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Protein

Photosystem I iron-sulfur center

Gene

psaC

Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
Mutant proteins with a 3Fe-4S center are not observed bound to PSI in vitro, and are probably not able to do so in vivo.

Catalytic activityi

Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin.

Cofactori

[4Fe-4S] clusterNote: Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Iron-sulfur 1 (4Fe-4S)
Metal bindingi14 – 141Iron-sulfur 1 (4Fe-4S)
Metal bindingi17 – 171Iron-sulfur 1 (4Fe-4S)
Metal bindingi21 – 211Iron-sulfur 2 (4Fe-4S)
Metal bindingi48 – 481Iron-sulfur 2 (4Fe-4S)
Metal bindingi51 – 511Iron-sulfur 2 (4Fe-4S)
Metal bindingi54 – 541Iron-sulfur 2 (4Fe-4S)
Metal bindingi58 – 581Iron-sulfur 1 (4Fe-4S)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyciSSP32049:GKF7-1590-MONOMER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:psaC
Ordered Locus Names:SYNPCC7002_A1589
OrganismiSynechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum quadruplicatum)
Taxonomic identifieri32049 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
Proteomesi
  • UP000001688 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Photosystem I, Thylakoid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141C → A, D or S: Generates altered FB cluster (in vitro). 2 Publications
Mutagenesisi21 – 211C → D: Unable to bind PSI cores (in vitro). 1 Publication
Mutagenesisi34 – 341C → A or S: No measurable effect. 1 Publication
Mutagenesisi51 – 511C → A, D or S: Generates altered FA cluster (in vitro). 3 Publications
Mutagenesisi58 – 581C → D: Unable to bind PSI cores (in vitro). 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 8180Photosystem I iron-sulfur centerPRO_0000062021Add
BLAST

Interactioni

Subunit structurei

The cyanobacterial PSI reaction center is composed of one copy each of PsaA,B,C,D,E,F,I,J,K,L,M and X, and forms trimeric complexes.By similarity

Protein-protein interaction databases

STRINGi32049.SYNPCC7002_A1589.

Structurei

Secondary structure

1
81
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 203Combined sources
Beta strandi26 – 305Combined sources
Beta strandi32 – 343Combined sources
Beta strandi37 – 415Combined sources
Beta strandi60 – 634Combined sources
Turni69 – 713Combined sources
Beta strandi74 – 796Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0TNMR-A2-81[»]
ProteinModelPortaliP31087.
SMRiP31087. Positions 2-81.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31087.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 31304Fe-4S ferredoxin-type 1Add
BLAST
Domaini37 – 68324Fe-4S ferredoxin-type 2Add
BLAST

Sequence similaritiesi

Contains 2 4Fe-4S ferredoxin-type domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108Z6M. Bacteria.
COG1145. LUCA.
HOGENOMiHOG000230505.
KOiK02691.
OMAiGQIAASP.
OrthoDBiEOG60SCM3.

Family and domain databases

HAMAPiMF_01303. PSI_PsaC.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR017491. PSI_PsaC.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03048. PS_I_psaC. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHSVKIYDT CIGCTQCVRA CPLDVLEMVP WDGCKAGQIA SSPRTEDCVG
60 70 80
CKRCETACPT DFLSIRVYLG AETTRSMGLA Y
Length:81
Mass (Da):8,814
Last modified:January 23, 2007 - v2
Checksum:i57B7D4A3371A4AFB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86238 Genomic DNA. Translation: AAA27353.1.
CP000951 Genomic DNA. Translation: ACA99580.1.

Genome annotation databases

EnsemblBacteriaiACA99580; ACA99580; SYNPCC7002_A1589.
KEGGisyp:SYNPCC7002_A1589.
PATRICi23817792. VBISynSp37135_1840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86238 Genomic DNA. Translation: AAA27353.1.
CP000951 Genomic DNA. Translation: ACA99580.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K0TNMR-A2-81[»]
ProteinModelPortaliP31087.
SMRiP31087. Positions 2-81.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi32049.SYNPCC7002_A1589.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA99580; ACA99580; SYNPCC7002_A1589.
KEGGisyp:SYNPCC7002_A1589.
PATRICi23817792. VBISynSp37135_1840.

Phylogenomic databases

eggNOGiENOG4108Z6M. Bacteria.
COG1145. LUCA.
HOGENOMiHOG000230505.
KOiK02691.
OMAiGQIAASP.
OrthoDBiEOG60SCM3.

Enzyme and pathway databases

BioCyciSSP32049:GKF7-1590-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP31087.

Family and domain databases

HAMAPiMF_01303. PSI_PsaC.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR017491. PSI_PsaC.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03048. PS_I_psaC. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 2 hits.
PS51379. 4FE4S_FER_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Bryant D.A., Rhiel E., de Lorimier R., Zhou J., Stirewalt V.L., Gasparich G.E., Dubbs J.M., Snyder W.
    (In) Baltscheffsky M. (eds.); Current research in photosynthesis, pp.2:1-9, Kluwer Academic Publishers, Dordrecht (1990)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The psaC genes of Synechococcus sp. PCC7002 and Cyanophora paradoxa: cloning and sequence analysis."
    Rhiel E., Stirewalt V.L., Gasparich G.E., Bryant D.A.
    Gene 112:123-128(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-10.
  3. "Complete sequence of Synechococcus sp. PCC 7002."
    Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T., Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J., Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.
    Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 27264 / PCC 7002 / PR-6.
  4. "Site-directed conversion of a cysteine to aspartate leads to the assembly of a [3Fe-4S] cluster in PsaC of photosystem I. The photoreduction of FA is independent of FB."
    Zhao J., Li N., Warren P.V., Golbeck J.H., Bryant D.A.
    Biochemistry 31:5093-5099(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-14 AND CYS-51.
  5. "Modified ligands to FA and FB in photosystem I. I. Structural constraints for the formation of iron-sulfur clusters in free and rebound PsaC."
    Mehari T., Qiao F., Scott M.P., Nellis D.F., Zhao J., Bryant D.A., Golbeck J.H.
    J. Biol. Chem. 270:28108-28117(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-14; CYS-21; CYS-34; CYS-51 AND CYS-58.
  6. "Modified ligands to FA and FB in photosystem I. II. Characterization of a mixed ligand [4Fe-4S] cluster in the C51D mutant of PsaC upon rebinding to P700-FX cores."
    Yu L., Vassiliev I.R., Jung Y.-S., Bryant D.A., Golbeck J.H.
    J. Biol. Chem. 270:28118-28125(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-51.

Entry informationi

Entry nameiPSAC_SYNP2
AccessioniPrimary (citable) accession number: P31087
Secondary accession number(s): B1XNQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.