(data stored in SCRATCH3701 zone)

HOGENOM6: XAORY1_1_PE2130

ID   XAORY1_1_PE2130                      STANDARD;      PRT;   898 AA.
AC   XAORY1_1_PE2130; Q2P2R6;
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; (XAORY1_1.PE2130).
GN   OrderedLocusNames=XOO2406;
OS   XANTHOMONAS ORYZAE PV. ORYZAE KACC10331.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=291331;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS XAORY1_1.PE2130.
CC       Xanthomonas oryzae pv. oryzae KACC10331 chromosome, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q2P2R6_XANOM
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: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q2P2R6; -.
DR   EMBL; AP008229; BAE69161.1; -; Genomic_DNA.
DR   RefSeq; YP_451435.1; NC_007705.1.
DR   ProteinModelPortal; Q2P2R6; -.
DR   SMR; Q2P2R6; 10-319.
DR   STRING; Q2P2R6; -.
DR   GeneID; 3857076; -.
DR   GenomeReviews; AP008229_GR; XOO2406.
DR   KEGG; xom:XOO_2406; -.
DR   eggNOG; COG0492; -.
DR   OMA; FRSSKIM; -.
DR   PhylomeDB; Q2P2R6; -.
DR   ProtClustDB; CLSK701941; -.
DR   BioCyc; XORY342109:XOO2406-MONOMER; -.
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; XAORY1_1.PE2130; -.
DR   PRODOM; XAORY1_1_PE2130.
DR   SWISS-2DPAGE; XAORY1_1_PE2130.
KW   DNA gyrase subunit A;
KW   Complete proteome; FAD; Flavoprotein; Oxidoreductase;
KW   Redox-active center.
SQ   SEQUENCE   898 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MAETAKEIIQ VNLEDEMRKS YLDYAMSVIV GRALPDARDG LKPVHRRVLF AMHELGAHSN
     KAYFKSARIV GDVIGKYHPH GDQSVYDTLV RMAQPFSLRY MMVDGQGNFG SVDGDSAAAM
     RYTESRMSRL AHELMADIDK ETVDFQPNYD EKEQEPTVMP TRFPSLLVNG SAGIAVGMAT
     NIPPHNLTEA INACIALIDT PELDVEGLME YIPGPDFPTA GIINGTAGIA AGYRTGRGRV
     RIRAKADVEV ADNGREAIVV TEIPYQVNKA RLIEKIAELV KEKKLEGISE LRDESDKDGM
     RIYIEIKRGE SAEVVLNNLY QQTQMESVFG INMVALIDGR PQLMNLKQML EAFIRHRREV
     VTRRTIFELR KARARAHVLE GLTVALANID EMIELIKTSA NPQEARERML AKTWQPGLVG
     ALLGAAGAEA SKPEDLPPGV GLIKGFYQLS EVQASQILEM RLHRLTGLEQ EKLTDEYKQL
     LGVIEGLIRI LENPDVLLQV IRDELINIRE EYGDERRTEI RHSEEDLDIL DLIAPEDVVV
     TLSHAGYAKR QPVSAYRAQR RGGRGRSAAA TKEEDFIDQL WLVNTHDTLL TFTSSGKVFW
     LPVHQLPEAG SNARGRPIIN WIPLEAGERV QAVLPVREYV DNRYVFFATR NGTVKKTSLS
     EFAFRLARGK IAINLDEGDA LIGVALTDGD RDVLLFASNG KTVRFGESTV RSMGRTATGV
     RGIRLTKGEE VVSLIVAERA GGADEEIEAD DVDDVVETTD GAETAVIEVA DDGNVAYILT
     ATENGYGKRT PLAEYPRKGR GTQGVIGIQT TERNGKLVRA VLLGATDEVL LISDGGTLVR
     TRGSEISRVG RNTQGVTLIR LSKGEKLQAV ERLDASLDEV EDVAGEAAVA SDTPPADA
//

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