P51386 (FTRC_PORPU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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 on

Plastid; Chloroplast

Organism

Porphyra purpurea

Taxonomic identifier

2787 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Rhodophyta › Bangiophyceae › Bangiales › Bangiaceae › Porphyra

Protein attributes

Sequence length	118 AA.
Sequence status	Complete.
Protein existence	Inferred 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	Plastid › chloroplast.

Ontologies

Keywords
Cellular component	Chloroplast Plastid
Domain	Redox-active center
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
PTM	Disulfide bond
Gene Ontology (GO)
Cellular_component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	4 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 118	118	Ferredoxin-thioredoxin reductase, catalytic chain		PRO_0000167673
Sites
	Metal binding	57	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	76	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	78	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	87	1	Iron-sulfur (4Fe-4S) By similarity
Amino acid modifications
	Disulfide bond	59 ↔ 89		Redox-active By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51386 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E490AE73708630A8	FASTA	118	13,539
	10 20 30 40 50 60 MKKQNLVSFS DNLEAMRKFS ETYAKRTGTF FCADNSVTAV VIEGLARHKD KYGAPLCPCR 70 80 90 100 110 HYEDKKAEIS ATYWNCPCVP MRERKECHCM LFLTPDNEFT SDLQEIDKTT LLEKIASS

References

[1]	"Complete nucleotide sequence of the Porphyra purpurea chloroplast genome." Reith M.E., Munholland J. Plant Mol. Biol. Rep. 13:333-335(1995) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Avonport.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U38804 Genomic DNA. Translation: AAC08272.1.
PIR	S73307.
RefSeq	NP_053996.1. NC_000925.1.
3D structure databases
ProteinModelPortal	P51386.
SMR	P51386. Positions 13-117.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	810027.
Phylogenomic databases
ProtClustDB	CHL00165.
Family and domain databases
Gene3D	3.90.460.10. 1 hit.
InterPro	IPR024707. FTR_bsu. IPR004209. FTR_bsu_dom. [Graphical view]
Pfam	PF02943. FeThRed_B. 1 hit. [Graphical view]
PIRSF	PIRSF000260. FTRc. 1 hit.
SUPFAM	SSF57662. Fe/thioredoxin_red_bsu-like. 1 hit.
ProtoNet	Search...

Entry information

Entry name

FTRC_PORPU

Accession

Primary (citable) accession number: P51386

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	March 6, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)