Reviewed, UniProtKB/Swiss-Prot P52213 (TRXB_CLOLI)

Names and origin

Protein names

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

Gene names

Name:

trxB

Organism

Clostridium litorale (Bacterium W6)

Taxonomic identifier

1557 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	315 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
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 – 315	315	Thioredoxin reductase		PRO_0000166727
Regions
	Nucleotide binding	34 – 41	8	FAD By similarity
	Nucleotide binding	282 – 291	10	FAD By similarity
Amino acid modifications
	Disulfide bond	134 ↔ 137		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P52213-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 2CA55D36E579E2EF	FASTA	315	33,946
	10 20 30 40 50 60 MENVYDIAII GSGPAGLAAA LYGARAKMKT LLLEGMKVGG QIVITHEVAN YPGSVPEATG 70 80 90 100 110 120 PSLIGRMEEQ VEEFGAERVM DNIVDVDFTD KIKVLKGAKG EYKAKAVIVA TGASPKLAGC 130 140 150 160 170 180 PGEKELTGKG VSYCATCDAD FFEDMEVFVI GGGDTAVEEA MFLTKFARKV TIVHRRAELR 190 200 210 220 230 240 AAKSIQEKAF KNEKLNFMWN TVIEEIKGDG IVESAVFKNR ETGEVTEFVA PEEDGTFGIF 250 260 270 280 290 300 VFIGYDPKSA LVEGKLELDE TGYIPTDDNM KTNVEGVFAA GDIRVKSLRQ VVTATADGAI 310 AAVQAEKYIE ELFAE

References

[1]

"Glycine reductase of Clostridium litorale. Cloning, sequencing, and molecular analysis of the grdAB operon that contains two in-frame TGA codons for selenium incorporation." Kreimer S., Andreesen J.R. Eur. J. Biochem. 234:192-199(1995) [PubMed: 8529640] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	U24268 Genomic DNA. Translation: AAC43575.1.
PIR	S63990.
3D structure databases
HSSP	HSSP built from PDB template 1VDC based on UniProtKB Q39243.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.9. 266700.
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_CLOLI

Accession

Primary (citable) accession number: P52213

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 58 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)