TRXB_HAEIN
ID TRXB_HAEIN Reviewed; 318 AA.
AC P43788;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Thioredoxin reductase;
DE Short=TRXR;
DE EC=1.8.1.9;
GN Name=trxB; OrderedLocusNames=HI_1158;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-dithiol + NADP(+) = [thioredoxin]-disulfide +
CC H(+) + NADPH; Xref=Rhea:RHEA:20345, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.8.1.9;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P0A9P4};
CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond.
CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; L42023; AAC22813.1; -; Genomic_DNA.
DR PIR; G64186; G64186.
DR RefSeq; NP_439316.1; NC_000907.1.
DR RefSeq; WP_005693473.1; NC_000907.1.
DR PDB; 5U63; X-ray; 1.99 A; A/B=1-318.
DR PDBsum; 5U63; -.
DR AlphaFoldDB; P43788; -.
DR SMR; P43788; -.
DR STRING; 71421.HI_1158; -.
DR EnsemblBacteria; AAC22813; AAC22813; HI_1158.
DR KEGG; hin:HI_1158; -.
DR PATRIC; fig|71421.8.peg.1209; -.
DR eggNOG; COG0492; Bacteria.
DR HOGENOM; CLU_031864_5_1_6; -.
DR OMA; FRAEDYW; -.
DR PhylomeDB; P43788; -.
DR BioCyc; HINF71421:G1GJ1-1192-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central.
DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS.
DR InterPro; IPR005982; Thioredox_Rdtase.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01292; TRX_reduct; 1.
DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP;
KW Oxidoreductase; Redox-active center; Reference proteome.
FT CHAIN 1..318
FT /note="Thioredoxin reductase"
FT /id="PRO_0000166732"
FT BINDING 36..43
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT BINDING 286..295
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT DISULFID 136..139
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:P0A9P4"
FT STRAND 5..12
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 91..101
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:5U63"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 156..166
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 215..225
FT /evidence="ECO:0007829|PDB:5U63"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 237..241
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:5U63"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:5U63"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 285..288
FT /evidence="ECO:0007829|PDB:5U63"
FT HELIX 295..315
FT /evidence="ECO:0007829|PDB:5U63"
SQ SEQUENCE 318 AA; 34395 MW; 2BAEBC5DDE6020AA CRC64;
MSDIKHAKLL ILGSGPAGYT AAIYAARANL KPVLVTGLQQ GGQLTTTDEI ENWPGDFEMT
TGSGLMQRML QHAEKFETEI VFDHINRVDL SSRPFKLFGD VQNFTCDALI IATGASARYI
GLPSEENYKG RGVSACATCD GFFYRNKPVG VIGGGNTAVE EALYLANIAS TVHLIHRRDS
FRAEKILIDR LYKKVEEGKI VLHTDRTLDE VLGDNMGVTG LRLANTKTGE KEELKLDGLF
VAIGHSPNTE IFQGQLELNN GYIVVKSGLD GNATATSVEG VFAAGDVMDH NYRQAITSAG
TGCMAALDAE RYLDAQEA
