ID   1.11.1.28
DE   lipoyl-dependent peroxiredoxin.
CA   a hydroperoxide + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[lipoyl-carrier
CA   protein] = an alcohol + H2O + N(6)-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier
CA   protein].
CC   -!- Peroxiredoxins (Prxs) are a ubiquitous family of antioxidant
CC       proteins.
CC   -!- They can be divided into three classes: typical 2-Cys, atypical 2-Cys
CC       and 1-Cys peroxiredoxins.
CC   -!- The peroxidase reaction comprises two steps centered around a redox-
CC       active cysteine called the peroxidatic cysteine.
CC   -!- All three peroxiredoxin classes have the first step in common,
CC       in which the peroxidatic cysteine attacks the peroxide substrate and
CC       is oxidized to S-hydroxycysteine (a sulfenic acid).
CC   -!- The second step of the peroxidase reaction, the regeneration of
CC       cysteine from S-hydroxycysteine, distinguishes the three
CC       peroxiredoxin classes.
CC   -!- For typical 2-Cys Prxs, in the second step, the peroxidatic
CC       S-hydroxycysteine from one subunit is attacked by the 'resolving'
CC       cysteine located in the C-terminus of the second subunit, to form an
CC       intersubunit disulfide bond, which is then reduced by one of several
CC       cell-specific thiol-containing reductants completing the catalytic
CC       cycle.
CC   -!- In the atypical 2-Cys Prxs, both the peroxidatic cysteine and its
CC       resolving cysteine are in the same polypeptide, so their reaction
CC       forms an intrachain disulfide bond.
CC   -!- The 1-Cys Prxs conserve only the peroxidatic cysteine, so its
CC       regeneration involves direct interaction with a reductant molecule.
CC   -!- Two types of lipoyl-dependent peroxiredoxins have been reported from
CC       bacteria.
CC   -!- One type is the AhpC/AhpD system, originally described from
CC       Mycobacterium tuberculosis.
CC   -!- In that system, AhpC catalyzes reduction of the substrate, resulting
CC       in an intramolecular disulfide.
CC   -!- AhpD then forms an intermolecular disulfide cross-link with AhpC,
CC       reducing it back to active state.
CC   -!- AhpD is reduced in turn by lipoylated proteins.
CC   -!- The second type, which has been characterized in Xylella fastidiosa,
CC       consists of only one type of subunit, which interacts directly with
CC       lipoylated proteins.
CC   -!- Formerly EC 1.11.1.15.
DR   A0R1V9, AHPC_MYCS2 ;  P9WQB6, AHPC_MYCTO ;  P9WQB7, AHPC_MYCTU ;
DR   C1F4K1, AHPD_ACIC5 ;  B8J9Z2, AHPD_ANAD2 ;  Q2IMQ8, AHPD_ANADE ;
DR   A7HCA3, AHPD_ANADF ;  B4UA87, AHPD_ANASK ;  A8HQP5, AHPD_AZOC5 ;
DR   B2IHZ4, AHPD_BEII9 ;  Q9ANL0, AHPD_BRADU ;  A5ENR3, AHPD_BRASB ;
DR   A4YYT0, AHPD_BRASO ;  B2SAW2, AHPD_BRUA1 ;  Q2YKW2, AHPD_BRUA2 ;
DR   A6X5N3, AHPD_BRUA4 ;  Q578J2, AHPD_BRUAB ;  A9MBZ4, AHPD_BRUC2 ;
DR   Q8YCF2, AHPD_BRUME ;  A9WZ04, AHPD_BRUSI ;  Q8FVW4, AHPD_BRUSU ;
DR   Q9A268, AHPD_CAUVC ;  B8GVX4, AHPD_CAUVN ;  C3PGV9, AHPD_CORA7 ;
DR   Q6NGT4, AHPD_CORDI ;  C4LJ26, AHPD_CORK4 ;  B6IZ19, AHPD_COXB2 ;
DR   A9KBI4, AHPD_COXBN ;  A9N917, AHPD_COXBR ;  Q83BM5, AHPD_COXBU ;
DR   Q0RH96, AHPD_FRAAA ;  A8L1J2, AHPD_FRASN ;  A9H8D2, AHPD_GLUDA ;
DR   Q0BUC5, AHPD_GRABC ;  Q0BXT2, AHPD_HYPNA ;  Q1IJ49, AHPD_KORVE ;
DR   Q0AKM4, AHPD_MARMM ;  B0UAJ8, AHPD_METS4 ;  B8EJZ2, AHPD_METSB ;
DR   A0QGI9, AHPD_MYCA1 ;  B1MJX0, AHPD_MYCA9 ;  P0A5N5, AHPD_MYCBO ;
DR   A1KLC4, AHPD_MYCBP ;  C1AQZ5, AHPD_MYCBT ;  B2HD59, AHPD_MYCMM ;
DR   Q73ZL4, AHPD_MYCPA ;  Q50441, AHPD_MYCS2 ;  A5U5C5, AHPD_MYCTA ;
DR   P9WQB4, AHPD_MYCTO ;  P9WQB5, AHPD_MYCTU ;  A0PSD4, AHPD_MYCUA ;
DR   Q5YT53, AHPD_NOCFA ;  A5VCB6, AHPD_RHIWR ;  B6IQZ3, AHPD_RHOCS ;
DR   C0ZYQ9, AHPD_RHOE4 ;  Q07I00, AHPD_RHOP5 ;  Q20Y19, AHPD_RHOPB ;
DR   Q02BZ5, AHPD_SOLUE ;  Q82IC5, AHPD_STRAW ;  Q7AKI6, AHPD_STRCO ;
DR   B1W2G7, AHPD_STRGG ;  Q9X5V1, AHPD_STRVD ;
//