P09856 (TRXF_SPIOL) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Thioredoxin F-type, chloroplastic Short name=Trx-F
Organism	Spinacia oleracea (Spinach)
Taxonomic identifier	3562 [NCBI]
Taxonomic lineage	Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › Caryophyllales › Amaranthaceae › Spinacia

Protein attributes

Sequence length	190 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 F form is known to activate a number of enzymes of the photosynthetic carbon cycle.
Subcellular location	Plastid › chloroplast.
Sequence similarities	Belongs to the thioredoxin family. Plant F-type subfamily. Contains 1 thioredoxin domain.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Chloroplast Plastid
Domain	Redox-active center Transit peptide
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	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ftrC	Q55389	4	EBI-863615,EBI-863211	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 77

77

Chloroplast Ref.1

Chain

78 – 190

113

Thioredoxin F-type, chloroplastic

PRO_0000034161

Regions

Domain

78 – 189

112

Thioredoxin

Sites

Active site

114

1

Nucleophile

Active site

117

1

Nucleophile

Site

108

1

Deprotonates C-terminal active site Cys

Site

115

1

Contributes to redox potential value

Site

116

1

Contributes to redox potential value

Amino acid modifications

Disulfide bond

114 ↔ 117

Redox-active Ref.3

Secondary structure

1

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190

Helix Strand Turn

Details...

Beta strand

84 – 88

5

Turn

90 – 92

3

Helix

93 – 98

6

Beta strand

105 – 110

6

Helix

115 – 130

16

Beta strand

134 – 140

7

Helix

146 – 152

7

Beta strand

155 – 164

10

Beta strand

167 – 175

9

Helix

177 – 188

12

Sequences

	Sequence		Length	Mass (Da)
	P09856 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: 4B162C69DBC11869	FASTA	190	21,024
	10 20 30 40 50 60 MALHLSLSHQ SWTSPAHPIT SSDPTRSSVP GTGLSRRVDF LGSCKINGVF VVKRKDRRRM 70 80 90 100 110 120 RGGEVRASME QALGTQEMEA IVGKVTEVNK DTFWPIVKAA GDKPVVLDMF TQWCGPCKAM 130 140 150 160 170 180 APKYEKLAEE YLDVIFLKLD CNQENKTLAK ELGIRVVPTF KILKENSVVG EVTGAKYDKL 190 LEAIQAARSS

References

[1]	"Primary structure of spinach-chloroplast thioredoxin f. Protein sequencing and analysis of complete cDNA clones for spinach-chloroplast thioredoxin f." Kamo M., Tsugita A., Wiessner C., Wedel N., Bartling D., Herrmann R.G., Aguilar F., Gardet-Salvi L., Schurmann P. Eur. J. Biochem. 182:315-322(1989) [PubMed: 2737203] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 78-190.
[2]	"Spinach chloroplast thioredoxins in evolutionary drift." Tsugita A., Maeda K., Schurmann P. Biochem. Biophys. Res. Commun. 115:1-7(1983) [PubMed: 6351859] [Abstract] Cited for: PRELIMINARY PARTIAL PROTEIN SEQUENCE.
[3]	"Crystal structures of two functionally different thioredoxins in spinach chloroplasts." Capitani G., Markovic-Housley Z., DelVal G., Morris M., Jansonius J.N., Schurmann P. J. Mol. Biol. 302:135-154(2000) [PubMed: 10964566] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 70-189, DISULFIDE BOND.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X14959 mRNA. Translation: CAA33082.1.

PIR

S04661.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F9M	X-ray	1.86	A/B	78-189	[»]
1FAA	X-ray	1.85	A	72-189	[»]
2PU9	X-ray	1.65	C	79-189	[»]
2PVO	X-ray	3.40	C	79-189	[»]

ProteinModelPortal

P09856.

SMR

P09856. Positions 78-189.

ModBase

Search...

Protein-protein interaction databases

IntAct

P09856. 1 interaction.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR005746. Thioredoxin.
IPR012336. Thioredoxin-like_fold.
IPR017937. Thioredoxin_CS.
IPR013766. Thioredoxin_domain.
[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.

SUPFAM

SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

TRXF_SPIOL

Accession

Primary (citable) accession number: P09856

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1989
Last modified:	September 21, 2011
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program