AC   MF_01831;
DC   Protein; auto
TR   HAMAP; MF_01831; -; 1; level=0
XX
Names: SufS_aminotrans_5
XX
ID   SUFS
DE   RecName: Full=Cysteine desulfurase;
DE            EC=2.8.1.7;
DE   AltName: Full=Selenocysteine beta-lyase;
DE            Short=SCL;
DE   AltName: Full=Selenocysteine lyase;
DE            EC=4.4.1.16;
DE   AltName: Full=Selenocysteine reductase;
GN   Name=sufS;
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CC   -!- FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to
CC       yield L-alanine, an essential step in sulfur metabolism for
CC       biosynthesis of a variety of sulfur-containing biomolecules. Component
CC       of the suf operon, which is activated and required under specific
CC       conditions such as oxidative stress and iron limitation. Acts as a
CC       potent selenocysteine lyase in vitro, that mobilizes selenium from L-
CC       selenocysteine. Selenocysteine lyase activity is however unsure in
CC       vivo.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC         alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC         COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC         ChEBI:CHEBI:64428; EC=2.8.1.7;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC         alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC         ChEBI:CHEBI:57972; EC=4.4.1.16;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC   -!- SUBUNIT: Homodimer. Interacts with SufE and the SufBCD complex composed
CC       of SufB, SufC and SufD. The interaction with SufE is required to
CC       mediate the direct transfer of the sulfur atom from the S-
CC       sulfanylcysteine.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. Csd subfamily.
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DR   Pfam; PF00266; Aminotran_5; 1; trigger=no
DR   NCBIfam; TIGR01979; SufS; 1; trigger=no
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1; trigger=no
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KW   Cytoplasm
KW   Lyase
KW   Pyridoxal phosphate
KW   Transferase
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GO   GO:0031071; F:cysteine desulfurase activity
GO   GO:0009000; F:selenocysteine lyase activity
GO   GO:0005737; C:cytoplasm
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FT   From: SUFS_ECOLI (P77444)
FT   ACT_SITE        364
FT                   /note="Cysteine persulfide intermediate"
FT   Condition: C
FT   MOD_RES         226
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   Condition: K
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Size: 406-412;
Related: None;
Template: P77444; Q9EXP2;
Scope:
 Bacteria; Enterobacterales
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: 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
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# Revision 1.26 2023/06/01
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