Reviewed, UniProtKB/Swiss-Prot P80880 (TRXB_BACSU)

Names and origin

Protein names

Recommended name:
    Thioredoxin reductase
      Short name=TRXR
    EC=1.8.1.9
Alternative name(s):
    General stress protein 35
      Short name=GSP35

Gene names

Name:	trxB
Synonyms:	yvcH
Ordered Locus Names:	BSU34790

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	316 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)

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.
Induction	By heat shock, salt stress, oxidative stress, glucose limitation and oxygen limitation.
Miscellaneous	The active site is a redox-active disulfide bond By similarity.
Sequence similarities	Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Cytoplasm
Domain	Redox-active center
Ligand	FAD Flavoprotein NADP
Molecular function	Oxidoreductase
PTM	Disulfide bond
Technical term	Complete proteome 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 response to stress Inferred from electronic annotation. Source: UniProtKB-KW
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 Ref.3
	Chain	2 – 316	315	Thioredoxin reductase		PRO_0000166719
Regions
	Nucleotide binding	36 – 43	8	FAD By similarity
	Nucleotide binding	278 – 287	10	FAD By similarity
Amino acid modifications
	Disulfide bond	135 ↔ 138		Redox-active By similarity
Experimental info
	Sequence conflict	2	1	S → A AA sequence Ref.3
	Sequence conflict	7	1	Y → E AA sequence Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P80880-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 9A14AC9E75A3F0AC	FASTA	316	34,519
	10 20 30 40 50 60 MSEEKIYDVI IIGAGPAGMT AAVYTSRANL STLMIERGIP GGQMANTEDV ENYPGFESIL 70 80 90 100 110 120 GPELSNKMFE HAKKFGAEYA YGDIKEVIDG KEYKVVKAGS KEYKARAVII AAGAEYKKIG 130 140 150 160 170 180 VPGEKELGGR GVSYCAVCDG AFFKGKELVV VGGGDSAVEE GVYLTRFASK VTIVHRRDKL 190 200 210 220 230 240 RAQSILQARA FDNEKVDFLW NKTVKEIHEE NGKVGNVTLV DTVTGEESEF KTDGVFIYIG 250 260 270 280 290 300 MLPLSKPFEN LGITNEEGYI ETNDRMETKV EGIFAAGDIR EKSLRQIVTA TGDGSIAAQS 310 VQHYVEELQE TLKTLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Denizot F. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[2]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[3]	"First steps from a two-dimensional protein index towards a response-regulation map for Bacillus subtilis." Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M. Electrophoresis 18:1451-1463(1997) [PubMed: 9298659] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-24. Strain: 168 / IS58.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z94043 Genomic DNA. Translation: CAB08055.1. AL009126 Genomic DNA. Translation: CAB15484.1.
PIR	A69727.
RefSeq	NP_391359.1.
3D structure databases
HSSP	HSSP built from PDB template 1VDC based on UniProtKB Q39243.
ModBase	Search...
Genome annotation databases
GeneID	936549.
GenomeReviews	Gene locus BSU34790 in contig AL009126_GR.
KEGG	bsu:BSU34790.
NMPDR	fig|224308.1.peg.3485.
Organism-specific databases
SubtiList	BG12398. trxB. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P80880.
OMA	P80880. AIYARRA.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU3476-MON.
BRENDA	1.8.1.9. 150.
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_BACSU

Accession

Primary (citable) accession number: P80880
Secondary accession number(s): O06971

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 75 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)