Photosystem I iron-sulfur center - Chlamydomonas reinhardtii

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Q00914 (PSAC_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 92. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Photosystem I iron-sulfur center
EC=1.97.1.12

Alternative name(s):
9 kDa polypeptide
PSI-C
Photosystem I subunit VII
PsaC

Gene names

Name:

psaC

Encoded on

Plastid; Chloroplast

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	81 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	Apoprotein for the two 4Fe-4S centers FA and FB of photosystem I (PSI); essential for photochemical activity. FB is the terminal electron acceptor of PSI, donating electrons to ferredoxin. The C-terminus interacts with psaA/B/D and helps assemble the protein into the PSI complex. Required for binding of psaD and psaE to PSI. PSI is a plastocyanin/cytochrome c6-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Ref.1
Catalytic activity	Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin. HAMAP MF_01303
Cofactor	Binds 2 4Fe-4S clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
Subunit structure	The eukaryotic PSI reaction center is composed of at least 11 subunits By similarity.
Subcellular location	Plastid › chloroplast thylakoid membrane; Peripheral membrane protein; Stromal side By similarity HAMAP MF_01303.
Sequence similarities	Contains 2 4Fe-4S ferredoxin-type domains.

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Chloroplast Membrane Photosystem I Plastid Thylakoid
Domain	Repeat
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	photosynthetic electron transport in photosystem I Inferred from electronic annotation. Source: InterPro transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell photosystem I Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW electron carrier activity Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity 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

Initiator methionine

Removed By similarity

Chain

2 – 81

Photosystem I iron-sulfur center HAMAP MF_01303

PRO_0000061974

Regions

Domain

2 – 31

4Fe-4S ferredoxin-type 1

Domain

39 – 68

4Fe-4S ferredoxin-type 2

Sites

Metal binding

Iron-sulfur 1 (4Fe-4S)

Metal binding

Iron-sulfur 1 (4Fe-4S)

Metal binding

Iron-sulfur 1 (4Fe-4S)

Metal binding

Iron-sulfur 2 (4Fe-4S)

Metal binding

Iron-sulfur 2 (4Fe-4S)

Metal binding

Iron-sulfur 2 (4Fe-4S)

Metal binding

Iron-sulfur 2 (4Fe-4S)

Metal binding

Iron-sulfur 1 (4Fe-4S)

Experimental info

Mutagenesis

D → K or N: No effect. Ref.5 Ref.7

Mutagenesis

I → V: 60-fold increase in affinity of PSI for ferredoxin; when associated with 15-KR-16. Unable to grow photoautotrophically. Ref.5 Ref.7

Mutagenesis

15 – 16

TQ → KR: 60-fold increase in affinity of PSI for ferredoxin; when associated with V-12. Unable to grow photoautotrophically. Ref.5

Mutagenesis

K → D or E: Drastically decreases affinity of PSI for ferredoxin, limits photoautotrophic growth at medium and greater light. Decreases cross-linking of ferredoxin to PSI-D and PSI-E. Ref.5 Ref.6

Mutagenesis

K → T: Drastically decreases affinity of PSI for ferredoxin. Decreases cross-linking of ferredoxin to PSI-D and PSI-E. Ref.5 Ref.6

Mutagenesis

E → K or Q: No effect. Ref.5 Ref.7

Mutagenesis

V → I: Leads to partial destabilization of PSI; when associated with 52-TQ-53, alters the FA center. Unable to grow photoautotrophically. Ref.5 Ref.7

Mutagenesis

52 – 53

KR → SA: Preferentially reduces FB, accumulates 20-30% PSI, 25% of which is damaged. Grows photoautotrophically under low light. Ref.5

Mutagenesis

52 – 53

KR → TQ: Leads to partial destabilization of PSI; when associated with I-49. Alters the FA center. Unable to grow photoautotrophically. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

Q00914 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 6EE84943D2E3E102
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FASTA

8,860

        10         20         30         40         50         60 
MAHIVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKASQMA SAPRTEDCVG CKRCETACPT 

        70         80 
DFLSVRVYLG SESTRSMGLS Y

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Directed chloroplast transformation in Chlamydomonas reinhardtii: insertional inactivation of the psaC gene encoding the iron sulfur protein destabilizes photosystem I." Takahashi Y., Goldschmidt-Clermont M., Soen S.-Y., Franzen L.-G., Rochaix J.-D. EMBO J. 10:2033-2040(1991) [PubMed: 1712288] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: 137c / CC-125.
[2]	"The chloroplast ycf7 (petL) open reading frame of Chlamydomonas reinhardtii encodes a small functionally important subunit of the cytochrome b6f complex." Takahashi Y., Rahire M., Breyton C., Popot J.-L., Joliot P., Rochaix J.-D. EMBO J. 15:3498-3506(1996) [PubMed: 8670852] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Nucleotide diversity in the chloroplast genome of Chlamydomonas reinhardtii." United States Department of Energy Joint Genome Institute Smith D.R. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC-503.
[4]	"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats." Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., Stern D.B. Plant Cell 14:2659-2679(2002) [PubMed: 12417694] [Abstract] Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.
[5]	"Targeted mutations in the psaC gene of Chlamydomonas reinhardtii: preferential reduction of FB at low temperature is not accompanied by altered electron flow from photosystem I to ferredoxin." Fischer N., Setif P., Rochaix J.-D. Biochemistry 36:93-102(1997) [PubMed: 8993322] [Abstract] Cited for: MUTAGENESIS OF 52-LYS-ARG-53.
[6]	"The PsaC subunit of photosystem I provides an essential lysine residue for fast electron transfer to ferredoxin." Fischer N., Hippler M., Setif P., Jacquot J.-P., Rochaix J.-D. EMBO J. 17:849-858(1998) [PubMed: 9463363] [Abstract] Cited for: MUTAGENESIS OF LYS-35, CROSS-LINKING TO FERREDOXIN.
[7]	"Site-directed mutagenesis of the PsaC subunit of photosystem I. F(b) is the cluster interacting with soluble ferredoxin." Fischer N., Setif P., Rochaix J.-D. J. Biol. Chem. 274:23333-23340(1999) [PubMed: 10438510] [Abstract] Cited for: MUTAGENESIS OF ASP-9; ILE-12; 15-THR-GLN-16; GLU-46; VAL-49 AND 52-LYS-ARG-53. Strain: 137c / CC-125.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60365 Genomic DNA. Translation: CAA42917.1. U43964 Genomic DNA. Translation: AAB17714.1. FJ423446 Genomic DNA. Translation: ACJ50154.1. BK000554 Genomic DNA. Translation: DAA00967.1.
PIR	S16351.
RefSeq	NP_958423.1. NC_005353.1.
3D structure databases
ProteinModelPortal	Q00914.
SMR	Q00914. Positions 2-81.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q00914. 5 interactions.
Proteomic databases
PRIDE	Q00914.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	DAA00967; DAA00967; DAA00967.
GeneID	2717046.
KEGG	cre:ChreCp067.
Phylogenomic databases
ProtClustDB	CHL00065.
Enzyme and pathway databases
BioCyc	CHLAMY:CHRECP067-MONOMER. MetaCyc:CHRECP067-MONOMER.
Family and domain databases
HAMAP	MF_01303. PSI_PsaC. [Tree]
InterPro	IPR001450. 4Fe4S-bd_dom. IPR017896. 4Fe4S_Fe-S-bd. IPR017900. 4Fe4S_Fe_S_CS. IPR017491. PSI_PsaC. [Graphical view]
KO	K02691.
Pfam	PF12838. Fer4_7. 1 hit. [Graphical view]
TIGRFAMs	TIGR03048. PS_I_psaC. 1 hit.
PROSITE	PS00198. 4FE4S_FER_1. 2 hits. PS51379. 4FE4S_FER_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PSAC_CHLRE

Accession

Primary (citable) accession number: Q00914
Secondary accession number(s): B7U1K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents