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PMID:172499
| Citation |
Meyer, TE, Ambler, RP, Bartsch, RG and Kamen, MD (1975) Amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1. J. Biol. Chem. 250:8416-21 |
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| Abstract |
The amino acid sequence of cytochrome c' from the purple photosynthetic bacterium Rhodospirillum rubrum S1 has been determined and is consistent with homology to cytochrome c' from the nonphotosynthetic bacterium Alcaligenes sp. NCIB 11015. There is 29% identity in the chosen alignment of these two proteins. R. rubrum cytochrome c' is composed of a single peptide chain of 126 amino acid residues with a single heme covalently bound near the COOH terminus. There is no sequence similarity to mitochondrial cytochrome c, except at the heme binding site. |
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| Keywords |
Amino Acid Sequence; Chymotrypsin; Cytochrome c Group/analysis; Peptide Fragments/analysis; Peptide Hydrolases; Rhodospirillum rubrum/enzymology; Thermolysin; Trypsin |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0022900: electron transport chain |
ECO:0000247: |
UniProtKB:P00138
|
P |
Figure 2: Alignment with Alcaligenes sp. cytochrome c' sequence showing heme binding site. |
complete | |||
See also
References
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