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P09144

- PSAB_CHLRE

UniProt

P09144 - PSAB_CHLRE

Protein

Photosystem I P700 chlorophyll a apoprotein A2

Gene

psaB

Organism
Chlamydomonas reinhardtii (Chlamydomonas smithii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 4 (28 Mar 2003)
      Previous versions | rss
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    Functioni

    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.
    Both potential cofactor branches in PSI seem to be active; however, electron transfer seems to proceed preferentially down the path including the phylloquinone bound by PsaA.

    Catalytic activityi

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

    Cofactori

    P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi560 – 5601Iron-sulfur (4Fe-4S); shared with dimeric partner
    Metal bindingi569 – 5691Iron-sulfur (4Fe-4S); shared with dimeric partnerBy similarity
    Metal bindingi655 – 6551Magnesium (chlorophyll-a B1 axial ligand; P700 special pair)
    Metal bindingi663 – 6631Magnesium (chlorophyll-a B3 axial ligand)By similarity
    Binding sitei671 – 6711Chlorophyll-a B3By similarity
    Binding sitei672 – 6721Phylloquinone B

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. chlorophyll binding Source: UniProtKB-KW
    3. electron carrier activity Source: UniProtKB-HAMAP
    4. magnesium ion binding Source: UniProtKB-HAMAP
    5. oxidoreductase activity Source: UniProtKB-KW

    GO - Biological processi

    1. photosynthesis Source: UniProtKB-HAMAP
    2. protein-chromophore linkage Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Electron transport, Photosynthesis, Transport

    Keywords - Ligandi

    4Fe-4S, Chlorophyll, Chromophore, Iron, Iron-sulfur, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciCHLAMY:CHRECP048-MONOMER.
    MetaCyc:CHRECP048-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Photosystem I P700 chlorophyll a apoprotein A2 (EC:1.97.1.12)
    Alternative name(s):
    PSI-B
    PsaB
    Gene namesi
    Name:psaB
    Synonyms:ps1a2
    Encoded oniPlastid; Chloroplast
    OrganismiChlamydomonas reinhardtii (Chlamydomonas smithii)
    Taxonomic identifieri3055 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeChlorophytaChlorophyceaeChlamydomonadalesChlamydomonadaceaeChlamydomonas
    ProteomesiUP000006906: Chloroplast

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast thylakoid membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. photosystem I Source: UniProtKB-KW

    Keywords - Cellular componenti

    Chloroplast, Membrane, Photosystem I, Plastid, Thylakoid

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi559 – 5591P → A or L: Assembles functional PSI. Reaction center is somewhat unstable and interaction with psaC is impaired. The LEU mutant is less stable than the ALA mutant. 1 Publication
    Mutagenesisi560 – 5601C → H: Loss of PSI assembly and function. 1 Publication
    Mutagenesisi561 – 5611D → N: Loss of PSI assembly and function. 1 Publication
    Mutagenesisi563 – 5631P → L: Assembles functional PSI. Reaction center is somewhat unstable and interaction with psaC is impaired. 1 Publication
    Mutagenesisi565 – 5651R → E: Loss of PSI assembly and function. 1 Publication
    Mutagenesisi655 – 6551H → C, G, N or S: Contains somewhat decreased amounts of PSI, depending on the strain; significantly changes the spin density of the P700+ cation radical. 2 Publications
    Mutagenesisi655 – 6551H → D: Very little PSI detected. 2 Publications
    Mutagenesisi655 – 6551H → F or L: Loss of P700 function. 2 Publications
    Mutagenesisi655 – 6551H → Q: Impairment of P700 function. More severe; when associated with Q-676 in psaA. 2 Publications
    Mutagenesisi655 – 6551H → R: No PSI detected. 2 Publications
    Mutagenesisi672 – 6721W → F: Still able to photoaccumulate an electron on A1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 735735Photosystem I P700 chlorophyll a apoprotein A2PRO_0000088609Add
    BLAST

    Proteomic databases

    PRIDEiP09144.

    Interactioni

    Subunit structurei

    The PsaA/B heterodimer binds the P700 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 eukaryotic PSI reaction center is composed of at least 11 subunits.

    Protein-protein interaction databases

    IntActiP09144. 4 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP09144.
    SMRiP09144. Positions 2-734.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei47 – 7024Helical; Name=ISequence AnalysisAdd
    BLAST
    Transmembranei136 – 15924Helical; Name=IISequence AnalysisAdd
    BLAST
    Transmembranei176 – 20025Helical; Name=IIISequence AnalysisAdd
    BLAST
    Transmembranei274 – 29219Helical; Name=IVSequence AnalysisAdd
    BLAST
    Transmembranei331 – 35424Helical; Name=VSequence AnalysisAdd
    BLAST
    Transmembranei370 – 39627Helical; Name=VISequence AnalysisAdd
    BLAST
    Transmembranei418 – 44023Helical; Name=VIISequence AnalysisAdd
    BLAST
    Transmembranei518 – 53619Helical; Name=VIIISequence AnalysisAdd
    BLAST
    Transmembranei576 – 59722Helical; Name=IXSequence AnalysisAdd
    BLAST
    Transmembranei644 – 66623Helical; Name=XSequence AnalysisAdd
    BLAST
    Transmembranei708 – 72821Helical; Name=XISequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PsaA/PsaB family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    KOiK02690.

    Family and domain databases

    Gene3Di1.20.1130.10. 1 hit.
    HAMAPiMF_00482. PSI_PsaB.
    InterProiIPR001280. PSI_PsaA/B.
    IPR020586. PSI_PsaA/B_CS.
    IPR006244. PSI_PsaB.
    [Graphical view]
    PfamiPF00223. PsaA_PsaB. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002905. PSI_A. 1 hit.
    PRINTSiPR00257. PHOTSYSPSAAB.
    SUPFAMiSSF81558. SSF81558. 1 hit.
    TIGRFAMsiTIGR01336. psaB. 1 hit.
    PROSITEiPS00419. PHOTOSYSTEM_I_PSAAB. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P09144-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATKLFPKFS QGLAQDPTTR RIWYGLAMAH DFESHDGMTE ENLYQKIFAS    50
    HFGQLSIIFL WTSGNLFHVA WQGNFEQWVT DPVHIRPIAH AIWDPHFGQP 100
    AVEAFTRGGA SGPVNISTSG VYQWWYTIGM RTNQDLYVGS VFLALVSAIF 150
    LFAGWLHLQP NFQPSLSWFK DAESRLNHHL SGLFGVSSLA WTGHLVHVAI 200
    PESRGQHVGW DNFLSVLPHP QGLTPFFTGN WAAYAQSPDT ASHVFGTAQG 250
    SGQAILTFLG GFHPQTQSLW LTDMAHHHLA IAVIFIVAGH MYRTNFGIGH 300
    RMQAILEAHT PPSGSLGAGH KGLFDTVNNS LHFQLGLALA SVGTITSLVA 350
    QHMYSLPPYA FQAIDFTTQA ALYTHHQYIA GFIMCGAFAH GAIFFIRDYD 400
    PEQNKGNVLA RMLDHKEALI SHLSWVSLFL GFHTLGLYVH NDVMQAFGTP 450
    EKQILIEPVF AQWIQAAHGK ALYGFDFLLS SKTSAAFANG QSLWLPGWLD 500
    AINNNQNSLF LTIGPGDFLV HHAIALGLHT TTLILVKGAL DARGSKLMPD 550
    KKDFGYSFPC DGPGRGGTCD ISAYDAFYLA VFWMLNTIGW VTFYWHWKHL 600
    TLWQGNVAQF DESSTYLMGW LRDYLWLNSS QLINGYNPFG MNSLSVWAWT 650
    FLFGHLIYAT GFMFLISWRG YWQELIETLV WAHEKTPLAN LVYWKDKPVA 700
    LSIVQARLVG LAHFSVGYIF TYAAFLIAST SGRFG 735
    Length:735
    Mass (Da):82,109
    Last modified:March 28, 2003 - v4
    Checksum:i82F9914CE07A7908
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151Q → R in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti18 – 181T → A in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti21 – 211R → I in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti37 – 382GM → VW in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti48 – 492FA → IS in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti89 – 891A → C in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti203 – 2031S → LQ in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti298 – 2981I → N in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti335 – 3351L → I in CAA29287. (PubMed:16453785)Curated
    Sequence conflicti515 – 5151P → L(PubMed:16453785)Curated
    Sequence conflicti515 – 5151P → L(PubMed:6302265)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05848 Genomic DNA. Translation: CAA29287.1.
    U57326 Genomic DNA. Translation: AAN78307.1.
    FJ423446 Genomic DNA. Translation: ACJ50135.1.
    AB044470 Genomic DNA. Translation: BAB18396.1.
    J01399 Genomic DNA. No translation available.
    S67792 Genomic DNA. Translation: AAB20423.2.
    BK000554 Genomic DNA. Translation: DAA00949.2.
    PIRiB28341.
    S18319.
    RefSeqiNP_958404.1. NC_005353.1.

    Genome annotation databases

    EnsemblPlantsiDAA00949; DAA00949; DAA00949.
    GeneIDi2717038.
    KEGGicre:ChreCp048.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05848 Genomic DNA. Translation: CAA29287.1 .
    U57326 Genomic DNA. Translation: AAN78307.1 .
    FJ423446 Genomic DNA. Translation: ACJ50135.1 .
    AB044470 Genomic DNA. Translation: BAB18396.1 .
    J01399 Genomic DNA. No translation available.
    S67792 Genomic DNA. Translation: AAB20423.2 .
    BK000554 Genomic DNA. Translation: DAA00949.2 .
    PIRi B28341.
    S18319.
    RefSeqi NP_958404.1. NC_005353.1.

    3D structure databases

    ProteinModelPortali P09144.
    SMRi P09144. Positions 2-734.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P09144. 4 interactions.

    Proteomic databases

    PRIDEi P09144.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi DAA00949 ; DAA00949 ; DAA00949 .
    GeneIDi 2717038.
    KEGGi cre:ChreCp048.

    Phylogenomic databases

    KOi K02690.

    Enzyme and pathway databases

    BioCyci CHLAMY:CHRECP048-MONOMER.
    MetaCyc:CHRECP048-MONOMER.

    Family and domain databases

    Gene3Di 1.20.1130.10. 1 hit.
    HAMAPi MF_00482. PSI_PsaB.
    InterProi IPR001280. PSI_PsaA/B.
    IPR020586. PSI_PsaA/B_CS.
    IPR006244. PSI_PsaB.
    [Graphical view ]
    Pfami PF00223. PsaA_PsaB. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002905. PSI_A. 1 hit.
    PRINTSi PR00257. PHOTSYSPSAAB.
    SUPFAMi SSF81558. SSF81558. 1 hit.
    TIGRFAMsi TIGR01336. psaB. 1 hit.
    PROSITEi PS00419. PHOTOSYSTEM_I_PSAAB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural and transcription analysis of two homologous genes for the P700 chlorophyll a-apoproteins in Chlamydomonas reinhardtii: evidence for in vivo trans-splicing."
      Kueck U., Choquet Y., Schneider M., Dron M., Bennoun P.
      EMBO J. 6:2185-2195(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CC-406.
    2. "Revised sequence of the Chlamydomonas reinhardtii chloroplast gene psaB."
      Forsyth A.M., Redding K., Purton S.
      Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome: addressing the mutational-hazard hypothesis."
      Smith D.R., Lee R.W.
      BMC Evol. Biol. 9:120-120(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CC-503.
    4. "Origin and evolution of the colonial Volvocales (Chlorophyceae) as inferred from multiple, chloroplast gene sequences."
      Nozaki H., Misawa K., Kajita T., Kato M., Nohara S., Watanabe M.M.
      Mol. Phylogenet. Evol. 17:256-268(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-578.
      Strain: 137c / CC-125.
    5. "Sequence of the chloroplast DNA region of Chlamydomonas reinhardii containing the gene of the large subunit of ribulose bisphosphate carboxylase and parts of its flanking genes."
      Dron M., Rahire M., Rochaix J.-D.
      J. Mol. Biol. 162:775-793(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 493-735.
    6. "Transformation of chloroplasts with the psaB gene encoding a polypeptide of the photosystem I reaction center."
      Bingham S.E., Xu R.H., Webber A.N.
      FEBS Lett. 292:137-140(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANT AC-U-G-2.3).
      Strain: CC-2341.
    7. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.
    8. "Site-directed mutagenesis of the photosystem I reaction center in chloroplasts. The proline-cysteine motif."
      Webber A.N., Gibbs P.B., Ward J.B., Bingham S.E.
      J. Biol. Chem. 268:12990-12995(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-559 AND CYS-560.
      Strain: 137c / CC-125 and CC-2341.
    9. "Evidence that the FX domain in photosystem I interacts with the subunit PsaC: site-directed changes in PsaB destabilize the subunit interaction in Chlamydomonas reinhardtii."
      Rodday S.M., Webber A.N., Bingham S.E., Biggins J.
      Biochemistry 34:6328-6334(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-561; PRO-563 AND ARG-565.
      Strain: 137c / CC-125.
    10. "Site-directed mutations affecting the spectroscopic characteristics and midpoint potential of the primary donor in photosystem I."
      Webber A.N., Su H., Bingham S.E., Kaess H., Krabben L., Kuhn M., Jordan R., Schlodder E., Lubitz W.
      Biochemistry 35:12857-12863(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-655.
      Strain: FuD7.
    11. "A systematic survey of conserved histidines in the core subunits of photosystem I by site-directed mutagenesis reveals the likely axial ligands of P700."
      Redding K., MacMillan F., Leibl W., Brettel K., Hanley J., Rutherford A.W., Breton J., Rochaix J.-D.
      EMBO J. 17:50-60(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CONSERVED HISTIDINES.
      Strain: 137c / CC-125.
    12. "Influence of the axial ligands on the spectral properties of P700 of photosystem I: a study of site-directed mutants."
      Krabben L., Schlodder E., Jordan R., Carbonera D., Giacometti G., Lee H., Webber A.N., Lubitz W.
      Biochemistry 39:13012-13025(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-655.
      Strain: CC-2696.
    13. "Evidence for two active branches for electron transfer in photosystem I."
      Guergova-Kuras M., Boudreaux B., Joliot A., Joliot P., Redding K.
      Proc. Natl. Acad. Sci. U.S.A. 98:4437-4442(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
      Strain: 137c / CC-125.
    14. "Reversed-phase HPLC determination of chlorophyll a' and phylloquinone in photosystem I of oxygenic photosynthetic organisms."
      Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.
      Eur. J. Biochem. 270:2446-2458(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRESENCE OF CHLOROPHYLL A' IN PSI.
      Strain: IAM C-9.
    15. "Mutations in both sides of the photosystem I reaction center identify the phylloquinone observed by electron paramagnetic resonance spectroscopy."
      Boudreaux B., MacMillan F., Teutloff C., Agalarov R., Gu F., Grimaldi S., Bittl R., Brettel K., Redding K.
      J. Biol. Chem. 276:37299-37306(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
      Strain: 137c / CC-125.

    Entry informationi

    Entry nameiPSAB_CHLRE
    AccessioniPrimary (citable) accession number: P09144
    Secondary accession number(s): B7U1I8
    , Q36714, Q8HR52, Q9GH44
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: March 28, 2003
    Last modified: October 1, 2014
    This is version 126 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3