(data stored in SCRATCH zone)

HOGENOM: CHLT1_1_PE103

ID   CHLT1_1_PE103                        STANDARD;      PRT;   351 AA.
AC   CHLT1_1_PE103; D6YPC7;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Thioredoxin reductase; EC=1.8.1 9; (CHLT1_1.PE103).
GN   OrderedLocusNames=E11023_00515;
OS   CHLAMYDIA TRACHOMATIS E/11023.
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae; Chlamydia.
OX   NCBI_TaxID=707183;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS CHLT1_1.PE103.
CC       Chlamydia trachomatis (serovar E, strain E/11023) chromosome, complete
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D6YPC7_CHLT1
CC   -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide
CC       + NADPH.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC       oxidoreductase family.
CC   -!- GENE_FAMILY: HOG000072912 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; D6YPC7; -.
DR   EMBL; CP001890; ADH20557.1; -; Genomic_DNA.
DR   ProteinModelPortal; D6YPC7; -.
DR   GenomeReviews; CP001890_GR; E11023_00515.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:EC.
DR   GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR   InterPro; IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD-bd_dom.
DR   InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
DR   InterPro; IPR005982; Thioredox_Rdtase.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR   PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
DR   HOGENOMDNA; CHLT1_1.PE103; -.
KW   ADH20557.100024376fold_1320000031;
KW   Thioredoxin reductase;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase;
KW   Redox-active center.
SQ   SEQUENCE   351 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MNVVCGKSRV GYSSFFCKSR EPFSCVFKAL LSKFILGVPM THAKLVIIGS GPAGYTAAIY
     ASRALLTPVL FEGFFSGIAG GQLMTTTEVE NFPGFPEGVL GHQLMDLMKT QAQRFGTQVL
     SKDITAVDFS VRPFVLKSGE ETFTCDACII ATGASAKRLS IPGAGDNEFW QKGVTACAVC
     DGASPIFRDK DLFVVGGGDS ALEEAMFLTR YGKRVFVVHR RDTLRASKVM VNKAQANEKI
     FFLWNSEIVK ISGDTLVRSI DIYNNVDKTT TTMEAAGVFF AIGHQPNTAF LGGQVALDEN
     GYIITEKGSS RTSVPGVFAA GDVQDKYYRQ AITSAGSGCM AALDAERFLE N
//

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