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Cytochrome c-550 (Cytochrome c-549) (Cytochrome c550) (Low-potential cytochrome c)

 CY550_THEEB             Reviewed;         163 AA.
P0A386; P56150; Q9ETF4;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
15-MAR-2005, sequence version 1.
28-MAR-2018, entry version 104.
RecName: Full=Cytochrome c-550 {ECO:0000255|HAMAP-Rule:MF_01378};
AltName: Full=Cytochrome c-549;
AltName: Full=Cytochrome c550 {ECO:0000255|HAMAP-Rule:MF_01378};
AltName: Full=Low-potential cytochrome c {ECO:0000255|HAMAP-Rule:MF_01378};
Flags: Precursor;
Name=psbV {ECO:0000255|HAMAP-Rule:MF_01378};
OrderedLocusNames=tll1285;
Thermosynechococcus elongatus (strain BP-1).
Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
Thermosynechococcus.
NCBI_TaxID=197221;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
PubMed=11427679; DOI=10.1093/pcp/pce074;
Katoh H., Itoh S., Shen J.-R., Ikeuchi M.;
"Functional analysis of psbV and a novel c-type cytochrome gene psbV2
of the thermophilic cyanobacterium Thermosynechococcus elongatus
strain BP-1.";
Plant Cell Physiol. 42:599-607(2001).
[2]
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).
[3]
PROTEIN SEQUENCE OF 27-33, COFACTOR, AND SUBCELLULAR LOCATION.
PubMed=17935689; DOI=10.1016/j.bbabio.2007.08.008;
Kashino Y., Takahashi T., Inoue-Kashino N., Ban A., Ikeda Y.,
Satoh K., Sugiura M.;
"Ycf12 is a core subunit in the photosystem II complex.";
Biochim. Biophys. Acta 1767:1269-1275(2007).
[4]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-163, COFACTOR, SUBUNIT,
AND SUBCELLULAR LOCATION.
PubMed=12881497; DOI=10.1093/pcp/pcg084;
Kerfeld C.A., Sawaya M.R., Bottin H., Tran K.T., Sugiura M.,
Cascio D., Desbois A., Yeates T.O., Kirilovsky D., Boussac A.;
"Structural and EPR characterization of the soluble form of cytochrome
c-550 and of the psbV2 gene product from the cyanobacterium
Thermosynechococcus elongatus.";
Plant Cell Physiol. 44:697-706(2003).
[5]
X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
HEME, 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).
[6]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
HEME, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
DOI=10.1039/b406989g;
Biesiadka J., Loll B., Kern J., Irrgangb 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).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II WITH
HEME, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II
WITH HEME, 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).
[9]
X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II
WITH HEME, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR LOCATION, AND MASS
SPECTROMETRY.
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).
[10]
X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II
WITH HEME, FUNCTION, COFACTOR, SUBUNIT, AND SUBCELLULAR LOCATION.
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).
[11]
X-RAY CRYSTALLOGRAPHY (6.56 ANGSTROMS) OF 27-163 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).
[12]
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).
[13]
X-RAY CRYSTALLOGRAPHY (5.00 ANGSTROMS) OF 27-163 IN PHOTOSYSTEM II
WITH HEME, 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).
[14]
X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) IN PHOTOSYSTEM II, FUNCTION,
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: Low-potential cytochrome c that plays a role in the
oxygen-evolving complex of photosystem II. It is not essential for
growth under normal conditions but is required under low CO(2)
concentrations. PSII is a light-driven water plastoquinone
oxidoreductase, using light energy to abstract electrons from
H(2)O, generating a proton gradient subsequently used for ATP
formation. {ECO:0000269|PubMed:11427679,
ECO:0000269|PubMed:20558739, ECO:0000269|PubMed:21367867,
ECO:0000269|PubMed:25006873}.
-!- COFACTOR:
Note=Binds 1 heme group covalently per subunit. PSII binds
multiple chlorophylls, carotenoids and specific lipids.
{ECO:0000269|PubMed:12881497, ECO:0000269|PubMed:14764885,
ECO:0000269|PubMed:16355230, ECO:0000269|PubMed:17935689,
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.6};
-!- SUBUNIT: The cyanobacterial oxygen-evolving complex is composed of
PsbO, PsbP, PsbQ, PsbV and PsbU (By similarity). PsbP and PsbQ are
not seen in the crystal structures; however there is biochemical
evidence that they are part of the OEC. Monomer in the isolated
crystal structure. 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, 3
peripheral proteins PsbO, PsbU, PsbV and a large number of
cofactors. It forms dimeric complexes. {ECO:0000255|HAMAP-
Rule:MF_01378, ECO:0000269|PubMed:12881497,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048, ECO:0000269|PubMed:20558739,
ECO:0000269|PubMed:22665786, ECO:0000269|PubMed:23413188,
ECO:0000269|PubMed:25006873, ECO:0000269|PubMed:25043005,
ECO:0000269|Ref.6}.
-!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
{ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12881497,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, 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.6}; Peripheral membrane protein
{ECO:0000255|HAMAP-Rule:MF_01378, ECO:0000269|PubMed:12881497,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, 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.6}; Lumenal side {ECO:0000255|HAMAP-Rule:MF_01378,
ECO:0000269|PubMed:14764885, ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:17935689, 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.6}. Note=Associated with photosystem II at the
lumenal side of the thylakoid membrane.
-!- MASS SPECTROMETRY: Mass=15752; Mass_error=11; Method=MALDI;
Range=27-163; Note=Mass includes covalently attached heme group.;
Evidence={ECO:0000269|PubMed:19219048};
-!- MASS SPECTROMETRY: Mass=15743; Method=MALDI; Range=27-163;
Note=Mass includes covalently attached heme group.;
Evidence={ECO:0000269|PubMed:20558739};
-!- DISRUPTION PHENOTYPE: Cells do not grow photoautotrophically under
low CO(2) concentrations. {ECO:0000269|PubMed:11427679}.
-!- SIMILARITY: Belongs to the cytochrome c family. PsbV subfamily.
{ECO:0000255|HAMAP-Rule:MF_01378}.
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EMBL; AB052597; BAB20059.1; -; Genomic_DNA.
EMBL; BA000039; BAC08837.1; -; Genomic_DNA.
RefSeq; NP_682075.1; NC_004113.1.
RefSeq; WP_011057125.1; NC_004113.1.
PDB; 1MZ4; X-ray; 1.80 A; A=27-163.
PDB; 1S5L; X-ray; 3.50 A; V/v=27-163.
PDB; 1W5C; X-ray; 3.20 A; T/V=1-163.
PDB; 2AXT; X-ray; 3.00 A; V/v=27-163.
PDB; 3KZI; X-ray; 3.60 A; V=27-163.
PDB; 4FBY; X-ray; 6.56 A; V/i=27-163.
PDB; 4IXQ; X-ray; 5.70 A; V/v=1-163.
PDB; 4IXR; X-ray; 5.90 A; V/v=1-163.
PDB; 4PBU; X-ray; 5.00 A; V/v=27-163.
PDB; 4PJ0; X-ray; 2.44 A; V/v=1-163.
PDB; 4RVY; X-ray; 5.50 A; V/v=27-163.
PDB; 4TNH; X-ray; 4.90 A; V/v=1-163.
PDB; 4TNI; X-ray; 4.60 A; V/v=1-163.
PDB; 4TNJ; X-ray; 4.50 A; V/v=1-163.
PDB; 4TNK; X-ray; 5.20 A; V/v=1-163.
PDB; 4V62; X-ray; 2.90 A; AV/BV=27-163.
PDB; 4V82; X-ray; 3.20 A; AV/BV=27-163.
PDB; 5E79; X-ray; 3.50 A; V/v=27-163.
PDB; 5E7C; X-ray; 4.50 A; V/v=27-163.
PDB; 5H2F; X-ray; 2.20 A; V/v=27-163.
PDB; 5KAF; X-ray; 3.00 A; V/v=1-163.
PDB; 5KAI; X-ray; 2.80 A; V/v=1-163.
PDB; 5MX2; X-ray; 2.20 A; V/v=1-163.
PDB; 5TIS; X-ray; 2.25 A; V/v=1-163.
PDBsum; 1MZ4; -.
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; P0A386; -.
SMR; P0A386; -.
DIP; DIP-48502N; -.
IntAct; P0A386; 19.
STRING; 197221.tll1285; -.
EnsemblBacteria; BAC08837; BAC08837; BAC08837.
GeneID; 1011288; -.
KEGG; tel:tll1285; -.
PATRIC; fig|197221.4.peg.1352; -.
eggNOG; ENOG4108UQX; Bacteria.
eggNOG; ENOG4111IIK; LUCA.
HOGENOM; HOG000276786; -.
KO; K02720; -.
OMA; WGGGKIY; -.
OrthoDB; POG091H143E; -.
BioCyc; TELO197221:G1G3I-1307-MONOMER; -.
EvolutionaryTrace; P0A386; -.
Proteomes; UP000000440; Chromosome.
GO; GO:0009523; C:photosystem II; IEA:UniProtKB-KW.
GO; GO:0042651; C:thylakoid membrane; IEA:UniProtKB-SubCell.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0020037; F:heme binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
Gene3D; 1.10.760.10; -; 1.
HAMAP; MF_01378; PSII_Cyt550; 1.
InterPro; IPR009056; Cyt_c-like_dom.
InterPro; IPR036909; Cyt_c-like_dom_sf.
InterPro; IPR029490; Cytochrom_C550.
InterPro; IPR016003; PSII_cyt_c550.
InterPro; IPR017851; PSII_PsbV_cyt_c550.
Pfam; PF14495; Cytochrom_C550; 1.
PIRSF; PIRSF005890; Phot_II_cyt_c550; 1.
SUPFAM; SSF46626; SSF46626; 2.
TIGRFAMs; TIGR03045; PS_II_C550; 1.
PROSITE; PS51007; CYTC; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Electron transport; Heme; Iron; Membrane; Metal-binding;
Photosynthesis; Photosystem II; Reference proteome; Signal; Thylakoid;
Transport.
SIGNAL 1 26 {ECO:0000255|HAMAP-Rule:MF_01378,
ECO:0000269|PubMed:17935689,
ECO:0000269|PubMed:19219048,
ECO:0000269|PubMed:20558739}.
CHAIN 27 163 Cytochrome c-550.
/FTId=PRO_0000006518.
METAL 67 67 Iron (heme axial ligand).
{ECO:0000269|PubMed:12881497,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.6}.
METAL 118 118 Iron (heme axial ligand).
{ECO:0000269|PubMed:12881497,
ECO:0000269|PubMed:16355230,
ECO:0000269|PubMed:19219048,
ECO:0000303|PubMed:14764885,
ECO:0000303|PubMed:20558739,
ECO:0000303|PubMed:21367867,
ECO:0000303|PubMed:25043005,
ECO:0000303|Ref.6}.
HELIX 31 34 {ECO:0000244|PDB:1MZ4}.
STRAND 35 39 {ECO:0000244|PDB:1MZ4}.
STRAND 44 46 {ECO:0000244|PDB:1MZ4}.
HELIX 49 62 {ECO:0000244|PDB:1MZ4}.
HELIX 64 67 {ECO:0000244|PDB:1MZ4}.
HELIX 68 70 {ECO:0000244|PDB:1MZ4}.
STRAND 73 75 {ECO:0000244|PDB:1W5C}.
HELIX 76 78 {ECO:0000244|PDB:1MZ4}.
HELIX 82 86 {ECO:0000244|PDB:1MZ4}.
STRAND 88 90 {ECO:0000244|PDB:1MZ4}.
HELIX 95 103 {ECO:0000244|PDB:1MZ4}.
STRAND 110 113 {ECO:0000244|PDB:1MZ4}.
TURN 115 117 {ECO:0000244|PDB:1MZ4}.
HELIX 121 123 {ECO:0000244|PDB:1MZ4}.
TURN 124 126 {ECO:0000244|PDB:1MZ4}.
HELIX 128 130 {ECO:0000244|PDB:1MZ4}.
HELIX 135 152 {ECO:0000244|PDB:1MZ4}.
HELIX 153 155 {ECO:0000244|PDB:1MZ4}.
TURN 156 158 {ECO:0000244|PDB:5TIS}.
HELIX 160 162 {ECO:0000244|PDB:5H2F}.
SEQUENCE 163 AA; 18027 MW; DA634C5C4084F676 CRC64;
MLKKCVWLAV ALCLCLWQFT MGTALAAELT PEVLTVPLNS EGKTITLTEK QYLEGKRLFQ
YACASCHVGG ITKTNPSLDL RTETLALATP PRDNIEGLVD YMKNPTTYDG EQEIAEVHPS
LRSADIFPKM RNLTEKDLVA IAGHILVEPK ILGDKWGGGK VYY


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EIAAB10219 Cyba,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Mouse,Mus musculus,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,
E1557h ELISA kit 21-OHase,CYP21,CYP21A2,CYP21B,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Cytochrome P450-C21B,Homo sapiens,Human,Steroid 21-hydroxylase 96T
E1557h ELISA 21-OHase,CYP21,CYP21A2,CYP21B,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Cytochrome P450-C21B,Homo sapiens,Human,Steroid 21-hydroxylase 96T
EIAAB10221 Bos taurus,Bovine,CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,p22 phagocyte B-cytochrome,p22phox,p22-phox,S
U1557h CLIA 21-OHase,CYP21,CYP21A2,CYP21B,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Cytochrome P450-C21B,Homo sapiens,Human,Steroid 21-hydroxylase 96T
EIAAB10223 CYBA,Cytochrome b(558) alpha chain,Cytochrome b-245 light chain,Cytochrome b558 subunit alpha,Neutrophil cytochrome b 22 kDa polypeptide,Oryctolagus cuniculus,p22 phagocyte B-cytochrome,p22phox,p22-ph
EIAAB08923 Cyp2c12,Cyp2c-12,Cyp2c40,CYPIIC12,Cytochrome P450 15-beta,Cytochrome P450 2C12, female-specific,Cytochrome P450I,Cytochrome P450-UT-1,Cytochrome P450-UT-I,Rat,Rattus norvegicus
EIAAB08901 Cyp2b1,Cyp2b-1,CYPIIB1,Cytochrome P450 2B1,Cytochrome P450b,Cytochrome P450-B,Cytochrome P450-LM2,Cytochrome P450-PB1,Cytochrome P450-PB2,Rat,Rattus norvegicus
EIAAB08920 CYP2C8,CYPIIC8,Cytochrome P450 2C8,Cytochrome P450 form 1,Cytochrome P450 IIC2,Cytochrome P450 MP-12,Cytochrome P450 MP-20,Homo sapiens,Human,S-mephenytoin 4-hydroxylase
EIAAB08851 Cyp1a2,Cyp1a-2,CYPIA2,Cytochrome P-448,Cytochrome P450 1A2,Cytochrome P-450d,Cytochrome P450-D,Rat,Rattus norvegicus
EIAAB08879 CYP26A2,CYP26B1,Cytochrome P450 26A2,Cytochrome P450 26B1,Cytochrome P450 retinoic acid-inactivating 2,Cytochrome P450RAI-2,Homo sapiens,Human,P450RAI2,Retinoic acid-metabolizing cytochrome
EIAAB08922 Cyp2c,Cyp2c11,Cyp2c-11,CYPIIC11,Cytochrome P450 2C11,Cytochrome P-450(M-1),Cytochrome P450H,Cytochrome P450-UT-2,Cytochrome P450-UT-A,Rat,Rattus norvegicus
EIAAB08974 Albendazole monooxygenase,Albendazole sulfoxidase,CYP3A3,CYP3A4,CYPIIIA3,CYPIIIA4,Cytochrome P450 3A3,Cytochrome P450 3A4,Cytochrome P450 HLp,Cytochrome P450 NF-25,Cytochrome P450-PCN1,Homo sapiens,Hu
E1557m ELISA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
E1557m ELISA kit 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
U1557m CLIA 21-OHase,Cyp21,Cyp21a1,Cyp21a-1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Mouse,Mus musculus,Steroid 21-hydroxylase 96T
U1557p CLIA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
E1557p ELISA 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
E1557b ELISA 21-OHase,Bos taurus,Bovine,CYP21,CYP21A1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Steroid 21-hydroxylase 96T
EIAAB08924 Cyp2c13,Cyp2c-13,CYPIIC13,Cytochrome P450 2C13, male-specific,Cytochrome P-450g,Cytochrome P450-G,Cytochrome P450-UT-5,Rat,Rattus norvegicus
E1557p ELISA kit 21-OHase,CYP21,CYP21A1,CYP21A3,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Pig,Steroid 21-hydroxylase,Sus scrofa 96T
E1557r ELISA kit 21-OHase,Cyp21,Cyp21a1,Cytochrome P450 21,Cytochrome P450 XXI,Cytochrome P-450c21,Cytochrome P450-C21,Rat,Rattus norvegicus,Steroid 21-hydroxylase 96T


 

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