MSRAB_NEIMA
ID MSRAB_NEIMA Reviewed; 522 AA.
AC Q9JWM8; A1IPD1;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
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=NMA0290;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
RN [2]
RP IDENTIFICATION OF THE METHIONINE SULFOXIDE REDUCTASE ACTIVITIES (MSRA AND
RP MSRB).
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=11812798; DOI=10.1074/jbc.m112350200;
RA Olry A., Boschi-Muller S., Marraud M., Sanglier-Cianferani S.,
RA van Dorsselaer A., Branlant G.;
RT "Characterization of the methionine sulfoxide reductase activities of PILB,
RT a probable virulence factor from Neisseria meningitidis.";
RL J. Biol. Chem. 277:12016-12022(2002).
CC -!- FUNCTION: Has an important function as a repair enzyme for proteins
CC that have been inactivated by oxidation (By similarity). Catalyzes the
CC reversible oxidation-reduction of methionine sulfoxide in proteins to
CC methionine. {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 -!- MISCELLANEOUS: The domain MsrB is stereospecific for the R isomer of
CC the sulfoxide of MetSO whereas the domain MsrA is stereospecific for
CC the S isomer.
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; AL157959; CAM07595.1; -; Genomic_DNA.
DR PIR; E82024; E82024.
DR RefSeq; WP_002216163.1; NC_003116.1.
DR PDB; 2FY6; X-ray; 1.90 A; A=34-176.
DR PDB; 2JZR; NMR; -; A=34-176.
DR PDB; 2JZS; NMR; -; A=34-176.
DR PDB; 2K9F; NMR; -; A=34-176.
DR PDB; 3BQE; X-ray; 2.00 A; A=196-389.
DR PDB; 3BQF; X-ray; 2.24 A; A=196-389.
DR PDB; 3BQG; X-ray; 2.00 A; A=196-389.
DR PDB; 3BQH; X-ray; 1.95 A; A=197-389.
DR PDB; 3HCG; X-ray; 1.82 A; A/B/C/D=377-522.
DR PDB; 3HCH; X-ray; 2.10 A; A/B=377-522.
DR PDBsum; 2FY6; -.
DR PDBsum; 2JZR; -.
DR PDBsum; 2JZS; -.
DR PDBsum; 2K9F; -.
DR PDBsum; 3BQE; -.
DR PDBsum; 3BQF; -.
DR PDBsum; 3BQG; -.
DR PDBsum; 3BQH; -.
DR PDBsum; 3HCG; -.
DR PDBsum; 3HCH; -.
DR AlphaFoldDB; Q9JWM8; -.
DR BMRB; Q9JWM8; -.
DR SMR; Q9JWM8; -.
DR EnsemblBacteria; CAM07595; CAM07595; NMA0290.
DR GeneID; 61282366; -.
DR KEGG; nma:NMA0290; -.
DR HOGENOM; CLU_031040_11_0_4; -.
DR OMA; EHDDFSF; -.
DR BioCyc; NMEN122587:NMA_RS01530-MON; -.
DR BRENDA; 1.8.4.11; 3593.
DR BRENDA; 1.8.4.12; 3593.
DR SABIO-RK; Q9JWM8; -.
DR EvolutionaryTrace; Q9JWM8; -.
DR Proteomes; UP000000626; Chromosome.
DR GO; GO:0033744; F:L-methionine:thioredoxin-disulfide S-oxidoreductase activity; IEA:RHEA.
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: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; 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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Electron transport; Multifunctional enzyme;
KW Oxidoreductase; Redox-active center; Transport.
FT CHAIN 1..522
FT /note="Peptide methionine sulfoxide reductase MsrA/MsrB"
FT /id="PRO_0000138509"
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:0000305"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2JZR"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:2FY6"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2FY6"
FT HELIX 75..83
FT /evidence="ECO:0007829|PDB:2FY6"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2JZS"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2FY6"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:2FY6"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:2FY6"
FT STRAND 198..206
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:3BQH"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:3BQH"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 238..243
FT /evidence="ECO:0007829|PDB:3BQH"
FT STRAND 249..257
FT /evidence="ECO:0007829|PDB:3BQH"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 263..273
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:3BQH"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:3BQH"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:3BQE"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3BQE"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 299..313
FT /evidence="ECO:0007829|PDB:3BQH"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:3BQH"
FT STRAND 330..332
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:3BQH"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:3BQH"
FT HELIX 383..389
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 392..400
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:3HCG"
FT TURN 423..425
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 432..434
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 454..461
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:3HCG"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 487..489
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 493..496
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 498..500
FT /evidence="ECO:0007829|PDB:3HCG"
FT STRAND 501..505
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 509..512
FT /evidence="ECO:0007829|PDB:3HCG"
FT HELIX 515..520
FT /evidence="ECO:0007829|PDB:3HCG"
SQ SEQUENCE 522 AA; 58015 MW; F61E8EA7189F0667 CRC64;
MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS VYLKKDKPTL
IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF LHEKKDGDFQ KWYAGLNYPK
LPVVTDNGGT IAQSLNISVY PSWALIGKDG 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 AAGYGALKSK VK
