Reviewed, UniProtKB/Swiss-Prot P43788 (TRXB_HAEIN)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase
      Short name=TRXR
    EC=1.8.1.9

Gene names

Name:	trxB
Ordered Locus Names:	HI1158

Organism

Haemophilus influenzae [Complete proteome] [HAMAP]

Taxonomic identifier

727 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length	318 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm By similarity.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW removal of superoxide radicals Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro thioredoxin-disulfide reductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 318	318	Thioredoxin reductase		PRO_0000166732
Regions
	Nucleotide binding	36 – 43	8	FAD By similarity
	Nucleotide binding	286 – 295	10	FAD By similarity
Amino acid modifications
	Disulfide bond	136 ↔ 139		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P43788-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 2BAEBC5DDE6020AA	FASTA	318	34,395
	10 20 30 40 50 60 MSDIKHAKLL ILGSGPAGYT AAIYAARANL KPVLVTGLQQ GGQLTTTDEI ENWPGDFEMT 70 80 90 100 110 120 TGSGLMQRML QHAEKFETEI VFDHINRVDL SSRPFKLFGD VQNFTCDALI IATGASARYI 130 140 150 160 170 180 GLPSEENYKG RGVSACATCD GFFYRNKPVG VIGGGNTAVE EALYLANIAS TVHLIHRRDS 190 200 210 220 230 240 FRAEKILIDR LYKKVEEGKI VLHTDRTLDE VLGDNMGVTG LRLANTKTGE KEELKLDGLF 250 260 270 280 290 300 VAIGHSPNTE IFQGQLELNN GYIVVKSGLD GNATATSVEG VFAAGDVMDH NYRQAITSAG 310 TGCMAALDAE RYLDAQEA

References

[1]

"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C. Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L42023 Genomic DNA. Translation: AAC22813.1.
PIR	G64186.
RefSeq	NP_439316.1.
3D structure databases
HSSP	HSSP built from PDB template 1TRB based on UniProtKB P09625.
SMR	P43788. Positions 5-315.
ModBase	Search...
Genome annotation databases
GeneID	950118.
GenomeReviews	Gene locus HI1158 in contig L42023_GR.
KEGG	hin:HI1158.
NMPDR	fig|71421.1.peg.1111.
TIGR	HI1158.
Phylogenomic databases
HOGENOM	P43788.
OMA	P43788. PSCGPCH.
Enzyme and pathway databases
BioCyc	HINF71421:HI_1158-MON.
BRENDA	1.8.1.9. 109.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR001327. Pyr_OxRdtase_NAD_bd. IPR000103. Pyridine_nuc-diS_OxRdtase_2. IPR005982. Thioredox_Rdtase. [Graphical view]
Pfam	PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. [Graphical view]
PRINTS	PR00368. FADPNR. PR00469. PNDRDTASEII.
ProDom	PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01292. TRX_reduct. 1 hit.
PROSITE	PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXB_HAEIN

Accession

Primary (citable) accession number: P43788

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	June 16, 2009
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)