PTHR10173; 1.
DR   Pfam; PF01625; PMSR; 1.
DR   Pfam; PF01641; SelR; 1.
DR   SUPFAM; SSF51316; SSF51316; 1.
DR   SUPFAM; SSF55068; SSF55068; 1.
DR   TIGRFAMs; TIGR00401; msrA; 1.
DR   TIGRFAMs; TIGR00357; TIGR00357; 1.
DR   PROSITE; PS51790; MSRB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W4X0.
DR   SWISS-2DPAGE; C8W4X0.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01400,
KW   ECO:0000256|SAAS:SAAS00102831, ECO:0000313|EMBL:ACV61322.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT   DOMAIN      187    309       MsrB. {ECO:0000259|PROSITE:PS51790}.
FT   ACT_SITE     19     19       {ECO:0000256|HAMAP-Rule:MF_01401}.
FT   ACT_SITE    298    298       Nucleophile. {ECO:0000256|HAMAP-Rule:
FT                                MF_01400}.
SQ   SEQUENCE   328 AA;  37887 MW;  C888226A6AE17739 CRC64;
     MKDSIDLGRD EFATFAGGCF WCMVRAFQET AGVADVISGY TGGCKENPTY EEVCTHTTGH
     YEAVQVRFNP VVVSYEKLLE VFWRQIDPTD PGGQFFDRGS PYQTAIFYHN EEQKQQAESS
     KKALIESNRF DKPVVTLILP AATFFPAEEY HQDYHQKNPL HYNQYRRSSG RDAFIEKYWE
     DKRSKDKEPL KQRLTKLQYE VTQNNATEPP FRNEYWDNQR EGIYVDIVSG EPLFSSIDKF
     NSGCGWPSFA KPLNAKNIKE EIDLSHGMKR TEVRSQAVDS HLGHVFQDGP TPTGLRYCIN
     SAALRFIPKE NLLKEGYDEY LSLFNFER
//

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