Reviewed, UniProtKB/Swiss-Prot P52215 (TRXB_STRCO)

Names and origin

Protein names

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

Gene names

Name:	trxB
Ordered Locus Names:	SCO3890
ORF Names:	SCH24.12c

Organism

Streptomyces coelicolor [Complete proteome] [HAMAP]

Taxonomic identifier

1902 [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	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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 322	321	Thioredoxin reductase		PRO_0000166753
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
Experimental info
	Sequence conflict	26	1	A → R in CAA63075. Ref.1
	Sequence conflict	26	1	A → R in CAA07451. Ref.1
	Sequence conflict	73 – 74	2	ER → DG in CAA63075. Ref.1
	Sequence conflict	73 – 74	2	ER → DG in CAA07451. Ref.1
	Sequence conflict	155	1	Missing in CAA63075. Ref.1
	Sequence conflict	234	1	G → A in CAA63075. Ref.1
	Sequence conflict	258	1	Missing in CAA63075. Ref.1
	Sequence conflict	300	1	V → L in CAB42713. Ref.3
	Sequence conflict	304	1	P → R in CAB42713. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P52215-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1B337B1742E3C457	FASTA	322	34,156
	10 20 30 40 50 60 MSDVRNVIII GSGPAGYTAA LYTARASLKP LVFEGAVTAG GALMNTTEVE NFPGFQDGIM 70 80 90 100 110 120 GPELMDNMRA QAERFGAELI PDDVVAVDLS GEIKTVTDTA GTVHRAKAVI VTTGSQHRKL 130 140 150 160 170 180 GLPNEDALSG RGVSWCATCD GFFFKDQDIA VIGGGDTAME EATFLSRFAK SVTIVHRRDT 190 200 210 220 230 240 LRASKAMQER AFADPKISFV WDSEVAEVQG DQKLAGLKLR NVKTGELSDL PVTGLFIAIG 250 260 270 280 290 300 HDPRTELFKG QLDLDPEGYL KVDAPSTRTN LTGVFGAGDV VDHTYRQAIT AAGTGCSAAV 310 320 DAEPFLAALS DEDKAEPEKT AV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene organization in the trxA/B-oriC region of the Streptomyces coelicolor chromosome and comparison with other eubacteria." Gal-Mor O., Borovok I., Av-Gay Y., Cohen G., Aharonowitz Y. Gene 217:83-90(1998) [PubMed: 9795152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.
[2]	Aharonowitz Y. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed: 12000953] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X92105 Genomic DNA. Translation: CAA63076.1. X92104 Genomic DNA. Translation: CAA63075.1. AJ007313 Genomic DNA. Translation: CAA07451.1. AL939118 Genomic DNA. Translation: CAB42713.1.
PIR	T36577. T42062.
RefSeq	NP_628076.1.
3D structure databases
HSSP	HSSP built from PDB template 1VDC based on UniProtKB Q39243.
SMR	P52215. Positions 4-307.
ModBase	Search...
Genome annotation databases
GeneID	1099326.
GenomeReviews	Gene locus SCO3890 in contig AL645882_GR.
KEGG	sco:SCO3890.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P52215.
Enzyme and pathway databases
BioCyc	SCOE100226:SCO3890-MON.
BRENDA	1.8.1.9. 1084.
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_STRCO

Accession

Primary (citable) accession number: P52215

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 74 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)