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 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)DescriptionActionsGraphical viewLength
Metal bindingi581Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation1
Metal bindingi590Iron-sulfur (4Fe-4S); shared with dimeric partnerUniRule annotation1
Metal bindingi683Magnesium (chlorophyll-a' A1 axial ligand; P700 special pair)UniRule annotation1
Metal bindingi691Magnesium (chlorophyll-a A3 axial ligand)UniRule annotation1
Binding sitei699Chlorophyll-a A3UniRule annotation1
Binding sitei700Phylloquinone AUniRule 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 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)DescriptionActionsGraphical viewLength
Transmembranei78 – 101Helical; Name=IUniRule annotationAdd BLAST24
Transmembranei164 – 187Helical; Name=IIUniRule annotationAdd BLAST24
Transmembranei203 – 227Helical; Name=IIIUniRule annotationAdd BLAST25
Transmembranei299 – 317Helical; Name=IVUniRule annotationAdd BLAST19
Transmembranei354 – 377Helical; Name=VUniRule annotationAdd BLAST24
Transmembranei393 – 419Helical; Name=VIUniRule annotationAdd BLAST27
Transmembranei441 – 463Helical; Name=VIIUniRule annotationAdd BLAST23
Transmembranei539 – 557Helical; Name=VIIIUniRule annotationAdd BLAST19
Transmembranei597 – 618Helical; Name=IXUniRule annotationAdd BLAST22
Transmembranei672 – 694Helical; Name=XUniRule annotationAdd BLAST23
Transmembranei732 – 753Helical; Name=XIUniRule annotationAdd BLAST22

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_00000885681 – 758Photosystem I P700 chlorophyll a apoprotein A1Add BLAST758

Proteomic databases

PRIDEiP05310.

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

1758
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 24Combined sources3
Beta strandi26 – 28Combined sources3
Turni31 – 35Combined sources5
Turni37 – 40Combined sources4
Helixi44 – 46Combined sources3
Helixi52 – 59Combined sources8
Beta strandi60 – 62Combined sources3
Helixi64 – 66Combined sources3
Helixi71 – 102Combined sources32
Helixi106 – 111Combined sources6
Turni113 – 115Combined sources3
Beta strandi119 – 121Combined sources3
Helixi129 – 132Combined sources4
Beta strandi133 – 137Combined sources5
Beta strandi140 – 144Combined sources5
Helixi149 – 155Combined sources7
Helixi161 – 187Combined sources27
Beta strandi189 – 191Combined sources3
Helixi193 – 196Combined sources4
Helixi199 – 208Combined sources10
Helixi211 – 224Combined sources14
Helixi226 – 235Combined sources10
Helixi239 – 241Combined sources3
Helixi247 – 250Combined sources4
Helixi252 – 258Combined sources7
Helixi260 – 264Combined sources5
Helixi267 – 270Combined sources4
Helixi274 – 277Combined sources4
Turni278 – 280Combined sources3
Turni289 – 291Combined sources3
Helixi296 – 313Combined sources18
Beta strandi320 – 322Combined sources3
Helixi327 – 333Combined sources7
Turni337 – 345Combined sources9
Helixi346 – 349Combined sources4
Turni350 – 352Combined sources3
Helixi354 – 378Combined sources25
Beta strandi382 – 384Combined sources3
Helixi389 – 420Combined sources32
Turni424 – 426Combined sources3
Helixi430 – 437Combined sources8
Helixi439 – 469Combined sources31
Helixi473 – 475Combined sources3
Beta strandi476 – 478Combined sources3
Turni479 – 481Combined sources3
Beta strandi482 – 484Combined sources3
Helixi487 – 498Combined sources12
Turni499 – 503Combined sources5
Beta strandi504 – 506Combined sources3
Beta strandi508 – 511Combined sources4
Beta strandi515 – 517Combined sources3
Beta strandi521 – 523Combined sources3
Beta strandi526 – 529Combined sources4
Helixi536 – 561Combined sources26
Beta strandi562 – 565Combined sources4
Helixi572 – 575Combined sources4
Turni586 – 588Combined sources3
Helixi594 – 623Combined sources30
Beta strandi626 – 628Combined sources3
Helixi630 – 632Combined sources3
Beta strandi634 – 638Combined sources5
Helixi642 – 645Combined sources4
Beta strandi646 – 648Combined sources3
Helixi649 – 654Combined sources6
Helixi657 – 660Combined sources4
Helixi662 – 665Combined sources4
Beta strandi670 – 672Combined sources3
Helixi673 – 694Combined sources22
Helixi697 – 713Combined sources17
Beta strandi719 – 721Combined sources3
Helixi727 – 757Combined sources31

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti117G → R in CAA29003 (Ref. 1) Curated1
Sequence conflicti176G → A in CAA29003 (Ref. 1) Curated1
Sequence conflicti194A → V in CAA29003 (Ref. 1) Curated1
Sequence conflicti220R → G in CAA29003 (Ref. 1) Curated1
Sequence conflicti239 – 253Missing (Ref. 1) CuratedAdd BLAST15
Sequence conflicti345G → GPFTGQGHKGPFTGQGHKG (Ref. 1) Curated1
Sequence conflicti371 – 378VVAQHMYS → IAAHHMIA in CAA29003 (Ref. 1) Curated8
Sequence conflicti382Y → I in CAA29003 (Ref. 1) Curated1
Sequence conflicti390A → G in CAA29003 (Ref. 1) Curated1
Sequence conflicti509A → T in CAA29003 (Ref. 1) Curated1
Sequence conflicti514T → I in CAA29003 (Ref. 1) Curated1
Sequence conflicti522A → S in CAA29003 (Ref. 1) Curated1
Sequence conflicti525N → G in CAA29003 (Ref. 1) Curated1
Sequence conflicti596D → V in CAA29003 (Ref. 1) Curated1
Sequence conflicti608S → A in CAA29003 (Ref. 1) Curated1
Sequence conflicti627T → S in CAA29003 (Ref. 1) Curated1
Sequence conflicti639 – 641AGN → GGR in CAA29003 (Ref. 1) Curated3

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60281N.

Proteomic databases

PRIDEiP05310.

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: November 2, 2016
This is version 116 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.