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A2C4V3 (PSAA_PROM1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Photosystem I P700 chlorophyll a apoprotein A1

EC=1.97.1.12
Alternative name(s):
PsaA
Gene names
Name:psaA
Ordered Locus Names:NATL1_19571
OrganismProchlorococcus marinus (strain NATL1A) [Complete proteome] [HAMAP]
Taxonomic identifier167555 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaProchloralesProchlorococcaceaeProchlorococcus

Protein attributes

Sequence length768 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. 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. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin or cytochrome c6 By similarity. HAMAP-Rule MF_00458

Catalytic activity

Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin. HAMAP-Rule MF_00458

Cofactor

PSI electron transfer chain: 5 divinyl chlorophyll a, 1 divinyl chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a divinyl chlorophyll a/divinyl chlorophyll a' dimer, A0 is one or more divinyl chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center By similarity.

Subunit structure

The PsaA/B heterodimer binds the P700 divinyl chlorophyll special pair and subsequent electron acceptors. PSI consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. 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.

Subcellular location

Cellular thylakoid membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00458.

Sequence similarities

Belongs to the PsaA/PsaB family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 768768Photosystem I P700 chlorophyll a apoprotein A1 HAMAP-Rule MF_00458
PRO_0000294204

Regions

Transmembrane76 – 9924Helical; Name=I; Potential
Transmembrane162 – 18524Helical; Name=II; Potential
Transmembrane201 – 22525Helical; Name=III; Potential
Transmembrane310 – 32819Helical; Name=IV; Potential
Transmembrane369 – 39224Helical; Name=V; Potential
Transmembrane408 – 43427Helical; Name=VI; Potential
Transmembrane456 – 47823Helical; Name=VII; Potential
Transmembrane559 – 57719Helical; Name=VIII; Potential
Transmembrane617 – 63822Helical; Name=IX; Potential
Transmembrane682 – 70423Helical; Name=X; Potential
Transmembrane742 – 76221Helical; Name=XI; Potential

Sites

Metal binding6011Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
Metal binding6101Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity
Metal binding6931Magnesium (divinyl chlorophyll-a' A1 axial ligand; P700 special pair) By similarity
Metal binding7011Magnesium (divinyl chlorophyll-a A3 axial ligand) By similarity
Binding site7091Divinyl chlorophyll-a A3 By similarity
Binding site7101Phylloquinone A By similarity

Sequences

Sequence LengthMass (Da)Tools
A2C4V3 [UniParc].

Last modified February 20, 2007. Version 1.
Checksum: 5F51B544D4E4471E

FASTA76884,390
        10         20         30         40         50         60 
MTISPPEKEQ KKEPVLDKPI ETDAIPVDFS KLDKPGFWSK SLAKGPKTTT WIWNLHADAH 

        70         80         90        100        110        120 
DFDTHVGDLQ ETSRKVFSAH FGHLAVIFIW MSAAFFHGAR FSNYSGWLSD PTHVKPGAQV 

       130        140        150        160        170        180 
VWPIVGQEML NADLGGNYHG IQITSGIFQM WRGWGITNET ELMALAIGAL LMAAIMLHGG 

       190        200        210        220        230        240 
IYHYHKAAPK LDWFRNLESM LNHHIAGLVG LGSIAWAGHC IHIGAPTAAL MDAIDAGKPL 

       250        260        270        280        290        300 
IIDGIPIASI ADMPLPHELC NPAIASQIFP GLAGRTVENF FTTNWWAFSD FLTFKGGLNP 

       310        320        330        340        350        360 
VTGSLWMTDI SHHHLAFGVL AVLGGHLYRT MFGIGHSLKE ILDNHAGDPI LFPAPNGHKG 

       370        380        390        400        410        420 
IYEFLANSWH AQLGLNLAMI GSLSIIISHH MYAMPPYPYL SIDYPTVLGL FTHHMWIGGL 

       430        440        450        460        470        480 
FIVGAAAHAG IAMIRDYDPA VHIDNVLDRI LKARDALISH LNWACMFLGF HSFGLYIHND 

       490        500        510        520        530        540 
VMRALGRPAD MFSDTGIQLQ PVFAQWIQNI HNSAAGSTTL AGANVNLQPG LVSEVFNGSV 

       550        560        570        580        590        600 
SQVGGKIGIA PIPLGTADFM IHHIHAFTIH VTLLILLKGV LFARSSRLIP DKANLGFRFP 

       610        620        630        640        650        660 
CDGPGRGGTC QVSSWDHVFL GLFWMYNGLS VVIFHFSWKM QSDVWGLTGG NFAQSSITIN 

       670        680        690        700        710        720 
GWLRDFLWAQ SSQVLTSYGQ PISMYGLMFL GAHFVWAFSL MFLFSGRGYW QELFESIIWA 

       730        740        750        760 
HNKLNLAPTI QPRALSITQG RAVGAAHFLL GGIATTWAFF HARLIGLG 

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References

[1]"Patterns and implications of gene gain and loss in the evolution of Prochlorococcus."
Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M., Richardson P., Chisholm S.W.
PLoS Genet. 3:2515-2528(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NATL1A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000553 Genomic DNA. Translation: ABM76513.1.
RefSeqYP_001015777.1. NC_008819.1.

3D structure databases

ProteinModelPortalA2C4V3.
SMRA2C4V3. Positions 20-768.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING167555.NATL1_19571.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM76513; ABM76513; NATL1_19571.
GeneID4779260.
KEGGpme:NATL1_19571.
PATRIC23021569. VBIProMar31285_1998.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGNOG05023.
HOGENOMHOG000276868.
KOK02689.
OMATWAFFHA.
OrthoDBEOG60W7PS.
ProtClustDBPRK13200.

Enzyme and pathway databases

BioCycPMAR167555:GI3K-1998-MONOMER.

Family and domain databases

Gene3D1.20.1130.10. 1 hit.
HAMAPMF_00458. PSI_PsaA.
InterProIPR006243. PSI_PsaA.
IPR001280. PSI_PsaA/B.
IPR020586. PSI_PsaA/B_CS.
[Graphical view]
PfamPF00223. PsaA_PsaB. 1 hit.
[Graphical view]
PIRSFPIRSF002905. PSI_A. 1 hit.
PRINTSPR00257. PHOTSYSPSAAB.
SUPFAMSSF81558. SSF81558. 1 hit.
TIGRFAMsTIGR01335. psaA. 1 hit.
PROSITEPS00419. PHOTOSYSTEM_I_PSAAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePSAA_PROM1
AccessionPrimary (citable) accession number: A2C4V3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: February 20, 2007
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families