Reviewed, UniProtKB/Swiss-Prot Q928B5 (TRXB_LISIN)

Names and origin

Protein names

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

Gene names

Name:	trxB
Ordered Locus Names:	lin2621

Organism

Listeria innocua [Complete proteome] [HAMAP]

Taxonomic identifier

1642 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria

Protein attributes

Sequence length	319 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 – 319	319	Thioredoxin reductase		PRO_0000166735
Regions
	Nucleotide binding	37 – 44	8	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)
	Q928B5-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: C77D54A952526CC1	FASTA	319	34,244
	10 20 30 40 50 60 MASEEKIYDV IIIGAGPAGM TAALYTSRAD LDTLMIERGV PGGQMVNTAE VENYPGFDSI 70 80 90 100 110 120 LGPDLSDKML SGAKQFGAEY AYGDIKEVID GKEFKTVTAG SKTYKARAII IATGAEHRKL 130 140 150 160 170 180 GAAGEEELSG RGVSYCAVCD GAFFKNRELV VVGGGDSAVE EGTYLTRYAD KVTIVHRRDK 190 200 210 220 230 240 LRAQQILQDR AFKDEKVDFI WNNTVEEIIG DGKKVTSVKL VSTVDGSESI MPVDGVFIYV 250 260 270 280 290 300 GLVPLTKAFL SLGITDEEGY IVTDEEMRTN LPGIFAAGDV RAKSLRQIVT ATGDGGLAGQ 310 NAQKYVEELK EALEAEAAK

References

[1]

"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262 / Serovar 6a.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL596173 Genomic DNA. Translation: CAC97848.1.
PIR	AH1759.
RefSeq	NP_471951.1.
3D structure databases
HSSP	HSSP built from PDB template 1VDC based on UniProtKB Q39243.
ModBase	Search...
Genome annotation databases
GeneID	1131452.
GenomeReviews	Gene locus lin2621 in contig AL592022_GR.
KEGG	lin:lin2621.
NMPDR	fig|272626.1.peg.2604.
Organism-specific databases
ListiList	LIN02621.
CMR	Search...
Phylogenomic databases
HOGENOM	Q928B5.
OMA	Q928B5. FGGIFIY.
Enzyme and pathway databases
BioCyc	LINN272626:LIN2621-MON.
BRENDA	1.8.1.9. 270396.
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_LISIN

Accession

Primary (citable) accession number: Q928B5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 57 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)