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Protein

Photosystem I P700 chlorophyll a apoprotein A1

Gene

psaA

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.

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 bindingi581 – 5811Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi590 – 5901Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation
Metal bindingi683 – 6831Magnesium (chlorophyll-a' A1 axial ligand; P700 special pair)UniRule annotation
Metal bindingi691 – 6911Magnesium (chlorophyll-a A3 axial ligand)UniRule annotation
Binding sitei699 – 6991Chlorophyll-a A3UniRule annotation
Binding sitei700 – 7001Phylloquinone AUniRule 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 A1UniRule annotation (EC:1.97.1.12UniRule annotation)
Alternative name(s):
PSI-AUniRule annotation
PsaAUniRule annotation
Gene namesi
Name:psaAUniRule annotation
Synonyms:psaA1
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
Transmembranei78 – 10124Helical; Name=IUniRule annotationAdd
BLAST
Transmembranei164 – 18724Helical; Name=IIUniRule annotationAdd
BLAST
Transmembranei203 – 22725Helical; Name=IIIUniRule annotationAdd
BLAST
Transmembranei299 – 31719Helical; Name=IVUniRule annotationAdd
BLAST
Transmembranei354 – 37724Helical; Name=VUniRule annotationAdd
BLAST
Transmembranei393 – 41927Helical; Name=VIUniRule annotationAdd
BLAST
Transmembranei441 – 46323Helical; Name=VIIUniRule annotationAdd
BLAST
Transmembranei539 – 55719Helical; Name=VIIIUniRule annotationAdd
BLAST
Transmembranei597 – 61822Helical; Name=IXUniRule annotationAdd
BLAST
Transmembranei672 – 69423Helical; Name=XUniRule annotationAdd
BLAST
Transmembranei732 – 75322Helical; 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 – 758758Photosystem I P700 chlorophyll a apoprotein A1PRO_0000088568Add
BLAST

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-60281N.

Structurei

Secondary structure

1
758
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 243Combined sources
Beta strandi26 – 283Combined sources
Turni31 – 355Combined sources
Turni37 – 404Combined sources
Helixi44 – 463Combined sources
Helixi52 – 598Combined sources
Beta strandi60 – 623Combined sources
Helixi64 – 663Combined sources
Helixi71 – 10232Combined sources
Helixi106 – 1116Combined sources
Turni113 – 1153Combined sources
Beta strandi119 – 1213Combined sources
Helixi129 – 1324Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi140 – 1445Combined sources
Helixi149 – 1557Combined sources
Helixi161 – 18727Combined sources
Beta strandi189 – 1913Combined sources
Helixi193 – 1964Combined sources
Helixi199 – 20810Combined sources
Helixi211 – 22414Combined sources
Helixi226 – 23510Combined sources
Helixi239 – 2413Combined sources
Helixi247 – 2504Combined sources
Helixi252 – 2587Combined sources
Helixi260 – 2645Combined sources
Helixi267 – 2704Combined sources
Helixi274 – 2774Combined sources
Turni278 – 2803Combined sources
Turni289 – 2913Combined sources
Helixi296 – 31318Combined sources
Beta strandi320 – 3223Combined sources
Helixi327 – 3337Combined sources
Turni337 – 3459Combined sources
Helixi346 – 3494Combined sources
Turni350 – 3523Combined sources
Helixi354 – 37825Combined sources
Beta strandi382 – 3843Combined sources
Helixi389 – 42032Combined sources
Turni424 – 4263Combined sources
Helixi430 – 4378Combined sources
Helixi439 – 46931Combined sources
Helixi473 – 4753Combined sources
Beta strandi476 – 4783Combined sources
Turni479 – 4813Combined sources
Beta strandi482 – 4843Combined sources
Helixi487 – 49812Combined sources
Turni499 – 5035Combined sources
Beta strandi504 – 5063Combined sources
Beta strandi508 – 5114Combined sources
Beta strandi515 – 5173Combined sources
Beta strandi521 – 5233Combined sources
Beta strandi526 – 5294Combined sources
Helixi536 – 56126Combined sources
Beta strandi562 – 5654Combined sources
Helixi572 – 5754Combined sources
Turni586 – 5883Combined sources
Helixi594 – 62330Combined sources
Beta strandi626 – 6283Combined sources
Helixi630 – 6323Combined sources
Beta strandi634 – 6385Combined sources
Helixi642 – 6454Combined sources
Beta strandi646 – 6483Combined sources
Helixi649 – 6546Combined sources
Helixi657 – 6604Combined sources
Helixi662 – 6654Combined sources
Beta strandi670 – 6723Combined sources
Helixi673 – 69422Combined sources
Helixi697 – 71317Combined sources
Beta strandi719 – 7213Combined sources
Helixi727 – 75731Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO9model-A1-758[»]
2O01X-ray3.40A5-758[»]
2WSCX-ray3.30A1-758[»]
2WSEX-ray3.49A1-758[»]
2WSFX-ray3.48A1-758[»]
3LW5X-ray3.30A21-758[»]
4RKUX-ray3.00A38-758[»]
4XK8X-ray2.80A/a17-758[»]
4Y28X-ray2.80A1-758[»]
ProteinModelPortaliP05310.
SMRiP05310. Positions 31-758.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05310.

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_00458. PSI_PsaA. 1 hit.
InterProiIPR006243. PSI_PsaA.
IPR001280. PSI_PsaA/B.
IPR020586. PSI_PsaA/B_CS.
[Graphical view]
PfamiPF00223. PsaA_PsaB. 1 hit.
[Graphical view]
PIRSFiPIRSF002905. PSI_A. 1 hit.
PRINTSiPR00257. PHOTSYSPSAAB.
SUPFAMiSSF81558. SSF81558. 1 hit.
TIGRFAMsiTIGR01335. psaA. 1 hit.
PROSITEiPS00419. PHOTOSYSTEM_I_PSAAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P05310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIIRSPEPKV QILADPEVKI LVDRDPIKTS FEQWAKPGHF SRTIAKGPDT
60 70 80 90 100
TTWIWNLHAD AHDFDSHTSD LEEISRKVFS AHFGQLSIIF LWLSGMYFHG
110 120 130 140 150
ARFSNYEAWL NDPTHIGPSA QVVWPIVGQE ILNGDVGGGF RGIQITSGFF
160 170 180 190 200
QIWRASGITS ELQLYCTAIG ALVFAGLMLF AGWFHYHKAA PKLAWFQDVE
210 220 230 240 250
SMLNHHLAGL LGLGSLSWAR HQVHVSLPIN QFLNAGVDPK EIPLPHEFIL
260 270 280 290 300
NRDLLAQLYP SFAEGATPFF TLNWSKYADF LTFRGGLDPL TGGLWLTDIA
310 320 330 340 350
HHHLAIAILF LIAGHMYRTN WGIGHGIKDI LEAHKGPFTG QGHKGLYEIL
360 370 380 390 400
TTSWHAQLSI NLAMLGSLTI VVAQHMYSMP PYPYLATDYA TQLSLFTHHM
410 420 430 440 450
WIGGFLIVGA AAHAAIFMVR DYDPTTRYND LLDRVLRHRD AIISHLNWVC
460 470 480 490 500
IFLGFHSFGL YIHNDTMSAL GRPQDMFSDT AIQLQPVFAQ WIQNTHALAP
510 520 530 540 550
GTTAPGATAS TSLTWGGGDL VAVGNKVALL PIPLGTADFL VHHIHAFTIH
560 570 580 590 600
VTVLILLKGV LFARSSRLIP DKANLGFRFP CDGPGRGGTC QVSAWDHVFL
610 620 630 640 650
GLFWMYNSIS VVIFHFSWKM QSDVWGTIND QGVVTHITAG NFAQSSITIN
660 670 680 690 700
GWLRDFLWAQ ASQVIQSYGS SLSAYGLFFL GAHFVWAFSL MFLFSGRGYW
710 720 730 740 750
QELIESIVWA HNKLKVAPAT QPRALSIVQG RAVGVTHYLL GGIATTWAFF

LARIIAVG
Length:758
Mass (Da):84,199
Last modified:October 18, 2001 - v2
Checksum:i4B6CA42A585294A2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171G → R in CAA29003 (Ref. 1) Curated
Sequence conflicti176 – 1761G → A in CAA29003 (Ref. 1) Curated
Sequence conflicti194 – 1941A → V in CAA29003 (Ref. 1) Curated
Sequence conflicti220 – 2201R → G in CAA29003 (Ref. 1) Curated
Sequence conflicti239 – 25315Missing (Ref. 1) CuratedAdd
BLAST
Sequence conflicti345 – 3451G → GPFTGQGHKGPFTGQGHKG (Ref. 1) Curated
Sequence conflicti371 – 3788VVAQHMYS → IAAHHMIA in CAA29003 (Ref. 1) Curated
Sequence conflicti382 – 3821Y → I in CAA29003 (Ref. 1) Curated
Sequence conflicti390 – 3901A → G in CAA29003 (Ref. 1) Curated
Sequence conflicti509 – 5091A → T in CAA29003 (Ref. 1) Curated
Sequence conflicti514 – 5141T → I in CAA29003 (Ref. 1) Curated
Sequence conflicti522 – 5221A → S in CAA29003 (Ref. 1) Curated
Sequence conflicti525 – 5251N → G in CAA29003 (Ref. 1) Curated
Sequence conflicti596 – 5961D → V in CAA29003 (Ref. 1) Curated
Sequence conflicti608 – 6081S → A in CAA29003 (Ref. 1) Curated
Sequence conflicti627 – 6271T → S in CAA29003 (Ref. 1) Curated
Sequence conflicti639 – 6413AGN → GGR in CAA29003 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05423 Genomic DNA. Translation: CAA29003.1.
AF223227 Genomic DNA. Translation: AAF65219.1.
PIRiS00703.
RefSeqiYP_003587538.1. NC_014057.1.

Genome annotation databases

GeneIDi9073071.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05423 Genomic DNA. Translation: CAA29003.1.
AF223227 Genomic DNA. Translation: AAF65219.1.
PIRiS00703.
RefSeqiYP_003587538.1. NC_014057.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YO9model-A1-758[»]
2O01X-ray3.40A5-758[»]
2WSCX-ray3.30A1-758[»]
2WSEX-ray3.49A1-758[»]
2WSFX-ray3.48A1-758[»]
3LW5X-ray3.30A21-758[»]
4RKUX-ray3.00A38-758[»]
4XK8X-ray2.80A/a17-758[»]
4Y28X-ray2.80A1-758[»]
ProteinModelPortaliP05310.
SMRiP05310. Positions 31-758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60281N.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi9073071.

Miscellaneous databases

EvolutionaryTraceiP05310.

Family and domain databases

Gene3Di1.20.1130.10. 1 hit.
HAMAPiMF_00458. PSI_PsaA. 1 hit.
InterProiIPR006243. PSI_PsaA.
IPR001280. PSI_PsaA/B.
IPR020586. PSI_PsaA/B_CS.
[Graphical view]
PfamiPF00223. PsaA_PsaB. 1 hit.
[Graphical view]
PIRSFiPIRSF002905. PSI_A. 1 hit.
PRINTSiPR00257. PHOTSYSPSAAB.
SUPFAMiSSF81558. SSF81558. 1 hit.
TIGRFAMsiTIGR01335. psaA. 1 hit.
PROSITEiPS00419. PHOTOSYSTEM_I_PSAAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPSAA_PEA
AccessioniPrimary (citable) accession number: P05310
Secondary accession number(s): Q9MUB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: October 18, 2001
Last modified: December 9, 2015
This is version 114 of the entry and version 2 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.