MSRAB_NEIMB
ID MSRAB_NEIMB Reviewed; 522 AA.
AC Q9K1N8;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB;
DE Includes:
DE RecName: Full=Thioredoxin;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrA;
DE Short=Protein-methionine-S-oxide reductase;
DE EC=1.8.4.11;
DE AltName: Full=Peptide-methionine (S)-S-oxide reductase;
DE Short=Peptide Met(O) reductase;
DE Includes:
DE RecName: Full=Peptide methionine sulfoxide reductase MsrB;
DE EC=1.8.4.12;
DE AltName: Full=Peptide-methionine (R)-S-oxide reductase;
GN Name=msrAB; Synonyms=pilB; OrderedLocusNames=NMB0044;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation. Catalyzes the reversible
CC oxidation-reduction of methionine sulfoxide in proteins to methionine
CC (By similarity). {ECO:0000250}.
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-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:44120,
CC ChEBI:CHEBI:50058; EC=1.8.4.11;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-
CC dithiol + L-methionine (S)-S-oxide; Xref=Rhea:RHEA:19993, Rhea:RHEA-
CC COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:50058, ChEBI:CHEBI:57844,
CC ChEBI:CHEBI:58772; EC=1.8.4.11;
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-COMP:10700,
CC Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12314, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHEBI:45764,
CC ChEBI:CHEBI:50058; EC=1.8.4.12;
CC -!- DOMAIN: Possesses 2 methionine sulfoxide reductase domains (A/MsrA and
CC B/MsrB) and 1 N-terminal thioredoxin domain. The domain B exhibits a
CC thioredoxin dependent methionine sulfoxide reductase activity; the Cys-
CC 495 is probably involved in the reduction of MetSO and in formation of
CC the sulfenic acid derivative. The regeneration of Cys-495 is probably
CC done via formation of a disulfide bond with Cys-440 followed by its
CC reduction by thioredoxin.
CC -!- SIMILARITY: In the N-terminal section; belongs to the thioredoxin
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the central section; belongs to the MsrA Met sulfoxide
CC reductase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
CC sulfoxide reductase family. {ECO:0000305}.
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DR EMBL; AE002098; AAF40515.1; -; Genomic_DNA.
DR PIR; G81243; G81243.
DR RefSeq; NP_273110.1; NC_003112.2.
DR RefSeq; WP_010980745.1; NC_003112.2.
DR AlphaFoldDB; Q9K1N8; -.
DR BMRB; Q9K1N8; -.
DR SMR; Q9K1N8; -.
DR STRING; 122586.NMB0044; -.
DR PaxDb; Q9K1N8; -.
DR EnsemblBacteria; AAF40515; AAF40515; NMB0044.
DR KEGG; nme:NMB0044; -.
DR PATRIC; fig|122586.8.peg.59; -.
DR HOGENOM; CLU_031040_11_0_4; -.
DR OMA; EHDDFSF; -.
DR Proteomes; UP000000425; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0036456; F:L-methionine-(S)-S-oxide reductase activity; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR GO; GO:0030091; P:protein repair; IEA:InterPro.
DR Gene3D; 3.30.1060.10; -; 1.
DR HAMAP; MF_01401; MsrA; 1.
DR HAMAP; MF_01400; MsrB; 1.
DR InterPro; IPR002569; Met_Sox_Rdtase_MsrA_dom.
DR InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
DR InterPro; IPR028427; Met_Sox_Rdtase_MsrB.
DR InterPro; IPR002579; Met_Sox_Rdtase_MsrB_dom.
DR InterPro; IPR011057; Mss4-like_sf.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR10173; PTHR10173; 1.
DR Pfam; PF01625; PMSR; 1.
DR Pfam; PF08534; Redoxin; 1.
DR Pfam; PF01641; SelR; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF55068; SSF55068; 1.
DR TIGRFAMs; TIGR00401; msrA; 1.
DR TIGRFAMs; TIGR00357; TIGR00357; 1.
DR PROSITE; PS51790; MSRB; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Electron transport; Multifunctional enzyme; Oxidoreductase;
KW Redox-active center; Reference proteome; Transport.
FT CHAIN 1..522
FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB"
FT /id="PRO_0000138510"
FT DOMAIN 17..174
FT /note="Thioredoxin"
FT DOMAIN 383..506
FT /note="MsrB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT REGION 199..354
FT /note="Peptide methionine sulfoxide reductase A"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 495
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01126"
FT DISULFID 68..71
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 440..495
FT /evidence="ECO:0000250"
SQ SEQUENCE 522 AA; 58015 MW; 535A823EDB76BFD1 CRC64;
MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS VYLKKDKPTL
IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF LHEKKDGDFQ KWYAGLNYPK
LPVVTDNGGT IAQSLNISVY PSWALIGKDS DVQRIVKGSI NEAQALALIR DPNADLGSLK
HSFYKPDTQK KDSKIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTKNPSYED
VSYRHTGHAE TVKVTYDADK LSLDDILQYF FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA
EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL
PGKTKTAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY
VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SYNMRRTEVR SHAADSHLGH
VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKGK VK
