P39916 (TRXB_COXBU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:	trxB
Ordered Locus Names:	CBU_1193

Organism

Coxiella burnetii (strain RSA 493 / Nine Mile phase I) [Reference proteome] [HAMAP]

Taxonomic identifier

227377 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Coxiellaceae › Coxiella › Coxiella burnetii

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
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 Reference proteome
Gene Ontology (GO)
Biological_process	removal of superoxide radicals Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	flavin adenine dinucleotide binding 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 – 320	320	Thioredoxin reductase		PRO_0000166728
Regions
	Nucleotide binding	36 – 43	8	FAD By similarity
	Nucleotide binding	287 – 296	10	FAD By similarity
Amino acid modifications
	Disulfide bond	136 ↔ 139		Redox-active By similarity
Experimental info
	Sequence conflict	21	1	A → D in CAA53288. Ref.1
	Sequence conflict	25	1	A → V in CAA53288. Ref.1
	Sequence conflict	51	1	D → A in CAA53288. Ref.1
	Sequence conflict	64 – 66	3	QLM → KLL in CAA53288. Ref.1
	Sequence conflict	74 – 77	4	ERLD → GGALN in CAA53288. Ref.1
	Sequence conflict	87 – 88	2	EA → KP in CAA53288. Ref.1
	Sequence conflict	92	1	Q → P in CAA53288. Ref.1
	Sequence conflict	98	1	K → Q in CAA53288. Ref.1
	Sequence conflict	127	1	A → P in CAA53288. Ref.1
	Sequence conflict	146	1	G → A in CAA53288. Ref.1
	Sequence conflict	158	1	A → S in CAA53288. Ref.1
	Sequence conflict	284 – 292	9	AAGDVTDHV → PAVVVRGQL in CAA53288. Ref.1
	Sequence conflict	296 – 298	3	AIT → TIA in CAA53288. Ref.1
	Sequence conflict	306	1	A → P in CAA53288. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P39916 [UniParc]. Last modified May 9, 2003. Version 2. Checksum: 750851B6FDDEB5E3	FASTA	320	34,620
	10 20 30 40 50 60 MNKPQHHSLI ILGSGPAGYT AAIYAARANL KPIMITGMEQ GGQLMTTTDV DNWPGEAPGL 70 80 90 100 110 120 QGPQLMERMQ KHAERLDTQF IFDHINEADL NQRPFLLKGD NATYSCDALI IATGASARYL 130 140 150 160 170 180 GLPSEKAYMG KGVSACATCD GFFYRGKKVA VVGGGNTAVE EALYLSHIAS HVTLIHRRDK 190 200 210 220 230 240 LRAEKMLSAQ LIKKVEEGKV AIVWSHVIEE VLGDDQGVTG VHLKHVKEEK TQDLTIDGLF 250 260 270 280 290 300 IAIGHDPNTK IFKEQLEMDE AGYLRAKSGL QGNATATNIP GVFAAGDVTD HVYRQAITAA 310 320 GMGCMAALDA ERYLDSLNQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Oswald W. Thesis (1994), Justus Liebig University / Frankfurt, Germany Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Nine Mile phase I / Bratislava.
[2]	"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii." Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., Lee K.H., Carty H.A. , Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F. Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: RSA 493 / Nine Mile phase I.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X75627 Genomic DNA. Translation: CAA53288.1. AE016828 Genomic DNA. Translation: AAO90702.1.
PIR	S43131.
RefSeq	NP_820188.1. NC_002971.3.
3D structure databases
ProteinModelPortal	P39916.
SMR	P39916. Positions 5-317.
ModBase	Search...
Protein-protein interaction databases
STRING	227377.CBU_1193.
Proteomic databases
PRIDE	P39916.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAO90702; AAO90702; CBU_1193.
GeneID	1209097.
KEGG	cbu:CBU_1193.
PATRIC	17931129. VBICoxBur82552_1190.
Phylogenomic databases
eggNOG	COG0492.
HOGENOM	HOG000072912.
KO	K00384.
OMA	VMGAFIA.
ProtClustDB	CLSK914603.
Enzyme and pathway databases
BioCyc	CBUR227377:GJ7S-1181-MONOMER.
Family and domain databases
InterPro	IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR008255. Pyr_nucl-diS_OxRdtase_2_AS. IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD. IPR001327. Pyr_OxRdtase_NAD-bd_dom. 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.
TIGRFAMs	TIGR01292. TRX_reduct. 1 hit.
PROSITE	PS00573. PYRIDINE_REDOX_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TRXB_COXBU

Accession

Primary (citable) accession number: P39916

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	May 9, 2003
Last modified:	May 1, 2013
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program