NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Nine Mile phase I / Bratislava;
Oswald W.;
Thesis (1994), Justus Liebig University / Frankfurt, Germany.

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nine Mile phase I / RSA 493;
DOI=10.1073/pnas.0931379100; PubMed=12704232 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).

Comments

CATALYTIC ACTIVITY: Thioredoxin + NADP⁺ = thioredoxin disulfide + NADPH.
COFACTOR: Binds 1 FAD per subunit (By similarity).
SUBUNIT: Homodimer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
MISCELLANEOUS: The active site is a redox-active disulfide bond.
SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X75627; CAA53288.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE016828; AAO90702.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S43131; S43131.

RefSeq

NP_820188.1; -.

3D structure databases

HSSP

P09625; 1CL0. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P39916.

Enzyme and pathway databases

BioCyc

CBUR227377:CBU_1193-MON; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0004791;	Molecular function: thioredoxin-disulfide reductase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0019430;	Biological process: removal of superoxide radicals (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000759; Adrndx_reductase.
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_reduct.
Graphical view of domain structure.

Pfam

PF00070; Pyr_redox; 1.
PF07992; Pyr_redox_2; 1.
Pfam graphical view of domain structure.

PRINTS

PR00419; ADXRDTASE.
PR00368; FADPNR.
PR00469; PNDRDTASEII.

ProDom

PD000139; FAD_pyr_redox; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01292; TRX_reduct; 1.

PROSITE

PS00573; PYRIDINE_REDOX_2; 1.

ProtoNet

P39916.

Genome annotation databases

GeneID

1209097; -.

GenomeReviews

AE016828_GR; CBU_1193.

KEGG

cbu:CBU_1193; -.

NMPDR

fig|227377.1.peg.1132; -.

TIGR

CBU_1193; -.

Phylogenomic databases

HOGENOM

P39916; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 320`	`320`	`Thioredoxin reductase.`	`PRO_0000166728`
`NP_BIND`	`36 43`	`8`	`FAD (By similarity).`
`NP_BIND`	`287 296`	`10`	`FAD (By similarity).`
`DISULFID`	`136 139`		`Redox-active (By similarity).`
`CONFLICT`	`21 21`		`A -> D (in Ref. 1; CAA53288).`
`CONFLICT`	`25 25`		`A -> V (in Ref. 1; CAA53288).`
`CONFLICT`	`51 51`		`D -> A (in Ref. 1; CAA53288).`
`CONFLICT`	`64 66`		`QLM -> KLL (in Ref. 1; CAA53288).`
`CONFLICT`	`74 77`		`ERLD -> GGALN (in Ref. 1; CAA53288).`
`CONFLICT`	`87 88`		`EA -> KP (in Ref. 1; CAA53288).`
`CONFLICT`	`92 92`		`Q -> P (in Ref. 1; CAA53288).`
`CONFLICT`	`98 98`		`K -> Q (in Ref. 1; CAA53288).`
`CONFLICT`	`127 127`		`A -> P (in Ref. 1; CAA53288).`
`CONFLICT`	`146 146`		`G -> A (in Ref. 1; CAA53288).`
`CONFLICT`	`158 158`		`A -> S (in Ref. 1; CAA53288).`
`CONFLICT`	`284 292`		`AAGDVTDHV -> PAVVVRGQL (in Ref. 1; CAA53288).`
`CONFLICT`	`296 298`		`AIT -> TIA (in Ref. 1; CAA53288).`
`CONFLICT`	`306 306`		`A -> P (in Ref. 1; CAA53288).`

Sequence information

Length: 320 AA [This is the length of the unprocessed precursor]

Molecular weight: 34620 Da [This is the MW of the unprocessed precursor]

CRC64: 750851B6FDDEB5E3 [This is a checksum on the sequence]

        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

P39916 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools