Reviewed, UniProtKB/Swiss-Prot P80028 (TRXH_CHLRE)

Names and origin

Protein names

Recommended name:
    Thioredoxin H-type
      Short name=Trx-H
Alternative name(s):
    Thioredoxin-CH1

Gene names

Name:

TRXH

Organism

Chlamydomonas reinhardtii

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	113 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)

Function	Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The H form is known to activate a number of cytosolic enzymes.
Subcellular location	Cytoplasm.
Miscellaneous	This thioredoxin cannot be used as a substrate for E.coli NAPDH: thioredoxin reductase, but is a substrate of spinach ferredoxin-thioredoxin reductase and can activate NADP-MDH.
Sequence similarities	Belongs to the thioredoxin family. Plant H-type subfamily. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Cytoplasm
Domain	Redox-active center
PTM	Disulfide bond
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW glycerol ether metabolic process Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 113

112

Thioredoxin H-type

PRO_0000120055

Regions

Domain

2 – 112

111

Thioredoxin

Sites

Active site

37

1

Nucleophile

Active site

40

1

Nucleophile

Site

31

1

Deprotonates C-terminal active site Cys

Site

38

1

Contributes to redox potential value

Site

39

1

Contributes to redox potential value

Amino acid modifications

Disulfide bond

37 ↔ 40

Redox-active Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

113

Helix Strand Turn

Details...

Beta strand

4 – 8

5

Helix

11 – 24

14

Beta strand

28 – 33

6

Helix

38 – 53

16

Turn

54 – 57

4

Beta strand

58 – 64

7

Turn

65 – 68

4

Helix

69 – 75

7

Beta strand

79 – 87

9

Beta strand

90 – 97

8

Helix

100 – 111

12

Sequences

	Sequence		Length	Mass (Da)
	P80028-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BCDDDCFA7810D3EE	FASTA	113	11,844
	10 20 30 40 50 60 MGGSVIVIDS KAAWDAQLAK GKEEHKPIVV DFTATWCGPC KMIAPLFETL SNDYAGKVIF 70 80 90 100 110 LKVDVDAVAA VAEAAGITAM PTFHVYKDGV KADDLVGASQ DKLKALVAKH AAA

References

[1]	"Chlamydomonas reinhardtii thioredoxins: structure of the genes coding for the chloroplastic m and cytosolic h isoforms; expression in Escherichia coli of the recombinant proteins, purification and biochemical properties." Stein M., Jacquot J.-P., Jeannette E., Decottignies P., Hodges M., Lancelin J.-M., Mittard V., Schmitter J.-M., Miginiac-Maslow M. Plant Mol. Biol. 28:487-503(1995) [PubMed: 7632918] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Characterization and primary structure of a second thioredoxin from the green alga, Chlamydomonas reinhardtii." Decottignies P., Schmitter J.-M., Dutka S., Jacquot J.-P., Miginiac-Maslow M. Eur. J. Biochem. 198:505-512(1991) [PubMed: 2040309] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-112, DISULFIDE BOND. Strain: 137c / CC-125.
[3]	"NMR solution structure of an oxidised thioredoxin h from the eukaryotic green alga Chlamydomonas reinhardtii." Mittard V., Blackledge M.J., Stein M., Jacquot J.-P., Marion D., Lancelin J.-M. Eur. J. Biochem. 243:374-383(1997) [PubMed: 9030762] [Abstract] Cited for: STRUCTURE BY NMR.
[4]	"Crystal structure of the wild-type and D30A mutant thioredoxin h of Chlamydomonas reinhardtii and implications for the catalytic mechanism." Menchise V., Corbier C., Didierjean C., Saviano M., Benedetti E., Jacquot J.-P., Aubry A. Biochem. J. 359:65-75(2001) [PubMed: 11563970] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

X78822 mRNA. Translation: CAA55399.1.
X80887 Genomic DNA. Translation: CAA56850.1.

PIR

S57775.

RefSeq

XP_001694574.1.

UniGene

Cre.13338

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EP7	X-ray	2.10	A/B	2-113	[»]
1EP8	X-ray	2.20	A/B	2-113	[»]
1TOF	NMR	-	A	2-113	[»]

ModBase

Search...

Proteomic databases

PRIDE

P80028.

Genome annotation databases

GeneID

5720085.

KEGG

cre:CHLREDRAFT_195887.

Family and domain databases

InterPro

IPR005746. Thioredoxin.
IPR017936. Thioredoxin-like.
IPR006662. Thioredoxin-like_subdom.
IPR015467. Thioredoxin_core.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
IPR012335. Thioredoxin_fold.
[Graphical view]

Gene3D

G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.

PANTHER

PTHR10438. Trx. 1 hit.

Pfam

PF00085. Thioredoxin. 1 hit.
[Graphical view]

PRINTS

PR00421. THIOREDOXIN.

TIGRFAMs

TIGR01068. thioredoxin. 1 hit.

PROSITE

PS00194. THIOREDOXIN_1. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TRXH_CHLRE

Accession

Primary (citable) accession number: P80028

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)