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Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)

 PSAB_CHLRE              Reviewed;         735 AA.
P09144; B7U1I8; Q36714; Q8HR52; Q9GH44;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
28-MAR-2003, sequence version 4.
16-JAN-2019, entry version 150.
RecName: Full=Photosystem I P700 chlorophyll a apoprotein A2;
EC=1.97.1.12;
AltName: Full=PSI-B;
AltName: Full=PsaB;
Name=psaB; Synonyms=ps1a2;
Chlamydomonas reinhardtii (Chlamydomonas smithii).
Plastid; Chloroplast.
Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae;
Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
NCBI_TaxID=3055;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CC-406;
PubMed=16453785;
Kueck U., Choquet Y., Schneider M., Dron M., Bennoun P.;
"Structural and transcription analysis of two homologous genes for the
P700 chlorophyll a-apoproteins in Chlamydomonas reinhardtii: evidence
for in vivo trans-splicing.";
EMBO J. 6:2185-2195(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Forsyth A.M., Redding K., Purton S.;
"Revised sequence of the Chlamydomonas reinhardtii chloroplast gene
psaB.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=CC-503;
PubMed=19473533; DOI=10.1186/1471-2148-9-120;
Smith D.R., Lee R.W.;
"Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
addressing the mutational-hazard hypothesis.";
BMC Evol. Biol. 9:120-120(2009).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-578.
STRAIN=137c / CC-125;
PubMed=11083939; DOI=10.1006/mpev.2000.0831;
Nozaki H., Misawa K., Kajita T., Kato M., Nohara S., Watanabe M.M.;
"Origin and evolution of the colonial Volvocales (Chlorophyceae) as
inferred from multiple, chloroplast gene sequences.";
Mol. Phylogenet. Evol. 17:256-268(2000).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 493-735.
PubMed=6302265; DOI=10.1016/0022-2836(82)90547-2;
Dron M., Rahire M., Rochaix J.-D.;
"Sequence of the chloroplast DNA region of Chlamydomonas reinhardii
containing the gene of the large subunit of ribulose bisphosphate
carboxylase and parts of its flanking genes.";
J. Mol. Biol. 162:775-793(1982).
[6]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANT AC-U-G-2.3).
STRAIN=CC-2341;
PubMed=1959594; DOI=10.1016/0014-5793(91)80851-S;
Bingham S.E., Xu R.H., Webber A.N.;
"Transformation of chloroplasts with the psaB gene encoding a
polypeptide of the photosystem I reaction center.";
FEBS Lett. 292:137-140(1991).
[7]
IDENTIFICATION, AND COMPLETE PLASTID GENOME.
PubMed=12417694; DOI=10.1105/tpc.006155;
Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W.,
Harris E.H., Stern D.B.;
"The Chlamydomonas reinhardtii plastid chromosome: islands of genes in
a sea of repeats.";
Plant Cell 14:2659-2679(2002).
[8]
MUTAGENESIS OF PRO-559 AND CYS-560.
STRAIN=137c / CC-125, and CC-2341;
PubMed=8509430;
Webber A.N., Gibbs P.B., Ward J.B., Bingham S.E.;
"Site-directed mutagenesis of the photosystem I reaction center in
chloroplasts. The proline-cysteine motif.";
J. Biol. Chem. 268:12990-12995(1993).
[9]
MUTAGENESIS OF ASP-561; PRO-563 AND ARG-565.
STRAIN=137c / CC-125;
PubMed=7756260; DOI=10.1021/bi00019a010;
Rodday S.M., Webber A.N., Bingham S.E., Biggins J.;
"Evidence that the FX domain in photosystem I interacts with the
subunit PsaC: site-directed changes in PsaB destabilize the subunit
interaction in Chlamydomonas reinhardtii.";
Biochemistry 34:6328-6334(1995).
[10]
MUTAGENESIS OF HIS-655.
STRAIN=FuD7;
PubMed=8841129; DOI=10.1021/bi961198w;
Webber A.N., Su H., Bingham S.E., Kaess H., Krabben L., Kuhn M.,
Jordan R., Schlodder E., Lubitz W.;
"Site-directed mutations affecting the spectroscopic characteristics
and midpoint potential of the primary donor in photosystem I.";
Biochemistry 35:12857-12863(1996).
[11]
MUTAGENESIS OF CONSERVED HISTIDINES.
STRAIN=137c / CC-125;
PubMed=9427740; DOI=10.1093/emboj/17.1.50;
Redding K., MacMillan F., Leibl W., Brettel K., Hanley J.,
Rutherford A.W., Breton J., Rochaix J.-D.;
"A systematic survey of conserved histidines in the core subunits of
photosystem I by site-directed mutagenesis reveals the likely axial
ligands of P700.";
EMBO J. 17:50-60(1998).
[12]
MUTAGENESIS OF HIS-655.
STRAIN=CC-2696;
PubMed=11041867; DOI=10.1021/bi001200q;
Krabben L., Schlodder E., Jordan R., Carbonera D., Giacometti G.,
Lee H., Webber A.N., Lubitz W.;
"Influence of the axial ligands on the spectral properties of P700 of
photosystem I: a study of site-directed mutants.";
Biochemistry 39:13012-13025(2000).
[13]
MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
STRAIN=137c / CC-125;
PubMed=11274371; DOI=10.1073/pnas.081078898;
Guergova-Kuras M., Boudreaux B., Joliot A., Joliot P., Redding K.;
"Evidence for two active branches for electron transfer in photosystem
I.";
Proc. Natl. Acad. Sci. U.S.A. 98:4437-4442(2001).
[14]
PRESENCE OF CHLOROPHYLL A' IN PSI.
STRAIN=IAM C-9;
PubMed=12755700; DOI=10.1046/j.1432-1033.2003.03616.x;
Nakamura A., Akai M., Yoshida E., Taki T., Watanabe T.;
"Reversed-phase HPLC determination of chlorophyll a' and phylloquinone
in photosystem I of oxygenic photosynthetic organisms.";
Eur. J. Biochem. 270:2446-2458(2003).
[15]
MUTAGENESIS OF A1 PHYLLOQUINONE LIGANDS.
STRAIN=137c / CC-125;
PubMed=11489879; DOI=10.1074/jbc.M102327200;
Boudreaux B., MacMillan F., Teutloff C., Agalarov R., Gu F.,
Grimaldi S., Bittl R., Brettel K., Redding K.;
"Mutations in both sides of the photosystem I reaction center identify
the phylloquinone observed by electron paramagnetic resonance
spectroscopy.";
J. Biol. Chem. 276:37299-37306(2001).
-!- 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/cytochrome c6-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 or cytochrome c6.
-!- FUNCTION: Both potential cofactor branches in PSI seem to be
active; however, electron transfer seems to proceed preferentially
down the path including the phylloquinone bound by PsaA.
-!- CATALYTIC ACTIVITY:
Reaction=hnu + oxidized [2Fe-2S]-[ferredoxin] + reduced
[plastocyanin] = oxidized [plastocyanin] + reduced [2Fe-2S]-
[ferredoxin]; Xref=Rhea:RHEA:30407, Rhea:RHEA-COMP:10000,
Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:10039, Rhea:RHEA-
COMP:10040, ChEBI:CHEBI:29036, ChEBI:CHEBI:30212,
ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:49552;
EC=1.97.1.12;
-!- COFACTOR:
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. {ECO:0000250};
-!- SUBUNIT: 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.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane;
Multi-pass membrane protein.
-!- SIMILARITY: Belongs to the PsaA/PsaB family. {ECO:0000305}.
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EMBL; X05848; CAA29287.1; -; Genomic_DNA.
EMBL; U57326; AAN78307.1; -; Genomic_DNA.
EMBL; FJ423446; ACJ50135.1; -; Genomic_DNA.
EMBL; AB044470; BAB18396.1; -; Genomic_DNA.
EMBL; J01399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; S67792; AAB20423.2; -; Genomic_DNA.
EMBL; BK000554; DAA00949.2; -; Genomic_DNA.
PIR; B28341; B28341.
PIR; S18319; S18319.
RefSeq; NP_958404.1; NC_005353.1.
ProteinModelPortal; P09144; -.
SMR; P09144; -.
IntAct; P09144; 4.
STRING; 3055.DAA00949; -.
PaxDb; P09144; -.
GeneID; 2717038; -.
KEGG; cre:ChreCp048; -.
eggNOG; ENOG410IE88; Eukaryota.
eggNOG; ENOG410Y2QV; LUCA.
InParanoid; P09144; -.
KO; K02690; -.
OrthoDB; 209831at2759; -.
BioCyc; MetaCyc:CHRECP048-MONOMER; -.
BRENDA; 1.97.1.12; 1318.
Proteomes; UP000006906; Chloroplast.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009522; C:photosystem I; IEA:UniProtKB-KW.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-UniRule.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
Gene3D; 1.20.1130.10; -; 1.
HAMAP; MF_00482; PSI_PsaB; 1.
InterPro; IPR001280; PSI_PsaA/B.
InterPro; IPR020586; PSI_PsaA/B_CS.
InterPro; IPR036408; PSI_PsaA/B_sf.
InterPro; IPR006244; PSI_PsaB.
Pfam; PF00223; PsaA_PsaB; 1.
PIRSF; PIRSF002905; PSI_A; 1.
PRINTS; PR00257; PHOTSYSPSAAB.
SUPFAM; SSF81558; SSF81558; 1.
TIGRFAMs; TIGR01336; psaB; 1.
PROSITE; PS00419; PHOTOSYSTEM_I_PSAAB; 1.
1: Evidence at protein level;
4Fe-4S; Chlorophyll; Chloroplast; Chromophore; Complete proteome;
Electron transport; Iron; Iron-sulfur; Magnesium; Membrane;
Metal-binding; Oxidoreductase; Photosynthesis; Photosystem I; Plastid;
Reference proteome; Thylakoid; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 735 Photosystem I P700 chlorophyll a
apoprotein A2.
/FTId=PRO_0000088609.
TRANSMEM 47 70 Helical; Name=I. {ECO:0000255}.
TRANSMEM 136 159 Helical; Name=II. {ECO:0000255}.
TRANSMEM 176 200 Helical; Name=III. {ECO:0000255}.
TRANSMEM 274 292 Helical; Name=IV. {ECO:0000255}.
TRANSMEM 331 354 Helical; Name=V. {ECO:0000255}.
TRANSMEM 370 396 Helical; Name=VI. {ECO:0000255}.
TRANSMEM 418 440 Helical; Name=VII. {ECO:0000255}.
TRANSMEM 518 536 Helical; Name=VIII. {ECO:0000255}.
TRANSMEM 576 597 Helical; Name=IX. {ECO:0000255}.
TRANSMEM 644 666 Helical; Name=X. {ECO:0000255}.
TRANSMEM 708 728 Helical; Name=XI. {ECO:0000255}.
METAL 560 560 Iron-sulfur (4Fe-4S); shared with dimeric
partner.
METAL 569 569 Iron-sulfur (4Fe-4S); shared with dimeric
partner. {ECO:0000250}.
METAL 655 655 Magnesium (chlorophyll-a B1 axial ligand;
P700 special pair).
METAL 663 663 Magnesium (chlorophyll-a B3 axial
ligand). {ECO:0000250}.
BINDING 671 671 Chlorophyll-a B3. {ECO:0000250}.
BINDING 672 672 Phylloquinone B.
MUTAGEN 559 559 P->A,L: Assembles functional PSI.
Reaction center is somewhat unstable and
interaction with psaC is impaired. The
LEU mutant is less stable than the ALA
mutant. {ECO:0000269|PubMed:8509430}.
MUTAGEN 560 560 C->H: Loss of PSI assembly and function.
{ECO:0000269|PubMed:8509430}.
MUTAGEN 561 561 D->N: Loss of PSI assembly and function.
{ECO:0000269|PubMed:7756260}.
MUTAGEN 563 563 P->L: Assembles functional PSI. Reaction
center is somewhat unstable and
interaction with psaC is impaired.
{ECO:0000269|PubMed:7756260}.
MUTAGEN 565 565 R->E: Loss of PSI assembly and function.
{ECO:0000269|PubMed:7756260}.
MUTAGEN 655 655 H->C,G,N,S: Contains somewhat decreased
amounts of PSI, depending on the strain;
significantly changes the spin density of
the P700+ cation radical.
{ECO:0000269|PubMed:11041867,
ECO:0000269|PubMed:8841129}.
MUTAGEN 655 655 H->D: Very little PSI detected.
{ECO:0000269|PubMed:11041867,
ECO:0000269|PubMed:8841129}.
MUTAGEN 655 655 H->F,L: Loss of P700 function.
{ECO:0000269|PubMed:11041867,
ECO:0000269|PubMed:8841129}.
MUTAGEN 655 655 H->Q: Impairment of P700 function. More
severe; when associated with Q-676 in
psaA. {ECO:0000269|PubMed:11041867,
ECO:0000269|PubMed:8841129}.
MUTAGEN 655 655 H->R: No PSI detected.
{ECO:0000269|PubMed:11041867,
ECO:0000269|PubMed:8841129}.
MUTAGEN 672 672 W->F: Still able to photoaccumulate an
electron on A1.
CONFLICT 15 15 Q -> R (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 18 18 T -> A (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 21 21 R -> I (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 37 38 GM -> VW (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 48 49 FA -> IS (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 89 89 A -> C (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 203 203 S -> LQ (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 298 298 I -> N (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 335 335 L -> I (in Ref. 1; CAA29287).
{ECO:0000305}.
CONFLICT 515 515 P -> L (in Ref. 1 and 5). {ECO:0000305}.
SEQUENCE 735 AA; 82109 MW; 82F9914CE07A7908 CRC64;
MATKLFPKFS QGLAQDPTTR RIWYGLAMAH DFESHDGMTE ENLYQKIFAS HFGQLSIIFL
WTSGNLFHVA WQGNFEQWVT DPVHIRPIAH AIWDPHFGQP AVEAFTRGGA SGPVNISTSG
VYQWWYTIGM RTNQDLYVGS VFLALVSAIF LFAGWLHLQP NFQPSLSWFK DAESRLNHHL
SGLFGVSSLA WTGHLVHVAI PESRGQHVGW DNFLSVLPHP QGLTPFFTGN WAAYAQSPDT
ASHVFGTAQG SGQAILTFLG GFHPQTQSLW LTDMAHHHLA IAVIFIVAGH MYRTNFGIGH
RMQAILEAHT PPSGSLGAGH KGLFDTVNNS LHFQLGLALA SVGTITSLVA QHMYSLPPYA
FQAIDFTTQA ALYTHHQYIA GFIMCGAFAH GAIFFIRDYD PEQNKGNVLA RMLDHKEALI
SHLSWVSLFL GFHTLGLYVH NDVMQAFGTP EKQILIEPVF AQWIQAAHGK ALYGFDFLLS
SKTSAAFANG QSLWLPGWLD AINNNQNSLF LTIGPGDFLV HHAIALGLHT TTLILVKGAL
DARGSKLMPD KKDFGYSFPC DGPGRGGTCD ISAYDAFYLA VFWMLNTIGW VTFYWHWKHL
TLWQGNVAQF DESSTYLMGW LRDYLWLNSS QLINGYNPFG MNSLSVWAWT FLFGHLIYAT
GFMFLISWRG YWQELIETLV WAHEKTPLAN LVYWKDKPVA LSIVQARLVG LAHFSVGYIF
TYAAFLIAST SGRFG


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Pathways :
WP1461: Photosynthetic Carbon Reduction
WP1689: Porphyrin and chlorophyll metabolism
WP2230: Chlorophyll b degradation

Related Genes :
[psaB ps1a2] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB slr1835] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PsaB)
[psaB tlr0732] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PsaB)
[psaB AtCg00340] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB glr3439] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaA ps1a1] Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12) (PSI-A) (PsaA)
[psaA AtCg00350] Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12) (PSI-A) (PsaA)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PsaB)
[psaB1 Ava_2406] Photosystem I P700 chlorophyll a apoprotein A2 1 (EC 1.97.1.12) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaA tlr0731] Photosystem I P700 chlorophyll a apoprotein A1 (EC 1.97.1.12) (PsaA)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB CYB_0021] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB ps1a2] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB LOC_Osp1g00330 Nip049] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB psaA2] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB 9311047] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB PA049] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB OtCpg00500] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)
[psaB] Photosystem I P700 chlorophyll a apoprotein A2 (EC 1.97.1.12) (PSI-B) (PsaB)

Bibliography :