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3.E.2.1.2
Reaction Center of four subunits, PufC, PufM, PufL and PuhA together with light-harvesting complex 1 of two subunits, LH1α and LH1β. The 3-D structure of the supercomplex with both RC and LH1 has been solved to 1.9 Å resolution (Kishi et al. 2020). The QB quinone binding site is converted to QBH2 upon light-induced reduction and QBH2 is transported to the quinone pool in the membrane through the LH1 ring. Quinone transport in Tch. tepidum occurs through the size-restricted hydrophobic channels in the closed LH1 ring and are consistent with structural studies that have revealed narrow hydrophobic channels in the Tch. tepidum LH1 transmembrane region (Kishi et al. 2020). The cryo-EM structure of the Rhodobacter sphaeroides RC-LH1 core monomer complex has been solved at 2.5 Å (Qian et al. 2021).

Accession Number:A8ASG6
Protein Name:Reaction center protein M chain
Length:325
Molecular Weight:36577.00
Species:Thermochromatium tepidum [1050]
Number of TMSs:5
Location1 / Topology2 / Orientation3: Cellular chromatophore membrane1 / Multi-pass membrane protein2
Substrate

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FASTA formatted sequence
1:	MPEYQNIFTA VQVRAPAYPG VPLPKGNLPR IGRPIFSYWL GKIGDAQIGP IYLGLTGTLS 
61:	IFFGLVAISI IGFNMLASVH WDVFQFLKHF FWLGLEPPPP QYGLRIPPLS EGGWWLMAGL 
121:	FLTLSILLWW VRTYKRAEAL GMSQHLSWAF AAAIFFYLVL GFIRPVMMGS WAKAVPFGIF 
181:	PHLDWTAAFS IRYGNLYYNP FHMLSIAFLY GSALLFAMHG ATILSVSRFG GDREIDQITH 
241:	RGTAAERAAL FWRWTMGFNV TMESIHRWAW WCAVLTVITA GIGILLSGTV VDNWYLWAVK 
301:	HGMAPAYPEV VTAVNPYETA AEVMQ