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Photosystem II protein D1 1 (PSII D1 protein 1) (EC 1.10.3.9) (Photosystem II Q(B) protein 1)

 PSBA1_THEEB             Reviewed;         360 AA.
P0A444; P35876;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
25-APR-2018, entry version 107.
RecName: Full=Photosystem II protein D1 1 {ECO:0000255|HAMAP-Rule:MF_01379};
Short=PSII D1 protein 1 {ECO:0000255|HAMAP-Rule:MF_01379};
EC=1.10.3.9 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:25006873};
AltName: Full=Photosystem II Q(B) protein 1 {ECO:0000255|HAMAP-Rule:MF_01379};
Flags: Precursor;
Name=psbA1 {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000305};
Synonyms=psbA-1; OrderedLocusNames=tlr1843;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BP-1;
PubMed=12240834; DOI=10.1093/dnares/9.4.123;
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N.,
Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.;
"Complete genome structure of the thermophilic cyanobacterium
Thermosynechococcus elongatus BP-1.";
DNA Res. 9:123-130(2002).
[2]
X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 1-360.
PubMed=11217865; DOI=10.1038/35055589;
Zouni A., Witt H.T., Kern J., Fromme P., Krauss N., Saenger W.,
Orth P.;
"Crystal structure of photosystem II from Synechococcus elongatus at
3.8 A resolution.";
Nature 409:739-743(2001).
[3]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
DOI=10.1039/B406989G;
Biesiadka J., Loll B., Kern J., Irrgang K.-D., Zouni A.;
"Crystal structure of cyanobacterial photosystem II at 3.2 A
resolution: a closer look at the Mn-cluster.";
Phys. Chem. Chem. Phys. 6:4733-4736(2004).
[4]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=14764885; DOI=10.1126/science.1093087;
Ferreira K.N., Iverson T.M., Maghlaoui K., Barber J., Iwata S.;
"Architecture of the photosynthetic oxygen-evolving center.";
Science 303:1831-1838(2004).
[5]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=16355230; DOI=10.1038/nature04224;
Loll B., Kern J., Saenger W., Zouni A., Biesiadka J.;
"Towards complete cofactor arrangement in the 3.0 A resolution
structure of photosystem II.";
Nature 438:1040-1044(2005).
[6]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
STRAIN=BP-1;
PubMed=19219048; DOI=10.1038/nsmb.1559;
Guskov A., Kern J., Gabdulkhakov A., Broser M., Zouni A., Saenger W.;
"Cyanobacterial photosystem II at 2.9-A resolution and the role of
quinones, lipids, channels and chloride.";
Nat. Struct. Mol. Biol. 16:334-342(2009).
[7]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR
LOCATION.
STRAIN=BP-1;
PubMed=20558739; DOI=10.1074/jbc.M110.127589;
Broser M., Gabdulkhakov A., Kern J., Guskov A., Muh F., Saenger W.,
Zouni A.;
"Crystal structure of monomeric photosystem II from
Thermosynechococcus elongatus at 3.6 A resolution.";
J. Biol. Chem. 285:26255-26262(2010).
[8]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II IN
COMPLEX WITH HERBICIDE, FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR
LOCATION.
STRAIN=BP-1;
PubMed=21367867; DOI=10.1074/jbc.M110.215970;
Broser M., Glockner C., Gabdulkhakov A., Guskov A., Buchta J.,
Kern J., Muh F., Dau H., Saenger W., Zouni A.;
"Structural basis of cyanobacterial photosystem II inhibition by the
herbicide terbutryn.";
J. Biol. Chem. 286:15964-15972(2011).
[9]
X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=22665786; DOI=10.1073/pnas.1204598109;
Kern J., Alonso-Mori R., Hellmich J., Tran R., Hattne J., Laksmono H.,
Glockner C., Echols N., Sierra R.G., Sellberg J., Lassalle-Kaiser B.,
Gildea R.J., Glatzel P., Grosse-Kunstleve R.W., Latimer M.J.,
McQueen T.A., DiFiore D., Fry A.R., Messerschmidt M., Miahnahri A.,
Schafer D.W., Seibert M.M., Sokaras D., Weng T.C., Zwart P.H.,
White W.E., Adams P.D., Bogan M.J., Boutet S., Williams G.J.,
Messinger J., Sauter N.K., Zouni A., Bergmann U., Yano J.,
Yachandra V.K.;
"Room temperature femtosecond X-ray diffraction of photosystem II
microcrystals.";
Proc. Natl. Acad. Sci. U.S.A. 109:9721-9726(2012).
[10]
X-RAY CRYSTALLOGRAPHY (5.70 ANGSTROMS) IN PHOTOSYSTEM II, COFACTOR,
SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=23413188; DOI=10.1126/science.1234273;
Kern J., Alonso-Mori R., Tran R., Hattne J., Gildea R.J., Echols N.,
Glockner C., Hellmich J., Laksmono H., Sierra R.G.,
Lassalle-Kaiser B., Koroidov S., Lampe A., Han G., Gul S., Difiore D.,
Milathianaki D., Fry A.R., Miahnahri A., Schafer D.W.,
Messerschmidt M., Seibert M.M., Koglin J.E., Sokaras D., Weng T.C.,
Sellberg J., Latimer M.J., Grosse-Kunstleve R.W., Zwart P.H.,
White W.E., Glatzel P., Adams P.D., Bogan M.J., Williams G.J.,
Boutet S., Messinger J., Zouni A., Sauter N.K., Yachandra V.K.,
Bergmann U., Yano J.;
"Simultaneous femtosecond X-ray spectroscopy and diffraction of
photosystem II at room temperature.";
Science 340:491-495(2013).
[11]
X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 11-344 IN PHOTOSYSTEM II,
COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
STRAIN=BP-1;
PubMed=25043005; DOI=10.1038/nature13453;
Kupitz C., Basu S., Grotjohann I., Fromme R., Zatsepin N.A.,
Rendek K.N., Hunter M.S., Shoeman R.L., White T.A., Wang D., James D.,
Yang J.H., Cobb D.E., Reeder B., Sierra R.G., Liu H., Barty A.,
Aquila A.L., Deponte D., Kirian R.A., Bari S., Bergkamp J.J.,
Beyerlein K.R., Bogan M.J., Caleman C., Chao T.C., Conrad C.E.,
Davis K.M., Fleckenstein H., Galli L., Hau-Riege S.P., Kassemeyer S.,
Laksmono H., Liang M., Lomb L., Marchesini S., Martin A.V.,
Messerschmidt M., Milathianaki D., Nass K., Ros A., Roy-Chowdhury S.,
Schmidt K., Seibert M., Steinbrener J., Stellato F., Yan L., Yoon C.,
Moore T.A., Moore A.L., Pushkar Y., Williams G.J., Boutet S.,
Doak R.B., Weierstall U., Frank M., Chapman H.N., Spence J.C.,
Fromme P.;
"Serial time-resolved crystallography of photosystem II using a
femtosecond X-ray laser.";
Nature 513:261-265(2014).
[12]
X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF 1-344 IN PHOTOSYSTEM II,
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND SUBCELLULAR
LOCATION.
STRAIN=BP-1;
PubMed=25006873; DOI=10.1038/ncomms5371;
Kern J., Tran R., Alonso-Mori R., Koroidov S., Echols N., Hattne J.,
Ibrahim M., Gul S., Laksmono H., Sierra R.G., Gildea R.J., Han G.,
Hellmich J., Lassalle-Kaiser B., Chatterjee R., Brewster A.S.,
Stan C.A., Gloeckner C., Lampe A., DiFiore D., Milathianaki D.,
Fry A.R., Seibert M.M., Koglin J.E., Gallo E., Uhlig J., Sokaras D.,
Weng T.C., Zwart P.H., Skinner D.E., Bogan M.J., Messerschmidt M.,
Glatzel P., Williams G.J., Boutet S., Adams P.D., Zouni A.,
Messinger J., Sauter N.K., Bergmann U., Yano J., Yachandra V.K.;
"Taking snapshots of photosynthetic water oxidation using femtosecond
X-ray diffraction and spectroscopy.";
Nat. Commun. 5:4371-4371(2014).
-!- FUNCTION: Photosystem II (PSII) is a light-driven water:
plastoquinone oxidoreductase that uses light energy to abstract
electrons from H(2)O, generating O(2) and a proton gradient
subsequently used for ATP formation. It consists of a core antenna
complex that captures photons, and an electron transfer chain that
converts photonic excitation into a charge separation. The D1/D2
(PsbA/PsbA) reaction center heterodimer binds P680, the primary
electron donor of PSII as well as several subsequent electron
acceptors. {ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:25006873}.
-!- CATALYTIC ACTIVITY: 2 H(2)O + 2 plastoquinone + 4 light = O(2) + 2
plastoquinol. {ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:25006873}.
-!- COFACTOR:
Note=The D1/D2 heterodimer binds P680, chlorophylls that are the
primary electron donor of PSII, and subsequent electron acceptors.
It shares a non-heme iron and each subunit binds pheophytin,
quinone, additional chlorophylls, carotenoids and lipids. D1
provides most of the ligands for the Mn4-Ca-O5 cluster of the
oxygen-evolving complex (OEC). There is also a Cl(-1) ion
associated with D1 and D2, which is required for oxygen evolution
(PubMed:19219048, PubMed:21367867). PSII binds additional
chlorophylls, carotenoids and specific lipids. {ECO:0000255|HAMAP-
Rule:MF_01379, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.3};
-!- SUBUNIT: Cyanobacterial PSII is composed of 1 copy each of
membrane proteins PsbA, PsbB, PsbC, PsbD, PsbE, PsbF, PsbH, PsbI,
PsbJ, PsbK, PsbL, PsbM, PsbT, PsbX, PsbY, PsbZ, Ycf12, at least 3
peripheral proteins PsbO, PsbU, PsbV and a large number of
cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP-
Rule:MF_01379, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.3}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.3}; Multi-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.3}.
-!- PTM: C-terminally processed by CtpA; processing is essential to
allow assembly of the oxygen-evolving complex and thus
photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}.
-!- PTM: Tyr-161 forms a radical intermediate that is referred to as
redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000303|PubMed:11217865, ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:19219048, ECO:0000303|PubMed:21367867,
ECO:0000303|Ref.3}.
-!- MASS SPECTROMETRY: Mass=38144; Mass_error=224; Method=MALDI;
Range=2-344; Note=Mass for C-terminally truncated D1. The measured
protein is probably a mixture of the products of the 3 psbA
genes.; Evidence={ECO:0000269|PubMed:19219048};
-!- MISCELLANEOUS: 2 of the reaction center chlorophylls (ChlD1 and
ChlD2) are entirely coordinated by water. {ECO:0000255|HAMAP-
Rule:MF_01379, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048}.
-!- MISCELLANEOUS: Herbicides such as terbutryn, atrazine, BNT, diuron
or ioxynil bind in the Q(B) binding site and block subsequent
electron transfer. {ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:21367867}.
-!- MISCELLANEOUS: Cyanobacteria usually contain more than 2 copies of
the psbA gene; this strain encodes 3. {ECO:0000255|HAMAP-
Rule:MF_01379, ECO:0000269|PubMed:12240834}.
-!- SIMILARITY: Belongs to the reaction center PufL/M/PsbA/D family.
{ECO:0000255|HAMAP-Rule:MF_01379}.
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EMBL; BA000039; BAC09395.1; -; Genomic_DNA.
RefSeq; NP_682633.1; NC_004113.1.
RefSeq; WP_011057680.1; NC_004113.1.
PDB; 1S5L; X-ray; 3.50 A; A/a=1-344.
PDB; 1W5C; X-ray; 3.20 A; A/G=1-360.
PDB; 2AXT; X-ray; 3.00 A; A/a=1-344.
PDB; 3KZI; X-ray; 3.60 A; A=1-344.
PDB; 4FBY; X-ray; 6.56 A; A/G=1-344.
PDB; 4IXQ; X-ray; 5.70 A; A/a=1-360.
PDB; 4IXR; X-ray; 5.90 A; A/a=1-360.
PDB; 4PBU; X-ray; 5.00 A; A/a=11-344.
PDB; 4PJ0; X-ray; 2.44 A; A/a=1-344.
PDB; 4RVY; X-ray; 5.50 A; A/a=11-344.
PDB; 4TNH; X-ray; 4.90 A; A/a=1-344.
PDB; 4TNI; X-ray; 4.60 A; A/a=1-344.
PDB; 4TNJ; X-ray; 4.50 A; A/a=1-344.
PDB; 4TNK; X-ray; 5.20 A; A/a=1-344.
PDB; 4V62; X-ray; 2.90 A; AA/BA=1-344.
PDB; 4V82; X-ray; 3.20 A; AA/BA=1-344.
PDB; 5E79; X-ray; 3.50 A; A/a=11-344.
PDB; 5E7C; X-ray; 4.50 A; A/a=11-344.
PDB; 5H2F; X-ray; 2.20 A; A/a=11-344.
PDB; 5KAF; X-ray; 3.00 A; A/a=1-344.
PDB; 5KAI; X-ray; 2.80 A; A/a=1-344.
PDB; 5MX2; X-ray; 2.20 A; A/a=1-344.
PDB; 5TIS; X-ray; 2.25 A; A/a=1-344.
PDBsum; 1S5L; -.
PDBsum; 1W5C; -.
PDBsum; 2AXT; -.
PDBsum; 3KZI; -.
PDBsum; 4FBY; -.
PDBsum; 4IXQ; -.
PDBsum; 4IXR; -.
PDBsum; 4PBU; -.
PDBsum; 4PJ0; -.
PDBsum; 4RVY; -.
PDBsum; 4TNH; -.
PDBsum; 4TNI; -.
PDBsum; 4TNJ; -.
PDBsum; 4TNK; -.
PDBsum; 4V62; -.
PDBsum; 4V82; -.
PDBsum; 5E79; -.
PDBsum; 5E7C; -.
PDBsum; 5H2F; -.
PDBsum; 5KAF; -.
PDBsum; 5KAI; -.
PDBsum; 5MX2; -.
PDBsum; 5TIS; -.
ProteinModelPortal; P0A444; -.
SMR; P0A444; -.
DIP; DIP-48487N; -.
IntAct; P0A444; 1.
STRING; 197221.tlr1843; -.
DrugBank; DB04735; MONOGALACTOSYL-DIACYLGLYCEROL.
EnsemblBacteria; BAC09395; BAC09395; BAC09395.
GeneID; 1010908; -.
KEGG; tel:tlr1843; -.
PATRIC; fig|197221.4.peg.1926; -.
eggNOG; ENOG4105EY5; Bacteria.
eggNOG; ENOG410XPX5; LUCA.
HOGENOM; HOG000246913; -.
KO; K02703; -.
OMA; ICCYMGR; -.
OrthoDB; POG091H15P4; -.
BioCyc; TELO197221:G1G3I-1875-MONOMER; -.
BRENDA; 1.10.3.9; 7763.
EvolutionaryTrace; P0A444; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016168; F:chlorophyll binding; IEA:UniProtKB-KW.
GO; GO:0045156; F:electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009772; P:photosynthetic electron transport in photosystem II; IEA:InterPro.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
GO; GO:0009635; P:response to herbicide; IEA:UniProtKB-KW.
CDD; cd09289; Photosystem-II_D1; 1.
Gene3D; 1.20.85.10; -; 1.
HAMAP; MF_01379; PSII_PsbA_D1; 1.
InterPro; IPR036854; Photo_II_D1/D2_sf.
InterPro; IPR000484; Photo_RC_L/M.
InterPro; IPR005867; PSII_D1.
PANTHER; PTHR33149; PTHR33149; 1.
Pfam; PF00124; Photo_RC; 1.
SUPFAM; SSF81483; SSF81483; 1.
TIGRFAMs; TIGR01151; psbA; 1.
PROSITE; PS00244; REACTION_CENTER; 1.
1: Evidence at protein level;
3D-structure; Calcium; Chlorophyll; Chromophore; Complete proteome;
Electron transport; Herbicide resistance; Iron; Magnesium; Manganese;
Membrane; Metal-binding; Oxidoreductase; Photosynthesis;
Photosystem II; Reference proteome; Thylakoid; Transmembrane;
Transmembrane helix; Transport.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:19219048}.
CHAIN 2 344 Photosystem II protein D1 1.
/FTId=PRO_0000090485.
PROPEP 345 360 {ECO:0000255|HAMAP-Rule:MF_01379}.
/FTId=PRO_0000316376.
TOPO_DOM 2 31 Cytoplasmic.
{ECO:0000269|PubMed:19219048}.
TRANSMEM 32 49 Helical. {ECO:0000269|PubMed:19219048}.
TOPO_DOM 50 114 Lumenal. {ECO:0000269|PubMed:19219048}.
TRANSMEM 115 130 Helical. {ECO:0000269|PubMed:19219048}.
TOPO_DOM 131 143 Cytoplasmic.
{ECO:0000269|PubMed:19219048}.
TRANSMEM 144 156 Helical. {ECO:0000269|PubMed:19219048}.
TOPO_DOM 157 196 Lumenal. {ECO:0000269|PubMed:19219048}.
TRANSMEM 197 214 Helical. {ECO:0000269|PubMed:19219048}.
TOPO_DOM 215 273 Cytoplasmic.
{ECO:0000269|PubMed:19219048}.
TRANSMEM 274 288 Helical. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:19219048}.
TOPO_DOM 289 344 Lumenal. {ECO:0000269|PubMed:19219048}.
REGION 264 265 Quinone (B). {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 118 118 Magnesium (chlorophyll-a ChlzD1 axial
ligand); via tele nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O];
calcium. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 170 170 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 189 189 Calcium-manganese-oxide [Ca-4Mn-5O];
calcium. {ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873}.
METAL 189 189 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 198 198 Magnesium (chlorophyll-a PD1 axial
ligand); via tele nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
METAL 215 215 Iron; shared with heterodimeric partner;
via tele nitrogen. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
METAL 272 272 Iron; shared with heterodimeric partner;
via tele nitrogen. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
METAL 332 332 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 2; via tele nitrogen.
{ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 1. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 333 333 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 3. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:19219048,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 2. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 342 342 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 4. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O];
calcium; via carboxylate.
{ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25043005}.
METAL 344 344 Calcium-manganese-oxide [Ca-4Mn-5O];
manganese 4; via carboxylate.
{ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:16355230,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
BINDING 126 126 Pheophytin D1. {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
BINDING 130 130 Pheophytin D1.
{ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
BINDING 147 147 Pheophytin D1.
{ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.3}.
BINDING 215 215 Quinone (B). {ECO:0000255|HAMAP-
Rule:MF_01379,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:22665786,
ECO:0000303|PubMed:23413188,
ECO:0000303|PubMed:25006873,
ECO:0000303|PubMed:25043005}.
SITE 161 161 Tyrosine radical intermediate.
{ECO:0000255|HAMAP-Rule:MF_01379,
ECO:0000303|PubMed:11217865,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:19219048,
ECO:0000303|PubMed:21367867,
ECO:0000303|Ref.3}.
SITE 190 190 Stabilizes free radical intermediate.
{ECO:0000255|HAMAP-Rule:MF_01379}.
SITE 344 345 Cleavage; by CtpA. {ECO:0000255|HAMAP-
Rule:MF_01379}.
HELIX 13 21 {ECO:0000244|PDB:5MX2}.
STRAND 24 28 {ECO:0000244|PDB:5MX2}.
HELIX 31 54 {ECO:0000244|PDB:5MX2}.
STRAND 62 64 {ECO:0000244|PDB:5MX2}.
HELIX 71 73 {ECO:0000244|PDB:5MX2}.
TURN 77 79 {ECO:0000244|PDB:5MX2}.
TURN 87 91 {ECO:0000244|PDB:5MX2}.
HELIX 96 98 {ECO:0000244|PDB:5H2F}.
STRAND 99 101 {ECO:0000244|PDB:5MX2}.
HELIX 102 108 {ECO:0000244|PDB:5MX2}.
HELIX 110 137 {ECO:0000244|PDB:5MX2}.
HELIX 143 158 {ECO:0000244|PDB:5MX2}.
HELIX 160 165 {ECO:0000244|PDB:5MX2}.
HELIX 168 170 {ECO:0000244|PDB:5MX2}.
HELIX 176 190 {ECO:0000244|PDB:5MX2}.
HELIX 192 194 {ECO:0000244|PDB:5MX2}.
HELIX 196 221 {ECO:0000244|PDB:5MX2}.
STRAND 229 231 {ECO:0000244|PDB:5MX2}.
HELIX 233 236 {ECO:0000244|PDB:5MX2}.
HELIX 248 258 {ECO:0000244|PDB:5MX2}.
HELIX 261 263 {ECO:0000244|PDB:5MX2}.
HELIX 268 293 {ECO:0000244|PDB:5MX2}.
TURN 294 296 {ECO:0000244|PDB:5MX2}.
STRAND 297 299 {ECO:0000244|PDB:5MX2}.
STRAND 309 311 {ECO:0000244|PDB:5H2F}.
HELIX 317 329 {ECO:0000244|PDB:5MX2}.
TURN 330 336 {ECO:0000244|PDB:5MX2}.
STRAND 339 341 {ECO:0000244|PDB:5MX2}.
SEQUENCE 360 AA; 39737 MW; D4B45833FA46A4D4 CRC64;
MTTTLQRRES ANLWERFCNW VTSTDNRLYV GWFGVIMIPT LLAATICFVI AFIAAPPVDI
DGIREPVSGS LLYGNNIITG AVVPSSNAIG LHFYPIWEAA SLDEWLYNGG PYQLIIFHFL
LGASCYMGRQ WELSYRLGMR PWICVAYSAP LASAFAVFLI YPIGQGSFSD GMPLGISGTF
NFMIVFQAEH NILMHPFHQL GVAGVFGGAL FCAMHGSLVT SSLIRETTET ESANYGYKFG
QEEETYNIVA AHGYFGRLIF QYASFNNSRS LHFFLAAWPV VGVWFTALGI STMAFNLNGF
NFNHSVIDAK GNVINTWADI INRANLGMEV MHERNAHNFP LDLASAESAP VAMIAPSING


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