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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Z2491 / Serogroup A / Serotype 4A;
DOI=10.1038/35006655; PubMed=10761919 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[2]
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IDENTIFICATION OF THE METHIONINE SULFOXIDE REDUCTASE ACTIVITIES (MSRA AND MSRB).
STRAIN=Z2491 / Serogroup A / Serotype 4A;
DOI=10.1074/jbc.M112350200; PubMed=11812798 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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- 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.
- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.
- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H2O = 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.
- SIMILARITY: In the central section; belongs to the msrA Met sulfoxide reductase family.
- SIMILARITY: In the C-terminal section; belongs to the msrB Met sulfoxide reductase family.
- SIMILARITY: Contains 1 thioredoxin domain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 522 AA [This is the length of the unprocessed precursor] |
Molecular weight: 58015 Da [This is the MW of the unprocessed precursor] |
CRC64: F61E8EA7189F0667 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKHRTFFSLC AKFGCLLALG ACSPKIVDAG AATVPHTLST LKTADNRPAS VYLKKDKPTL
70 80 90 100 110 120
IKFWASWCPL CLSELGQTEK WAQDAKFSSA NLITVASPGF LHEKKDGDFQ KWYAGLNYPK
130 140 150 160 170 180
LPVVTDNGGT IAQSLNISVY PSWALIGKDG DVQRIVKGSI NEAQALALIR DPNADLGSLK
190 200 210 220 230 240
HSFYKPDTQK KDSKIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTKNPSYED
250 260 270 280 290 300
VSYRHTGHAE TVKVTYDADK LSLDDILQYF FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA
310 320 330 340 350 360
EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL
370 380 390 400 410 420
PGKTKTAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY
430 440 450 460 470 480
VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SYNMRRTEVR SHAADSHLGH
490 500 510 520
VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKSK VK
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Q9JWM8 in FASTA format |
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