Photosystem I P700 chlorophyll a apoprotein A1 - Sequoia sempervirens (California redwood)

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Q9MUK3 (PSAA_SEQSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 64. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Photosystem I P700 chlorophyll a apoprotein A1
EC=1.97.1.12

Alternative name(s):
PSI-A
PsaA

Gene names

Name:

psaA

Encoded on

Plastid; Chloroplast

Organism

Sequoia sempervirens (California redwood) (Taxodium sempervirens)

Taxonomic identifier

28980 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Coniferopsida › Coniferales › Cupressaceae › Sequoia

Protein attributes

Sequence length	720 AA.
Sequence status	Fragment.
Protein existence	Inferred from homology

General annotation (Comments)

Function	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. HAMAP-Rule MF_00458
Catalytic activity	Reduced plastocyanin + oxidized ferredoxin + light = oxidized plastocyanin + reduced ferredoxin. HAMAP-Rule MF_00458
Cofactor	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.
Subunit structure	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 By similarity.
Subcellular location	Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein By similarity HAMAP-Rule MF_00458.
Sequence similarities	Belongs to the PsaA/PsaB family.

Ontologies

Keywords
Biological process	Electron transport Photosynthesis Transport
Cellular component	Chloroplast Membrane Photosystem I Plastid Thylakoid
Domain	Transmembrane Transmembrane helix
Ligand	4Fe-4S Chlorophyll Chromophore Iron Iron-sulfur Magnesium Metal-binding
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW photosynthesis Inferred from electronic annotation. Source: UniProtKB-KW protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	chloroplast thylakoid membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW photosystem I Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW chlorophyll binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

‹1 – ›720

›720

Photosystem I P700 chlorophyll a apoprotein A1 HAMAP-Rule MF_00458

PRO_0000088576

Regions

Transmembrane

61 – 84

Helical; Name=I; Potential

Transmembrane

147 – 170

Helical; Name=II; Potential

Transmembrane

186 – 210

Helical; Name=III; Potential

Transmembrane

282 – 300

Helical; Name=IV; Potential

Transmembrane

337 – 360

Helical; Name=V; Potential

Transmembrane

376 – 402

Helical; Name=VI; Potential

Transmembrane

424 – 446

Helical; Name=VII; Potential

Transmembrane

522 – 540

Helical; Name=VIII; Potential

Transmembrane

580 – 601

Helical; Name=IX; Potential

Transmembrane

655 – 677

Helical; Name=X; Potential

Transmembrane

715 – ›720

›6

Helical; Name=XI; Potential

Sites

Metal binding

564

Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity

Metal binding

573

Iron-sulfur (4Fe-4S); shared with dimeric partner By similarity

Metal binding

666

Magnesium (chlorophyll-a' A1 axial ligand; P700 special pair) By similarity

Metal binding

674

Magnesium (chlorophyll-a A3 axial ligand) By similarity

Binding site

682

Chlorophyll-a A3 By similarity

Binding site

683

Phylloquinone A By similarity

Experimental info

Non-terminal residue

720

Sequences

Sequence

Length

Mass (Da)

Tools

Q9MUK3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 1BE8F3BF22D9D1D8
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FASTA

720

80,039

        10         20         30         40         50         60 
IKIVVERDPI KTSFEKWAKP GHFSKTLAKG PNTTTWIWNL HADAHDFDSH TNDLEEISRK 

        70         80         90        100        110        120 
VFSAHFGQLA IIFIWLSGMY FHGARFSNYE AWLGDPTHIK PSAQVVWPIV GQEILNGDVG 

       130        140        150        160        170        180 
GGFRGIQITS GFFQIWRASG ITSELQLYCT AIGALIFAAL MLFAGWFHYH KAAPKLAWFQ 

       190        200        210        220        230        240 
DVESMLNHHL AGLLGLGSLS WAGHQIHVSL PINELLDAGV DPKEIPLPHE FILNRELLAQ 

       250        260        270        280        290        300 
LYPSFAKGLT PFFTLNWSEY SEFLTFRGGL NPVTGGLWLT DTAHHHLAIA ILFLIAGHMY 

       310        320        330        340        350        360 
RTNWSIGHNL KEILEAHKGP FTGEGHRGLY EILTTSWHAQ LALNLAMLGS LTIVVAHHMY 

       370        380        390        400        410        420 
SMPPYPYLAT DYGTQLSLFT HHMWIGGFLI VGAAAHAAIF MVRDYDPTTQ YNNLLDRVLR 

       430        440        450        460        470        480 
HRDAIVSHLN WACIFLGFHS FGLYIHNDTM SALGRPKDMF SDTAIQLQPI FAQWIQNTHA 

       490        500        510        520        530        540 
LAPSLTAPDA TASTSLTWGG GDLVAVGAKV ALLPIPLGTA DFLVHHIHAF TIHVTVLILL 

       550        560        570        580        590        600 
KGVLFARSSR LIPDKVNLGF RFPCDGPGRG GTCQVSAWDH VFLGLFWMYN AISVVIFHFS 

       610        620        630        640        650        660 
WKMQSDVWGS ISDQGVVTHI TGGNFAQSSI TINGWLRDFL WAQASQVIQS YGSSLSAYGL 

       670        680        690        700        710        720 
LFLGAHFVWA FSLMFLFSGR GYWQELIESI VWAHNKLKVA PAIQPRALSI VQGRAVGVAH

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References

[1]	"Error, bias, and long-branch attraction in data for two chloroplast photosystem genes in seed plants." Sanderson M.J., Wojciechowski M.F., Hu J.-M., Sher Khan T., Brady S.G. Mol. Biol. Evol. 17:782-797(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF180012 Genomic DNA. Translation: AAF29813.1.
3D structure databases
ProteinModelPortal	Q9MUK3.
SMR	Q9MUK3. Positions 14-720.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	1.20.1130.10. 1 hit.
HAMAP	MF_00458. PSI_PsaA.
InterPro	IPR006243. PSI_PsaA. IPR001280. PSI_PsaA/B. IPR020586. PSI_PsaA/B_CS. [Graphical view]
Pfam	PF00223. PsaA_PsaB. 1 hit. [Graphical view]
PIRSF	PIRSF002905. PSI_A. 1 hit.
PRINTS	PR00257. PHOTSYSPSAAB.
TIGRFAMs	TIGR01335. psaA. 1 hit.
PROSITE	PS00419. PHOTOSYSTEM_I_PSAAB. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PSAA_SEQSE

Accession

Primary (citable) accession number: Q9MUK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents