Reaction center protein M chain
Details
- Name
- Reaction center protein M chain
- Synonyms
- Photosynthetic reaction center M subunit
- Gene Name
- pufM
- Organism
- Rhodobacter sphaeroides
- Amino acid sequence
>lcl|BSEQ0012749|Reaction center protein M chain MAEYQNIFSQVQVRGPADLGMTEDVNLANRSGVGPFSTLLGWFGNAQLGPIYLGSLGVLS LFSGLMWFFTIGIWFWYQAGWNPAVFLRDLFFFSLEPPAPEYGLSFAAPLKEGGLWLIAS FFMFVAVWSWWGRTYLRAQALGMGKHTAWAFLSAIWLWMVLGFIRPILMGSWSEAVPYGI FSHLDWTNNFSLVHGNLFYNPFHGLSIAFLYGSALLFAMHGATILAVSRFGGERELEQIA DRGTAAERAALFWRWTMGFNATMEGIHRWAIWMAVLVTLTGGIGILLSGTVVDNWYVWGQ NHGMAPLN
- Number of residues
- 308
- Molecular Weight
- 34508.725
- Theoretical pI
- 6.63
- GO Classification
- Functionsbacteriochlorophyll binding / electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity / metal ion bindingProcessesphotosynthetic electron transport in photosystem II / protein-chromophore linkageComponentsintegral component of membrane / plasma membrane light-harvesting complex / plasma membrane-derived chromatophore membrane
- General Function
- The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
- Specific Function
- Bacteriochlorophyll binding
- Pfam Domain Function
- Photo_RC (PF00124)
- Transmembrane Regions
- 54-80 111-140 143-168 198-226 260-286
- Cellular Location
- Cellular chromatophore membrane
- Gene sequence
>lcl|BSEQ0007562|927 bp GAGGCATCAATGGCTGAGTATCAGAACATCTTCTCCCAGGTCCAGGTCCGCGGACCGGCC GACCTGGGGATGACCGAAGACGTCAACCTGGCCAACCGTTCGGGCGTCGGTCCCTTCTCG ACCCTGCTCGGCTGGTTCGGCAACGCCCAGCTCGGCCCGATCTATCTCGGCTCGCTCGGC GTCCTGTCCCTCTTCTCGGGCCTGATGTGGTTCTTCACCATCGGGATCTGGTTCTGGTAT CAGGCGGGCTGGAACCCGGCCGTCTTCCTGCGCGACCTGTTCTTCTTCTCGCTCGAGCCG CCGGCACCCGAATACGGTCTGTCCTTCGCGGCTCCGCTGAAGGAAGGCGGGCTGTGGCTG ATCGCGTCGTTCTTCATGTTCGTCGCGGTCTGGTCCTGGTGGGGCCGCACCTATCTCCGC GCTCAGGCGCTGGGCATGGGCAAGCACACCGCCTGGGCGTTCCTCTCGGCCATCTGGCTG TGGATGGTGCTGGGCTTCATCCGTCCGATCCTCATGGGGTCCTGGTCGGAAGCGGTTCCC TACGGCATCTTCTCGCACCTCGACTGGACGAACAACTTCTCGCTCGTCCACGGCAACCTG TTCTACAACCCCTTCCACGGTCTCTCGATCGCCTTCCTCTACGGGTCGGCCCTGCTCTTC GCGATGCACGGTGCGACCATCCTCGCGGTCTCCCGCTTCGGCGGCGAGCGCGAGCTGGAG CAGATCGCCGACCGCGGGACGGCAGCGGAGCGGGCCGCCCTCTTCTGGCGCTGGACCATG GGTTTCAACGCCACGATGGAAGGCATCCACCGCTGGGCCATCTGGATGGCGGTCCTCGTG ACCCTCACCGGCGGCATCGGCATCCTGCTCTCGGGCACGGTCGTGGACAACTGGTACGTC TGGGGCCAGAACCACGGCATGGCGCCG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0C0Y9 UniProtKB Entry Name RCEM_RHOSH GenBank Protein ID 152028 GenBank Gene ID K00827 - General References
- Williams JC, Steiner LA, Ogden RC, Simon MI, Feher G: Primary structure of the M subunit of the reaction center from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1983 Nov;80(21):6505-9. [Article]
- Arnoux B, Ducruix A, Astier C, Picaud M, Roth M, Reiss-Husson F: Towards the understanding of the function of Rb sphaeroides Y wild type reaction center: gene cloning, protein and detergent structures in the three-dimensional crystals. Biochimie. 1990 Aug;72(8):525-30. [Article]
- Williams JC, Steiner LA, Feher G, Simon MI: Primary structure of the L subunit of the reaction center from Rhodopseudomonas sphaeroides. Proc Natl Acad Sci U S A. 1984 Dec;81(23):7303-7. [Article]
- Chang CH, el-Kabbani O, Tiede D, Norris J, Schiffer M: Structure of the membrane-bound protein photosynthetic reaction center from Rhodobacter sphaeroides. Biochemistry. 1991 Jun 4;30(22):5352-60. [Article]
- Allen JP, Feher G, Yeates TO, Komiya H, Rees DC: Structure of the reaction center from Rhodobacter sphaeroides R-26: protein-cofactor (quinones and Fe2+) interactions. Proc Natl Acad Sci U S A. 1988 Nov;85(22):8487-91. [Article]
- Allen JP, Feher G, Yeates TO, Komiya H, Rees DC: Structure of the reaction center from Rhodobacter sphaeroides R-26: the protein subunits. Proc Natl Acad Sci U S A. 1987 Sep;84(17):6162-6. [Article]
- McAuley-Hecht KE, Fyfe PK, Ridge JP, Prince SM, Hunter CN, Isaacs NW, Cogdell RJ, Jones MR: Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal. Biochemistry. 1998 Apr 7;37(14):4740-50. [Article]