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O78461 (FTRC_GUITH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ferredoxin-thioredoxin reductase, catalytic chain

Short name=FTR-C
EC=1.8.7.2
Alternative name(s):
Ferredoxin-thioredoxin reductase subunit B
Short name=FTR-B
Gene names
Name:ftrB
Encoded onPlastid; Chloroplast
OrganismGuillardia theta (Cryptomonas phi)
Taxonomic identifier55529 [NCBI]
Taxonomic lineageEukaryotaCryptophytaPyrenomonadalesGeminigeraceaeGuillardia

Protein attributes

Sequence length102 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

FTR is a [4Fe-4S] protein playing a central role in the ferredoxin/thioredoxin regulatory chain. It converts an electron signal (photoreduced ferredoxin) to a thiol signal (reduced thioredoxin) in the regulation of enzymes by reduction of specific disulfide groups. Catalyzes the light-dependent activation of several photosynthetic enzymes By similarity.

Catalytic activity

2 reduced ferredoxin + thioredoxin disulfide = 2 oxidized ferredoxin + thioredoxin + 2 H+.

Subunit structure

Heterodimer of subunit A (variable subunit) and subunit B (catalytic subunit) By similarity.

Subcellular location

Plastidchloroplast.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainRedox-active center
   Ligand4Fe-4S
Iron
Iron-sulfur
Metal-binding
   Molecular functionOxidoreductase
   PTMDisulfide bond
Gene Ontology (GO)
   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

ferredoxin-NAD(P) reductase activity

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 102102Ferredoxin-thioredoxin reductase, catalytic chain
PRO_0000167672

Sites

Metal binding531Iron-sulfur (4Fe-4S) By similarity
Metal binding721Iron-sulfur (4Fe-4S) By similarity
Metal binding741Iron-sulfur (4Fe-4S) By similarity
Metal binding831Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Disulfide bond55 ↔ 85Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
O78461 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 6E9092A68E5491C3

FASTA10211,766
        10         20         30         40         50         60 
MIESYSDSFV AMKKFAETYA KRTNTFFCND LSITQIVLEG LAKHKDEYGA PLCPCRHYDD 

        70         80         90        100 
KSEEVASTYW NCPCVPMRER KECHCMLFLT KDNEFAGSSQ TL 

« Hide

References

[1]"The plastid genome of the cryptophyte alga, Guillardia theta: complete sequence and conserved synteny groups confirm its common ancestry with red algae."
Douglas S.E., Penny S.L.
J. Mol. Evol. 48:236-244(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041468 Genomic DNA. Translation: AAC35652.1.
RefSeqNP_050718.1. NC_000926.1.

3D structure databases

ProteinModelPortalO78461.
SMRO78461. Positions 8-102.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID857021.

Phylogenomic databases

HOGENOMHOG000265597.
OMAEDNPFAC.
ProtClustDBCHL00165.

Family and domain databases

Gene3D3.90.460.10. 1 hit.
InterProIPR024707. FTR_bsu.
IPR004209. FTR_bsu_dom.
[Graphical view]
PfamPF02943. FeThRed_B. 1 hit.
[Graphical view]
PIRSFPIRSF000260. FTRc. 1 hit.
SUPFAMSSF57662. Fe/thioredoxin_red_bsu-like. 1 hit.
ProtoNetSearch...

Entry information

Entry nameFTRC_GUITH
AccessionPrimary (citable) accession number: O78461
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1998
Last modified: May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)