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Peptide methionine sulfoxide reductase MsrA/MsrB [Includes: Thioredoxin; Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase); Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase)]

 MSRAB_NEIMA             Reviewed;         522 AA.
Q9JWM8; A1IPD1;
02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 125.
RecName: Full=Peptide methionine sulfoxide reductase MsrA/MsrB;
Includes:
RecName: Full=Thioredoxin;
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrA;
Short=Protein-methionine-S-oxide reductase;
EC=1.8.4.11;
AltName: Full=Peptide-methionine (S)-S-oxide reductase;
Short=Peptide Met(O) reductase;
Includes:
RecName: Full=Peptide methionine sulfoxide reductase MsrB;
EC=1.8.4.12;
AltName: Full=Peptide-methionine (R)-S-oxide reductase;
Name=msrAB; Synonyms=pilB; OrderedLocusNames=NMA0290;
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491).
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
Neisseriaceae; Neisseria.
NCBI_TaxID=122587;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Z2491;
PubMed=10761919; DOI=10.1038/35006655;
Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T.,
Davies R.M., Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S.,
Jagels K., Leather S., Moule S., Mungall K.L., Quail M.A.,
Rajandream M.A., Rutherford K.M., Simmonds M., Skelton J.,
Whitehead S., Spratt B.G., Barrell B.G.;
"Complete DNA sequence of a serogroup A strain of Neisseria
meningitidis Z2491.";
Nature 404:502-506(2000).
[2]
IDENTIFICATION OF THE METHIONINE SULFOXIDE REDUCTASE ACTIVITIES (MSRA
AND MSRB).
STRAIN=Z2491;
PubMed=11812798; DOI=10.1074/jbc.M112350200;
Olry A., Boschi-Muller S., Marraud M., Sanglier-Cianferani S.,
van Dorsselaer A., Branlant G.;
"Characterization of the methionine sulfoxide reductase activities of
PILB, a probable virulence factor from Neisseria meningitidis.";
J. Biol. Chem. 277:12016-12022(2002).
-!- FUNCTION: Has an important function as a repair enzyme for
proteins that have been inactivated by oxidation (By similarity).
Catalyzes the reversible oxidation-reduction of methionine
sulfoxide in proteins to methionine. {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin.
-!- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H(2)O =
L-methionine (S)-S-oxide + thioredoxin.
-!- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide +
H(2)O = peptide-L-methionine (R)-S-oxide + thioredoxin.
-!- DOMAIN: Possesses 2 methionine sulfoxide reductase domains (A/MsrA
and B/MsrB) and 1 N-terminal thioredoxin domain. The domain B
exhibits a thioredoxin dependent methionine sulfoxide reductase
activity; the Cys-495 is probably involved in the reduction of
MetSO and in formation of the sulfenic acid derivative. The
regeneration of Cys-495 is probably done via formation of a
disulfide bond with Cys-440 followed by its reduction by
thioredoxin.
-!- MISCELLANEOUS: The domain MsrB is stereospecific for the R isomer
of the sulfoxide of MetSO whereas the domain MsrA is
stereospecific for the S isomer.
-!- SIMILARITY: In the N-terminal section; belongs to the thioredoxin
family. {ECO:0000305}.
-!- SIMILARITY: In the central section; belongs to the MsrA Met
sulfoxide reductase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the MsrB Met
sulfoxide reductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL157959; CAM07595.1; -; Genomic_DNA.
PIR; E82024; E82024.
RefSeq; WP_002216163.1; NC_003116.1.
PDB; 2FY6; X-ray; 1.90 A; A=34-176.
PDB; 2JZR; NMR; -; A=34-176.
PDB; 2JZS; NMR; -; A=34-176.
PDB; 2K9F; NMR; -; A=34-176.
PDB; 3BQE; X-ray; 2.00 A; A=196-389.
PDB; 3BQF; X-ray; 2.24 A; A=196-389.
PDB; 3BQG; X-ray; 2.00 A; A=196-389.
PDB; 3BQH; X-ray; 1.95 A; A=197-389.
PDB; 3HCG; X-ray; 1.82 A; A/B/C/D=377-522.
PDB; 3HCH; X-ray; 2.10 A; A/B=377-522.
PDBsum; 2FY6; -.
PDBsum; 2JZR; -.
PDBsum; 2JZS; -.
PDBsum; 2K9F; -.
PDBsum; 3BQE; -.
PDBsum; 3BQF; -.
PDBsum; 3BQG; -.
PDBsum; 3BQH; -.
PDBsum; 3HCG; -.
PDBsum; 3HCH; -.
ProteinModelPortal; Q9JWM8; -.
SMR; Q9JWM8; -.
EnsemblBacteria; CAM07595; CAM07595; NMA0290.
KEGG; nma:NMA0290; -.
HOGENOM; HOG000243423; -.
KO; K12267; -.
OMA; AQYDITQ; -.
BRENDA; 1.8.4.11; 3593.
BRENDA; 1.8.4.12; 3593.
SABIO-RK; Q9JWM8; -.
EvolutionaryTrace; Q9JWM8; -.
Proteomes; UP000000626; Chromosome.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0033743; F:peptide-methionine (R)-S-oxide reductase activity; IEA:UniProtKB-EC.
GO; GO:0008113; F:peptide-methionine (S)-S-oxide reductase activity; IEA:UniProtKB-EC.
GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
GO; GO:0030091; P:protein repair; IEA:InterPro.
GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
Gene3D; 3.30.1060.10; -; 1.
HAMAP; MF_01401; MsrA; 1.
HAMAP; MF_01400; MsrB; 1.
InterPro; IPR028427; Met_Sox_Rdtase.
InterPro; IPR002569; Met_Sox_Rdtase_MsrA.
InterPro; IPR036509; Met_Sox_Rdtase_MsrA_sf.
InterPro; IPR002579; Met_Sox_Rdtase_MsrB.
InterPro; IPR011057; Mss4-like.
InterPro; IPR013740; Redoxin.
InterPro; IPR036249; Thioredoxin-like_sf.
InterPro; IPR013766; Thioredoxin_domain.
PANTHER; PTHR10173; PTHR10173; 1.
Pfam; PF01625; PMSR; 1.
Pfam; PF08534; Redoxin; 1.
Pfam; PF01641; SelR; 1.
SUPFAM; SSF51316; SSF51316; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF55068; SSF55068; 1.
TIGRFAMs; TIGR00401; msrA; 1.
TIGRFAMs; TIGR00357; TIGR00357; 1.
PROSITE; PS51790; MSRB; 1.
PROSITE; PS51352; THIOREDOXIN_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Electron transport;
Multifunctional enzyme; Oxidoreductase; Redox-active center;
Transport.
CHAIN 1 522 Peptide methionine sulfoxide reductase
MsrA/MsrB.
/FTId=PRO_0000138509.
DOMAIN 17 174 Thioredoxin.
DOMAIN 383 506 MsrB. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
REGION 199 354 Peptide methionine sulfoxide reductase A.
ACT_SITE 207 207 {ECO:0000250}.
ACT_SITE 495 495 Nucleophile. {ECO:0000255|PROSITE-
ProRule:PRU01126}.
DISULFID 68 71 Redox-active. {ECO:0000250}.
DISULFID 440 495 {ECO:0000305}.
HELIX 35 39 {ECO:0000244|PDB:2FY6}.
STRAND 46 48 {ECO:0000244|PDB:2JZR}.
HELIX 49 52 {ECO:0000244|PDB:2FY6}.
STRAND 59 64 {ECO:0000244|PDB:2FY6}.
HELIX 69 72 {ECO:0000244|PDB:2FY6}.
HELIX 75 83 {ECO:0000244|PDB:2FY6}.
HELIX 85 87 {ECO:0000244|PDB:2FY6}.
STRAND 90 96 {ECO:0000244|PDB:2FY6}.
STRAND 100 102 {ECO:0000244|PDB:2JZS}.
HELIX 108 113 {ECO:0000244|PDB:2FY6}.
STRAND 123 125 {ECO:0000244|PDB:2FY6}.
HELIX 130 134 {ECO:0000244|PDB:2FY6}.
STRAND 139 146 {ECO:0000244|PDB:2FY6}.
STRAND 152 158 {ECO:0000244|PDB:2FY6}.
HELIX 162 170 {ECO:0000244|PDB:2FY6}.
STRAND 198 206 {ECO:0000244|PDB:3BQH}.
HELIX 208 216 {ECO:0000244|PDB:3BQH}.
STRAND 221 230 {ECO:0000244|PDB:3BQH}.
STRAND 232 235 {ECO:0000244|PDB:3BQH}.
HELIX 238 243 {ECO:0000244|PDB:3BQH}.
STRAND 249 257 {ECO:0000244|PDB:3BQH}.
TURN 258 260 {ECO:0000244|PDB:3BQH}.
HELIX 263 273 {ECO:0000244|PDB:3BQH}.
HELIX 278 280 {ECO:0000244|PDB:3BQH}.
STRAND 281 283 {ECO:0000244|PDB:3BQH}.
STRAND 285 287 {ECO:0000244|PDB:3BQE}.
HELIX 288 290 {ECO:0000244|PDB:3BQE}.
STRAND 292 298 {ECO:0000244|PDB:3BQH}.
HELIX 299 313 {ECO:0000244|PDB:3BQH}.
STRAND 323 326 {ECO:0000244|PDB:3BQH}.
STRAND 330 332 {ECO:0000244|PDB:3BQH}.
HELIX 335 337 {ECO:0000244|PDB:3BQH}.
HELIX 340 343 {ECO:0000244|PDB:3BQH}.
TURN 355 357 {ECO:0000244|PDB:3BQH}.
HELIX 383 389 {ECO:0000244|PDB:3HCG}.
HELIX 392 400 {ECO:0000244|PDB:3HCG}.
HELIX 410 413 {ECO:0000244|PDB:3HCG}.
STRAND 417 422 {ECO:0000244|PDB:3HCG}.
TURN 423 425 {ECO:0000244|PDB:3HCG}.
STRAND 428 431 {ECO:0000244|PDB:3HCG}.
HELIX 432 434 {ECO:0000244|PDB:3HCG}.
STRAND 439 442 {ECO:0000244|PDB:3HCG}.
STRAND 444 447 {ECO:0000244|PDB:3HCG}.
HELIX 451 453 {ECO:0000244|PDB:3HCG}.
STRAND 454 461 {ECO:0000244|PDB:3HCG}.
STRAND 464 471 {ECO:0000244|PDB:3HCG}.
TURN 472 474 {ECO:0000244|PDB:3HCG}.
STRAND 477 483 {ECO:0000244|PDB:3HCG}.
HELIX 487 489 {ECO:0000244|PDB:3HCG}.
STRAND 493 496 {ECO:0000244|PDB:3HCG}.
HELIX 498 500 {ECO:0000244|PDB:3HCG}.
STRAND 501 505 {ECO:0000244|PDB:3HCG}.
HELIX 506 508 {ECO:0000244|PDB:3HCG}.
HELIX 509 512 {ECO:0000244|PDB:3HCG}.
HELIX 515 520 {ECO:0000244|PDB:3HCG}.
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


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