Photosystem Q(B) protein precursor - Chlamydomonas reinhardtii

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P07753 (PSBA_CHLRE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 97. 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 Q(B) protein
EC=1.10.3.9

Alternative name(s):
32 kDa thylakoid membrane protein
Photosystem II protein D1

Gene names

Name:	psbA-A
AND
Name:	psbA-B

Encoded on

Plastid; Chloroplast

Organism

Chlamydomonas reinhardtii (Chlamydomonas smithii)

Taxonomic identifier

3055 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Chlorophyta › Chlorophyceae › Chlamydomonadales › Chlamydomonadaceae › Chlamydomonas

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This is one of the two reaction center proteins of photosystem II. HAMAP MF_01379
Catalytic activity	2 H₂O + 2 plastoquinone + 4 light = O₂ + 2 plastoquinol. HAMAP MF_01379
Cofactor	The psbA/B heterodimer binds P680, the primary electron donor of PSII. It shares a non-heme iron and each subunit binds additional chlorophylls and pheophytin. PsbA provides most of the ligands for the Mn-cluster of the oxygen-evolving complex By similarity.
Subunit structure	The psbA/B heterodimer binds the P680 chlorophylls and subsequent electron acceptors. PSII consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. PSII forms dimeric complexes By similarity.
Subcellular location	Plastid › chloroplast thylakoid membrane; Multi-pass membrane protein By similarity HAMAP MF_01379.
Miscellaneous	Herbicides such as atrazine, BNT, diuron or ioxynil bind to Q(B) and block electron transport. HAMAP MF_01379
Sequence similarities	Belongs to the reaction center pufL/M/psbA/D family.

Ontologies

Keywords
Biological process	Electron transport Herbicide resistance Photosynthesis Transport
Cellular component	Chloroplast Membrane Photosystem II Plastid Thylakoid
Domain	Transmembrane Transmembrane helix
Ligand	Iron Metal-binding
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	photosynthetic electron transport in photosystem II Inferred from electronic annotation. Source: InterPro response to herbicide Inferred from electronic annotation. Source: UniProtKB-KW transport 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 light-harvesting complex Inferred from electronic annotation. Source: InterPro photosystem II Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity Inferred from electronic annotation. Source: InterPro 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

Initiator methionine

Removed By similarity

Chain

2 – 344

343

Photosystem Q(B) protein HAMAP MF_01379

PRO_0000090432

Propeptide

345 – 352

Potential

PRO_0000316443

Regions

Transmembrane

36 – 56

Helical; Potential

Transmembrane

109 – 129

Helical; Potential

Transmembrane

141 – 164

Helical; Potential

Transmembrane

192 – 218

Helical; Potential

Transmembrane

269 – 289

Helical; Potential

Sites

Metal binding

215

Iron; shared with heterodimeric partner By similarity

Metal binding

272

Iron; shared with heterodimeric partner By similarity

Site

344 – 345

Cleavage; by ctpA By similarity

Amino acid modifications

Modified residue

N-acetylthreonine By similarity

Modified residue

Phosphothreonine By similarity

Experimental info

Mutagenesis

219

V → I: Herbicide resistance.

Mutagenesis

251

A → V: Herbicide resistance.

Mutagenesis

256

G → D: Herbicide resistance.

Mutagenesis

264

S → A: Herbicide resistance.

Mutagenesis

266

N → T: Herbicide resistance.

Mutagenesis

275

L → F: Herbicide resistance.

Mutagenesis

275

L → P: Herbicide resistance.

Sequences

Sequence

Length

Mass (Da)

Tools

P07753 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 844E0252B42421AB
Show »

FASTA

352

39,042

        10         20         30         40         50         60 
MTAILERREN SSLWARFCEW ITSTENRLYI GWFGVIMIPC LLTATSVFII AFIAAPPVDI 

        70         80         90        100        110        120 
DGIREPVSGS LLYGNNIITG AVIPTSNAIG LHFYPIWEAA SLDEWLYNGG PYQLIVCHFL 

       130        140        150        160        170        180 
LGVYCYMGRE WELSFRLGMR PWIAVAYSAP VAAASAVFLV YPIGQGSFSD GMPLGISGTF 

       190        200        210        220        230        240 
NFMIVFQAEH NILMHPFHML GVAGVFGGSL FSAMHGSLVT SSLIRETTEN ESANEGYRFG 

       250        260        270        280        290        300 
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV IGIWFTALGL STMAFNLNGF 

       310        320        330        340        350 
NFNQSVVDSQ GRVLNTWADI INRANLGMEV MHERNAHNFP LDLASTNSSS NN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Chlamydomonas reinhardii gene for the 32,000 mol. wt. protein of photosystem II contains four large introns and is located entirely within the chloroplast inverted repeat." Erickson J.M., Rahire M., Rochaix J.-D. EMBO J. 3:2753-2762(1984) [PubMed: 16453578] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide diversity in the chloroplast genome of Chlamydomonas reinhardtii." United States Department of Energy Joint Genome Institute Smith D.R. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CC-503.
[3]	"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats." Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H., Stern D.B. Plant Cell 14:2659-2679(2002) [PubMed: 12417694] [Abstract] Cited for: IDENTIFICATION, COMPLETE PLASTID GENOME.
[4]	"A new mutation in the gene coding for the herbicide-binding protein in Chlamydomonas." Johanningmeier U., Bodner U., Wildner G.F. FEBS Lett. 211:221-224(1987) Cited for: MUTAGENESIS FOR HERBICIDE RESISTANCE.
[5]	"Molecular and biophysical analysis of herbicide-resistant mutants of Chlamydomonas reinhardtii: structure-function relationship of the photosystem II D1 polypeptide." Erickson J.M., Pfister K., Rahire M., Togasaki R.K., Mets L., Rochaix J.-D. Plant Cell 1:361-371(1989) [PubMed: 2535507] [Abstract] Cited for: MUTAGENESIS FOR HERBICIDE RESISTANCE.
[6]	"Herbicide cross-resistance and mutations of the psbA gene in Chlamydomonas reinhardtii." Wildner G.F., Heisterkamp U., Trebst A. Z. Naturforsch. C 45:1142-1150(1990) Cited for: MUTAGENESIS FOR HERBICIDE RESISTANCE.
[7]	"Site-specific mutagenesis of the D1 subunit of photosystem II in wild-type Chlamydomonas." Przibilla E., Heiss S., Johanningmeier U., Trebst A. Plant Cell 3:169-174(1991) [PubMed: 1840907] [Abstract] Cited for: MUTAGENESIS FOR HERBICIDE RESISTANCE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X01424 , X02347, X02348, X02349, X02350 Genomic DNA. Translation: CAA25670.1. FJ423446 Genomic DNA. Translation: ACJ50111.1. FJ423446 Genomic DNA. Translation: ACJ50144.1. BK000554 Genomic DNA. Translation: DAA00922.1. BK000554 Genomic DNA. Translation: DAA00957.1.
PIR	A22780.
RefSeq	NP_958377.1. NC_005353.1. NP_958413.1. NC_005353.1.
3D structure databases
ProteinModelPortal	P07753.
SMR	P07753. Positions 10-344.
ModBase	Search...
Proteomic databases
PRIDE	P07753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	DAA00922; DAA00922; DAA00922. DAA00957; DAA00957; DAA00957.
GeneID	2716969. 2716987.
KEGG	cre:ChreCp021. cre:ChreCp057.
Phylogenomic databases
ProtClustDB	CHL00003.
Enzyme and pathway databases
BioCyc	CHLAMY:CHRECP021-MONOMER. CHLAMY:CHRECP057-MONOMER. MetaCyc:CHRECP057-MONOMER.
Family and domain databases
HAMAP	MF_01379. PSII_PsbA_D1. [Tree]
InterPro	IPR000484. Photo_RC_L/M. IPR005867. PSII_PsbA/D1. [Graphical view]
Gene3D	G3DSA:1.20.85.10. Photo_RC_L/M. 1 hit.
KO	K02703.
Pfam	PF00124. Photo_RC. 1 hit. [Graphical view]
PRINTS	PR00256. REACTNCENTRE.
SUPFAM	SSF81483. Photo_RC_L/M. 1 hit.
TIGRFAMs	TIGR01151. PsbA. 1 hit.
PROSITE	PS00244. REACTION_CENTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
PMAP-CutDB	P07753.

Entry information

Entry name

PSBA_CHLRE

Accession

Primary (citable) accession number: P07753
Secondary accession number(s): B7U1G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	December 14, 2011
This is version 97 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

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents