Reviewed, UniProtKB/Swiss-Prot P94284 (TRXB_BORBU)

Names and origin

Protein names

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

Gene names

Name:	trxB
Ordered Locus Names:	BB_0515

Organism

Borrelia burgdorferi (Lyme disease spirochete) [Complete proteome] [HAMAP]

Taxonomic identifier

139 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	326 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 – 326	326	Thioredoxin reductase		PRO_0000166720
Regions
	Nucleotide binding	55 – 62	8	FAD By similarity
	Nucleotide binding	298 – 307	10	FAD By similarity
Amino acid modifications
	Disulfide bond	156 ↔ 159		Redox-active By similarity
Experimental info
	Sequence conflict	303	1	L → P in AAB41020. Ref.1
	Sequence conflict	315 – 326	12	FIASV…GNFLK → LLHLLS in AAB41020. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P94284-1 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: E0F5AC6ACFFFFF3B	FASTA	326	35,673
	10 20 30 40 50 60 MLEFETIDIN LTKKKNLSQK EVDFIEDVII VGSGPAGLTA GIYSVMSNYK AAILEGPEPG 70 80 90 100 110 120 GQLTTTTEVY NYPGFKNGIS GRNLMLNMRE QVVNLGAKTF PETVFSIKRK GNIFYLYTEN 130 140 150 160 170 180 YIYKSKAVII AVGSKPKKLE TLKNSGLFWN KGISVCAICD GHLFKGKRVA VIGGGNTALS 190 200 210 220 230 240 ESIYLSKLVD KVYLIVRKNN LRAIAMLRDS VAKLPNIEIL YNSEAIEVDG KSSVSSVKIF 250 260 270 280 290 300 NKKDNVVYEL EVSAVFMAVG YKPNTEFLKG FLDLDEEGFI VTKDVVKTSV DGVFSCGDVS 310 320 NKLYAQAITA AAEGFIASVE LGNFLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phenylalanyl-tRNA synthetase genes (alpha and beta subunits) and thioredoxin reductase gene of Borrelia burgdorferi." Barbour A.G., Hinnebusch J. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.
[2]	"Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi." Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A., Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J. , Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B., Smith H.O., Venter J.C. Nature 390:580-586(1997) [PubMed: 9403685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 35210 / B31 / CIP 102532 / DSM 4680.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U82978 Genomic DNA. Translation: AAB41020.1. AE000783 Genomic DNA. Translation: AAC66890.1.
PIR	B70164.
RefSeq	NP_212649.1.
3D structure databases
HSSP	HSSP built from PDB template 1VDC based on UniProtKB Q39243.
ModBase	Search...
Genome annotation databases
GeneID	1195361.
GenomeReviews	Gene locus BB_0515 in contig AE000783_GR.
KEGG	bbu:BB0515.
NMPDR	fig|224326.1.peg.899.
TIGR	BB_0515.
Phylogenomic databases
HOGENOM	P94284.
OMA	YRNREVA.
Enzyme and pathway databases
BioCyc	BBUR224326:BB_0515-MON.
BRENDA	1.8.1.9. 142596.
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_BORBU

Accession

Primary (citable) accession number: P94284
Secondary accession number(s): O51467

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	December 15, 1998
Last modified:	November 3, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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