Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Metal bindingi559Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation1
Metal bindingi568Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation1
Metal bindingi654Magnesium (chlorophyll-a B1 axial ligand; P700 special pair)UniRule annotation1
Metal bindingi662Magnesium (chlorophyll-a B3 axial ligand)UniRule annotation1
Binding sitei670Chlorophyll-a B3UniRule annotation1
Binding sitei671Phylloquinone BUniRule annotation1

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)DescriptionActionsGraphical viewLength
Transmembranei46 – 69Helical; Name=IUniRule annotationAdd BLAST24
Transmembranei135 – 158Helical; Name=IIUniRule annotationAdd BLAST24
Transmembranei175 – 199Helical; Name=IIIUniRule annotationAdd BLAST25
Transmembranei273 – 291Helical; Name=IVUniRule annotationAdd BLAST19
Transmembranei330 – 353Helical; Name=VUniRule annotationAdd BLAST24
Transmembranei369 – 395Helical; Name=VIUniRule annotationAdd BLAST27
Transmembranei417 – 439Helical; Name=VIIUniRule annotationAdd BLAST23
Transmembranei517 – 535Helical; Name=VIIIUniRule annotationAdd BLAST19
Transmembranei575 – 596Helical; Name=IXUniRule annotationAdd BLAST22
Transmembranei643 – 665Helical; Name=XUniRule annotationAdd BLAST23
Transmembranei707 – 727Helical; Name=XIUniRule annotationAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Photosystem I, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000886301 – 734Photosystem I P700 chlorophyll a apoprotein A2Add BLAST734

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

1734
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Helixi10 – 13Combined sources4
Helixi19 – 26Combined sources8
Turni27 – 29Combined sources3
Helixi31 – 33Combined sources3
Beta strandi34 – 36Combined sources3
Helixi39 – 71Combined sources33
Helixi74 – 79Combined sources6
Beta strandi81 – 84Combined sources4
Beta strandi87 – 90Combined sources4
Helixi98 – 103Combined sources6
Beta strandi109 – 111Combined sources3
Beta strandi113 – 115Combined sources3
Helixi120 – 127Combined sources8
Helixi132 – 157Combined sources26
Turni159 – 161Combined sources3
Helixi165 – 168Combined sources4
Helixi171 – 180Combined sources10
Turni181 – 183Combined sources3
Helixi184 – 196Combined sources13
Helixi198 – 202Combined sources5
Turni209 – 214Combined sources6
Turni219 – 222Combined sources4
Helixi223 – 227Combined sources5
Helixi230 – 234Combined sources5
Beta strandi244 – 249Combined sources6
Beta strandi260 – 262Combined sources3
Turni263 – 266Combined sources4
Helixi270 – 287Combined sources18
Beta strandi288 – 291Combined sources4
Beta strandi294 – 296Combined sources3
Helixi301 – 307Combined sources7
Turni314 – 321Combined sources8
Helixi322 – 327Combined sources6
Helixi330 – 354Combined sources25
Beta strandi358 – 360Combined sources3
Beta strandi362 – 364Combined sources3
Helixi365 – 396Combined sources32
Helixi401 – 403Combined sources3
Helixi407 – 413Combined sources7
Helixi415 – 445Combined sources31
Helixi449 – 451Combined sources3
Helixi458 – 466Combined sources9
Helixi477 – 479Combined sources3
Helixi484 – 488Combined sources5
Turni490 – 493Combined sources4
Helixi494 – 501Combined sources8
Beta strandi504 – 506Combined sources3
Helixi514 – 539Combined sources26
Turni540 – 542Combined sources3
Beta strandi547 – 549Combined sources3
Helixi550 – 552Combined sources3
Helixi563 – 565Combined sources3
Helixi572 – 603Combined sources32
Helixi606 – 612Combined sources7
Helixi616 – 622Combined sources7
Turni623 – 625Combined sources3
Helixi626 – 628Combined sources3
Helixi629 – 632Combined sources4
Turni633 – 635Combined sources3
Helixi636 – 638Combined sources3
Helixi644 – 665Combined sources22
Helixi668 – 683Combined sources16
Helixi688 – 690Combined sources3
Beta strandi694 – 696Combined sources3
Helixi702 – 730Combined sources29

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4XK8X-ray2.80B/b2-734[»]
4Y28X-ray2.80B1-733[»]
ProteinModelPortaliP05311.
SMRiP05311.
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. 1 hit.
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
PDB 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[»]
4XK8X-ray2.80B/b2-734[»]
4Y28X-ray2.80B1-733[»]
ProteinModelPortaliP05311.
SMRiP05311.
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. 1 hit.
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...

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: November 2, 2016
This is version 113 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

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.