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Protein

Photosystem I P700 chlorophyll a apoprotein A2

Gene

psaB

Organism
Pisum sativum (Garden pea)
Status
Reviewed-Annotation score: Annotation score: 4 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-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.UniRule annotation

Catalytic activityi

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

Cofactori

Note: 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.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi559 – 5591Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi568 – 5681Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi654 – 6541Magnesium (chlorophyll-a B1 axial ligand; P700 special pair)UniRule annotation
Metal bindingi662 – 6621Magnesium (chlorophyll-a B3 axial ligand)UniRule annotation
Binding sitei670 – 6701Chlorophyll-a B3UniRule annotation
Binding sitei671 – 6711Phylloquinone BUniRule annotation

GO - Molecular functioni

GO - Biological processi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Photosystem I P700 chlorophyll a apoprotein A2UniRule annotation (EC:1.97.1.12UniRule annotation)
Alternative name(s):
PSI-BUniRule annotation
PsaBUniRule annotation
Gene namesi
Name:psaBUniRule annotation
Synonyms:psaA2
Encoded oniPlastid; Chloroplast
OrganismiPisum sativum (Garden pea)
Taxonomic identifieri3888 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

Subcellular locationi

  • Plastidchloroplast thylakoid membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei46 – 6924Helical; Name=IUniRule annotationAdd
BLAST
Transmembranei135 – 15824Helical; Name=IIUniRule annotationAdd
BLAST
Transmembranei175 – 19925Helical; Name=IIIUniRule annotationAdd
BLAST
Transmembranei273 – 29119Helical; Name=IVUniRule annotationAdd
BLAST
Transmembranei330 – 35324Helical; Name=VUniRule annotationAdd
BLAST
Transmembranei369 – 39527Helical; Name=VIUniRule annotationAdd
BLAST
Transmembranei417 – 43923Helical; Name=VIIUniRule annotationAdd
BLAST
Transmembranei517 – 53519Helical; Name=VIIIUniRule annotationAdd
BLAST
Transmembranei575 – 59622Helical; Name=IXUniRule annotationAdd
BLAST
Transmembranei643 – 66523Helical; Name=XUniRule annotationAdd
BLAST
Transmembranei707 – 72721Helical; Name=XIUniRule annotationAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem I, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 734734Photosystem I P700 chlorophyll a apoprotein A2PRO_0000088630Add
BLAST

Proteomic databases

PRIDEiP05311.

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.UniRule annotation

Protein-protein interaction databases

DIPiDIP-60282N.

Structurei

Secondary structure

1
734
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi10 – 134Combined sources
Helixi19 – 268Combined sources
Turni27 – 293Combined sources
Helixi31 – 333Combined sources
Beta strandi34 – 363Combined sources
Helixi39 – 7032Combined sources
Helixi75 – 784Combined sources
Beta strandi82 – 843Combined sources
Beta strandi87 – 904Combined sources
Helixi98 – 1036Combined sources
Beta strandi109 – 1113Combined sources
Beta strandi113 – 1153Combined sources
Helixi120 – 1278Combined sources
Helixi132 – 15524Combined sources
Turni159 – 1613Combined sources
Helixi165 – 1684Combined sources
Helixi172 – 1809Combined sources
Turni181 – 1833Combined sources
Helixi184 – 19613Combined sources
Helixi198 – 2036Combined sources
Turni209 – 2135Combined sources
Beta strandi217 – 2204Combined sources
Helixi223 – 2275Combined sources
Helixi231 – 2344Combined sources
Beta strandi244 – 2496Combined sources
Beta strandi260 – 2623Combined sources
Turni263 – 2664Combined sources
Helixi270 – 28718Combined sources
Beta strandi288 – 2914Combined sources
Beta strandi294 – 2963Combined sources
Helixi301 – 3077Combined sources
Beta strandi311 – 3155Combined sources
Turni316 – 3216Combined sources
Helixi322 – 3276Combined sources
Helixi330 – 35425Combined sources
Beta strandi358 – 3603Combined sources
Beta strandi362 – 3643Combined sources
Helixi365 – 38622Combined sources
Helixi389 – 3968Combined sources
Turni400 – 4056Combined sources
Turni407 – 4115Combined sources
Helixi415 – 44531Combined sources
Helixi449 – 4513Combined sources
Helixi458 – 4658Combined sources
Turni466 – 4683Combined sources
Beta strandi479 – 4824Combined sources
Turni484 – 4863Combined sources
Helixi487 – 4893Combined sources
Helixi493 – 5019Combined sources
Beta strandi504 – 5074Combined sources
Helixi514 – 53926Combined sources
Helixi540 – 5423Combined sources
Beta strandi547 – 5493Combined sources
Helixi550 – 5523Combined sources
Helixi563 – 5653Combined sources
Helixi572 – 60231Combined sources
Helixi606 – 6127Combined sources
Helixi616 – 6227Combined sources
Turni623 – 6275Combined sources
Helixi629 – 6324Combined sources
Turni633 – 6353Combined sources
Helixi636 – 6383Combined sources
Helixi644 – 66522Combined sources
Helixi668 – 68316Combined sources
Turni686 – 6905Combined sources
Beta strandi694 – 6963Combined sources
Helixi702 – 73231Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO9model-B1-734[»]
2O01X-ray3.40B2-733[»]
2WSCX-ray3.30B1-734[»]
2WSEX-ray3.49B1-734[»]
2WSFX-ray3.48B1-734[»]
3LW5X-ray3.30B2-734[»]
4RKUX-ray3.00B3-733[»]
ProteinModelPortaliP05311.
SMRiP05311. Positions 2-733.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05311.

Family & Domainsi

Sequence similaritiesi

Belongs to the PsaA/PsaB family.UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

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.

P05311-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALRIPRFSQ GIAQDPTTRR IWFGIATAHD FESHDDITEG RLYQNIFASH
60 70 80 90 100
FGQLAIIFLW TSGNLFHVAW QGNFEAWVQD PFHVRPIAHA IWDPHFGQPA
110 120 130 140 150
VEAFTRGGAL GPVNNAYSGV YQWWYTIGLR TNEDLYTGAI FLLFLSFISL
160 170 180 190 200
LAGWLHLQPK WKPSVSWFKN AESRLNHHLS GLFGVSSLAW AGHLVHVAIP
210 220 230 240 250
GSRGEYVRWN NFLDVLPYPQ GLGPLLTGQW NLYAQNPSSS NHLFGTTQGA
260 270 280 290 300
GTAILTILGG FHPQTQSLWL TDVAHHHLAI AFLFLIGGLM YRTNFGIGHS
310 320 330 340 350
IKYILEAHIP PGGRLGRGHK GLYDTINNSI HFQLGLALAS LGVITSLVAQ
360 370 380 390 400
HMYSLPAYAF IAQDFTTQAA LYTHHQYIAG FIMTGAFAHG PIFFIRDYNP
410 420 430 440 450
EQNADNVLAR MLEHKEAIIS HLSWASLFLG FHTLGLYVHN DVMLAFGTPE
460 470 480 490 500
KQILIEPIFA QWIQSAHGKT TYGFDIPLSS TNGPALNAGR NIWLPGWLNA
510 520 530 540 550
INENSNSLFL TIGPGDFLVH HAIALGLHTT TLILVKGALD ARGSKLMPDK
560 570 580 590 600
KDFGYSFPCD GPGRGGTCDI SAWDDFYLAV FWMLNTIGWV TFYWHWKHIT
610 620 630 640 650
LWRGNVSQFN ESSTYLMGWL RDYLWLNSSQ LINGITPLVC NSLSVWAWMF
660 670 680 690 700
LFGHLVWATG FMFLISWRGY WQELIETLAW AHERTPLANL IRWRDKPVAL
710 720 730
SIVQARLVGL VHFSVGYIFT YAAFLIASTS GKFG
Length:734
Mass (Da):82,412
Last modified:November 1, 1988 - v1
Checksum:i2ACF1F77D46FA8E7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05423 Genomic DNA. Translation: CAA29004.1.
PIRiS00704.
RefSeqiYP_003587537.1. NC_014057.1.

Genome annotation databases

GeneIDi9073070.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05423 Genomic DNA. Translation: CAA29004.1.
PIRiS00704.
RefSeqiYP_003587537.1. NC_014057.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO9model-B1-734[»]
2O01X-ray3.40B2-733[»]
2WSCX-ray3.30B1-734[»]
2WSEX-ray3.49B1-734[»]
2WSFX-ray3.48B1-734[»]
3LW5X-ray3.30B2-734[»]
4RKUX-ray3.00B3-733[»]
ProteinModelPortaliP05311.
SMRiP05311. Positions 2-733.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60282N.

Proteomic databases

PRIDEiP05311.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9073070.

Miscellaneous databases

EvolutionaryTraceiP05311.

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]
ProtoNetiSearch...

Publicationsi

  1. "Sequence of two genes in pea chloroplast DNA coding for 84 and 82 kD polypeptides of the photosystem I complex."
    Lehmbeck J., Rasmussen O.F., Bookjans G.B., Jepsen B.R., Stummann B.M., Henningsen K.W.
    Plant Mol. Biol. 7:3-10(1986)
    [AGRICOLA] [Europe PMC]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiPSAB_PEA
AccessioniPrimary (citable) accession number: P05311
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: May 27, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

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

External Data

Dasty 3

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 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.