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Annotation rule MF_01831 |
Accession | MF_01831 |
Dates | 30-SEP-2004 (Created) 19-NOV-2019 (Last updated, Version 25) |
Name | SufS_aminotrans_5 |
Scope | Bacteria; Enterobacterales |
Templates | P77444 (SUFS_ECOLI); Q9EXP2 (SUFS_DICD3): [Recover all] |
Triggered by |
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Protein name |
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Gene name |
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Function | Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo. |
Catalytic activity | RHEA:43892: [sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine
EC 2.8.1.7 |
RHEA:11632: AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-alanine
EC 4.4.1.16 |
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Cofactor | pyridoxal 5'-phosphate |
Pathway | Cofactor biosynthesis; iron-sulfur cluster biosynthesis. |
Subunit | Homodimer. Interacts with SufE and the SufBCD complex composed of SufB, SufC and SufD. The interaction with SufE is required to mediate the direct transfer of the sulfur atom from the S-sulfanylcysteine. |
Subcellular location | Cytoplasm. |
Similarity | Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. Csd subfamily. |
From: SUFS_ECOLI (P77444) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ACT_SITE | 364 | 364 | Cysteine persulfide intermediate | C | ||||||||
MOD_RES | 226 | 226 | N6-(pyridoxal phosphate)lysine | K |
Size range | 406-412 amino acids |
Related rules | None |
Fusion | None |
Comments | The suf operon encodes a minor pathway of Fe-S cluster, which is probably activated and required only in specific stressfull conditions such as oxidative stress and/or iron limitation. Although cysteine desulfurase (EC 2.8.1.7) and selenocysteine lyase (EC 4.4.1.16) activities are reported as unrelated enzymatic reactions, they probably represent a same type of reaction, using either L-cysteine or L-selenocysteine as substrate, respectively. The catalytic activity for cysteine desulfurase reaction is incomplete, and lacks the direct transfer of the sulfur atom from the sufS-S-sulfanylcysteine |