Reviewed, UniProtKB/Swiss-Prot Q05741 (TRXB_STRCL)

Names and origin

Protein names

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

Gene names

Name:

trxB

Organism

Streptomyces clavuligerus

Taxonomic identifier

1901 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the thioredoxin-thioredoxin reductase system which may be involved in biosynthesis of penicillins and cephalosporins and may be important in determining the thiol-disulfide redox balance.
Catalytic activity	Thioredoxin + NADP+ = thioredoxin disulfide + NADPH.
Cofactor	Binds 1 FAD per subunit By similarity.
Subunit structure	Homodimer.
Miscellaneous	The active site is a redox-active disulfide bond.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Direct protein sequencing
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: InterPro
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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 322	321	Thioredoxin reductase		PRO_0000166752
Regions
	Nucleotide binding	34 – 42	9	FAD By similarity
	Nucleotide binding	279 – 288	10	FAD By similarity
Amino acid modifications
	Disulfide bond	136 ↔ 139		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q05741-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 6D9AE0EBF43A8E26	FASTA	322	34,146
	10 20 30 40 50 60 MSDVRNVIII GSGPAGYTAA LYTARASLQP LVFEGAVTAG GALMNTTDVE NFPGFRDGIM 70 80 90 100 110 120 GPDLMDNMRA QAERFGAELI PDDVVSVDLT GDIKTVTDSA GTVHRAKAVI VTTGSQHRKL 130 140 150 160 170 180 GLPREDALSG RGVSWCATCD GFFFKDQDIV VVGGGDTAME EATFLSRFAK SVTIVHRRDS 190 200 210 220 230 240 LRASKAMQDR AFADPKISFA WNSEVATIHG EQKLTGLTLR DTKTGETREL AATGLFIAVG 250 260 270 280 290 300 HDPRTELFKG QLDLDDEGYL KVASPSTRTN LTGVFAAGDV VDHTYRQAIT AAGTGCSAAL 310 320 DAERYLAALA DSEQIAEPAP AV

References

[1]

"Thioredoxin-thioredoxin reductase system of Streptomyces clavuligerus: sequences, expression, and organization of the genes." Cohen G., Yanko M., Mislovati M., Argaman A., Schreiber R., Av-Gay Y., Aharonowitz Y. J. Bacteriol. 175:5159-5167(1993) [PubMed: 8349555] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-33. Strain: ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585.

[2]

"Characterization of a broad-range disulfide reductase from Streptomyces clavuligerus and its possible role in beta-lactam antibiotic biosynthesis." Aharonowitz Y., Av-Gay Y., Schreiber R., Cohen G. J. Bacteriol. 175:623-629(1993) [PubMed: 8423136] [Abstract] Cited for: CHARACTERIZATION. Strain: ATCC 27064 / DSM 738 / IFO 13307 / JCM 4710 / NRRL 3585.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z21946 Genomic DNA. Translation: CAA79940.1.
PIR	A53307.
3D structure databases
HSSP	HSSP built from PDB template 1CL0 based on UniProtKB P09625.
SMR	Q05741. Positions 4-310.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.8.1.9. 229786.
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_STRCL

Accession

Primary (citable) accession number: Q05741

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	September 22, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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