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P09144

- PSAB_CHLRE

UniProt

P09144 - PSAB_CHLRE

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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

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
Complete GO annotation...

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-HAMAP
  2. integral component of membrane Source: UniProtKB-KW
  3. photosystem I Source: UniProtKB-KW
Complete GO annotation...

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

InParanoidiP09144.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATKLFPKFS QGLAQDPTTR RIWYGLAMAH DFESHDGMTE ENLYQKIFAS
60 70 80 90 100
HFGQLSIIFL WTSGNLFHVA WQGNFEQWVT DPVHIRPIAH AIWDPHFGQP
110 120 130 140 150
AVEAFTRGGA SGPVNISTSG VYQWWYTIGM RTNQDLYVGS VFLALVSAIF
160 170 180 190 200
LFAGWLHLQP NFQPSLSWFK DAESRLNHHL SGLFGVSSLA WTGHLVHVAI
210 220 230 240 250
PESRGQHVGW DNFLSVLPHP QGLTPFFTGN WAAYAQSPDT ASHVFGTAQG
260 270 280 290 300
SGQAILTFLG GFHPQTQSLW LTDMAHHHLA IAVIFIVAGH MYRTNFGIGH
310 320 330 340 350
RMQAILEAHT PPSGSLGAGH KGLFDTVNNS LHFQLGLALA SVGTITSLVA
360 370 380 390 400
QHMYSLPPYA FQAIDFTTQA ALYTHHQYIA GFIMCGAFAH GAIFFIRDYD
410 420 430 440 450
PEQNKGNVLA RMLDHKEALI SHLSWVSLFL GFHTLGLYVH NDVMQAFGTP
460 470 480 490 500
EKQILIEPVF AQWIQAAHGK ALYGFDFLLS SKTSAAFANG QSLWLPGWLD
510 520 530 540 550
AINNNQNSLF LTIGPGDFLV HHAIALGLHT TTLILVKGAL DARGSKLMPD
560 570 580 590 600
KKDFGYSFPC DGPGRGGTCD ISAYDAFYLA VFWMLNTIGW VTFYWHWKHL
610 620 630 640 650
TLWQGNVAQF DESSTYLMGW LRDYLWLNSS QLINGYNPFG MNSLSVWAWT
660 670 680 690 700
FLFGHLIYAT GFMFLISWRG YWQELIETLV WAHEKTPLAN LVYWKDKPVA
710 720 730
LSIVQARLVG LAHFSVGYIF TYAAFLIAST SGRFG
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

InParanoidi P09144.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 127 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