Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Cytochrome b559 subunit beta (PSII reaction center subunit VI)

 H2FA47_9ASPA            Unreviewed;        39 AA.
H2FA47;
21-MAR-2012, integrated into UniProtKB/TrEMBL.
21-MAR-2012, sequence version 1.
25-OCT-2017, entry version 34.
RecName: Full=Cytochrome b559 subunit beta {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
AltName: Full=PSII reaction center subunit VI {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
Name=psbF {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000313|EMBL:AEX95530.1};
Hosta ventricosa (blue plantain lily).
Plastid {ECO:0000313|EMBL:AEX95530.1}.
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Asparagaceae;
Agavoideae; Hosta.
NCBI_TaxID=39527 {ECO:0000313|EMBL:AEX95530.1};
[1] {ECO:0000313|EMBL:AFA27556.1}
NUCLEOTIDE SEQUENCE.
Givnish T.J., Ames M., McNeal J.R., McKain M.J., Steele P.R.,
dePamphilis C.W., Graham S.W., Pires J.C., Stevenson D.W.,
Zomlefer W.B., Briggs B.G., Duvall M.R., Moore M.J., Heaney J.M.,
Soltis D.E., Soltis P.S., Thiele K., Leebens-Mack J.H.;
"Assembling the Tree of the Monocotyledons: Plastome Sequence
Phylogeny and Evolution of Poales.";
Ann. Mo. Bot. Gard. 97:584-616(2010).
[2] {ECO:0000313|EMBL:AEX95530.1}
NUCLEOTIDE SEQUENCE.
PubMed=22291168; DOI=10.3732/ajb.1100491;
Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J.,
Pires J.C.;
"Quality and quantity of data recovered from massively parallel
sequencing: Examples in Asparagales and Poaceae.";
Am. J. Bot. 99:330-348(2012).
[3] {ECO:0000313|EMBL:APO12238.1}
NUCLEOTIDE SEQUENCE.
PubMed=27793858;
McKain M.R., McNeal J.R., Kellar P.R., Eguiarte L.E., Pires J.C.,
Leebens-Mack J.;
"Timing of rapid diversification and convergent origins of active
pollination within Agavoideae (Asparagaceae).";
Am. J. Bot. 103:1717-1729(2016).
-!- FUNCTION: This b-type cytochrome is tightly associated with the
reaction center of photosystem II (PSII). 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. {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000256|HAMAP-Rule:MF_00643};
Note=With its partner (PsbE) binds heme. PSII binds additional
chlorophylls, carotenoids and specific lipids. {ECO:0000256|HAMAP-
Rule:MF_00643};
-!- SUBUNIT: Heterodimer of an alpha subunit and a beta subunit. 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 of the oxygen-
evolving complex and a large number of cofactors. It forms dimeric
complexes. {ECO:0000256|HAMAP-Rule:MF_00643}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000256|HAMAP-Rule:MF_00643}; Single-pass membrane protein
{ECO:0000256|HAMAP-Rule:MF_00643}.
-!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
{ECO:0000256|RuleBase:RU004529}; Single-pass membrane protein
{ECO:0000256|RuleBase:RU004529}.
-!- SIMILARITY: Belongs to the PsbE/PsbF family. {ECO:0000256|HAMAP-
Rule:MF_00643, ECO:0000256|RuleBase:RU004529}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; JQ275701; AEX95530.1; -; Genomic_DNA.
EMBL; HQ182050; AFA27556.1; -; Genomic_DNA.
EMBL; KX931460; APO12238.1; -; Genomic_DNA.
RefSeq; YP_009335180.1; NC_032706.1.
ProteinModelPortal; H2FA47; -.
SMR; H2FA47; -.
GeneID; 30766941; -.
GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0009539; C:photosystem II reaction center; IEA:InterPro.
GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-UniRule.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
GO; GO:0009767; P:photosynthetic electron transport chain; IEA:InterPro.
HAMAP; MF_00643; PSII_PsbF; 1.
InterPro; IPR006241; PSII_cyt_b559_bsu.
InterPro; IPR006216; PSII_cyt_b559_CS.
InterPro; IPR013081; PSII_cyt_b559_N.
PANTHER; PTHR33391:SF3; PTHR33391:SF3; 1.
Pfam; PF00283; Cytochrom_B559; 1.
PIRSF; PIRSF000037; PsbF; 1.
TIGRFAMs; TIGR01333; cyt_b559_beta; 1.
PROSITE; PS00537; CYTOCHROME_B559; 1.
3: Inferred from homology;
Chloroplast {ECO:0000256|RuleBase:RU004529,
ECO:0000313|EMBL:AEX95530.1};
Electron transport {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529};
Heme {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
Iron {ECO:0000256|HAMAP-Rule:MF_00643, ECO:0000256|RuleBase:RU004529};
Membrane {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529};
Photosynthesis {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529};
Photosystem II {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529};
Plastid {ECO:0000256|RuleBase:RU004529, ECO:0000313|EMBL:AEX95530.1};
Thylakoid {ECO:0000256|HAMAP-Rule:MF_00643};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529};
Transport {ECO:0000256|HAMAP-Rule:MF_00643,
ECO:0000256|RuleBase:RU004529}.
TRANSMEM 15 37 Helical. {ECO:0000256|RuleBase:RU004529}.
DOMAIN 1 29 Cytochrom_B559.
{ECO:0000259|Pfam:PF00283}.
METAL 18 18 Iron (heme axial ligand); shared with
alpha subunit. {ECO:0000256|HAMAP-
Rule:MF_00643}.
NON_TER 39 39 {ECO:0000313|EMBL:AFA27556.1}.
SEQUENCE 39 AA; 4424 MW; F61251852D7E1D6F CRC64;
MTIDRTYPIF TVRWLAVHGL AVPTVSFLGS ISAMQFIQR


Related products :

Catalog number Product name Quantity
AS06113 PsbF | beta subunit of Cytochrome b559 of PSII 200 ul
AS06 113 PsbF | beta subunit of Cytochrome b559 of PSII 200 ul
AS06 113 rabbit polyclonal PsbF | beta subunit of Cytochrome b559 of PSII 200
AS06112 PsbE | alfa subunit of Cytochrome b559 of PSII 100 ul
AS06 112 PsbE | alfa subunit of Cytochrome b559 of PSII 100 ul
AS06 112 rabbit polyclonal PsbE | alfa subunit of Cytochrome b559 of PSII 100
AS06 113 Antibody: PsbF | beta subunit of Cytochrome b559 of PSII, Immunogen: KLH-conjugated synthetic peptide derived from plant PsbF sequences including Arabidopsis thaliana P62095, Host: rabbit, polyclonal, 200
20312192-1 PsbF | beta subunit of Cytochrome b559 o 200 uL
AS06 112 Antibody: PsbE | alfa subunit of Cytochrome b559 of PSII, Immunogen: KLH-conjugated synthetic peptide chosen from PsbE protein of Arabidopsis thaliana P56779, Host: rabbit, polyclonal, Confirmed react 100
20312191-1 PsbE | alfa subunit of Cytochrome b559 o 100 uL
EIAAB10228 CGD91-phox,CYBB,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Neutrophil cytochrome b 91 kDa pol
EIAAB10227 Cgd,CGD91-phox,Cybb,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Mouse,Mus musculus,Neutrophil
EIAAB10226 Bos taurus,Bovine,CGD91-phox,CYBB,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Neutrophil cytoc
EIAAB10225 CGD91-phox,CYBB,Cytochrome b(558) subunit beta,Cytochrome b-245 heavy chain,Cytochrome b558 subunit beta,gp91-1,gp91-phox,Heme-binding membrane glycoprotein gp91phox,Homo sapiens,Human,NADPH oxidase 2
EIAAB10234 COB,Complex III subunit 3,Complex III subunit III,CYTB,Cytochrome b,Cytochrome b-c1 complex subunit 3,Homo sapiens,Human,MTCYB,MT-CYB,Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
EIAAB10215 Complex III subunit 4,Complex III subunit IV,CYC1,Cytochrome b-c1 complex subunit 4,Cytochrome c-1,Cytochrome c1, heme protein, mitochondrial,Homo sapiens,Human,Ubiquinol-cytochrome-c reductase comple
EIAAB10105 COX7A2,COX7AL,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIaL,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart,Homo sapiens,Human
EIAAB10238 Bos taurus,Bovine,COB,Complex III subunit 3,Complex III subunit III,CYTB,Cytochrome b,Cytochrome b-c1 complex subunit 3,MTCYB,MT-CYB,Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
EIAAB10217 Complex III subunit 4,Complex III subunit IV,Cyc1,Cytochrome b-c1 complex subunit 4,Cytochrome c-1,Cytochrome c1, heme protein, mitochondrial,Mouse,Mus musculus,Ubiquinol-cytochrome-c reductase comple
EIAAB08785 Bos taurus,Bovine,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,IX,VIIIb
EIAAB08789 COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-liver_heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Oryctolagus cuniculus,Rabb
EIAAB10236 COB,Complex III subunit 3,Complex III subunit III,CYTB,Cytochrome b,Cytochrome b-c1 complex subunit 3,MTCYB,MT-CYB,Pig,Sus scrofa,Ubiquinol-cytochrome-c reductase complex cytochrome b subunit
EIAAB08787 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Mouse,Mus musculus
EIAAB08788 Cox8b,Cox8h,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase subunit 8H,Rat,Rattus norvegicus
EIAAB10216 Bos taurus,Bovine,Complex III subunit 4,Complex III subunit IV,CYC1,Cytochrome b-c1 complex subunit 4,Cytochrome c-1,Cytochrome c1, heme protein, mitochondrial,Ubiquinol-cytochrome-c reductase complex


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur