AC   MF_01541;
DC   Protein; auto
TR   HAMAP; MF_01541; -; 1; level=0
XX
Names: CysJ
XX
ID   CYSJ
DE   RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component;
DE            Short=SiR-FP;
DE            EC=1.8.1.2;
GN   Name=cysJ;
XX
CC   -!- FUNCTION: Component of the sulfite reductase complex that catalyzes the
CC       6-electron reduction of sulfite to sulfide. This is one of several
CC       activities required for the biosynthesis of L-cysteine from sulfate.
CC       The flavoprotein component catalyzes the electron flow from NADPH ->
CC       FAD -> FMN to the hemoprotein component.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 H2O + hydrogen sulfide + 3 NADP(+) = 4 H(+) + 3 NADPH +
CC         sulfite; Xref=Rhea:RHEA:13801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:29919, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.8.1.2;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC       Note=Binds 1 FMN per subunit.;
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC       sulfide from sulfite (NADPH route): step 1/1.
CC   -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC       beta component is a hemoprotein.
CC   -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase
CC       flavoprotein subunit CysJ family.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC       family.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC       pyridine nucleotide cytochrome reductase family.
XX
DR   PROSITE; PS50902; FLAVODOXIN_LIKE; 1; trigger=no
DR   PROSITE; PS51384; FAD_FR; 1; trigger=yes
DR   Pfam; PF00667; FAD_binding_1; 1; trigger=no
DR   Pfam; PF00258; Flavodoxin_1; 1; trigger=no
DR   Pfam; PF00175; NAD_binding_1; 1; trigger=no
DR   PRINTS; PR00369; FLAVODOXIN; 1; trigger=no
DR   PRINTS; PR00371; FPNCR; 1; trigger=no
DR   NCBIfam; TIGR01931; CysJ; 1; trigger=no
XX
KW   Amino-acid biosynthesis
KW   Cysteine biosynthesis
KW   Electron transport
KW   FAD
KW   Flavoprotein
KW   FMN
KW   NADP
KW   Oxidoreductase
KW   Transport
XX
GO   GO:0004783; F:sulfite reductase (NADPH) activity
GO   GO:0000103; P:sulfate assimilation
GO   GO:0070814; P:hydrogen sulfide biosynthetic process
XX
FT   From: CYSJ_ECOLI (P38038)
FT   DOMAIN          64..202
FT                   /note="Flavodoxin-like"
FT   BINDING         70..75
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: S-Q-T-G-N-[AG]
FT   BINDING         117..120
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: S-T-[QHN]-G
FT   BINDING         153..162
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT   Condition: L-G-D-x-[ST]-Y-x(2)-F-[CA]
FT   BINDING         386..389
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: R-[LF]-Y-S
FT   BINDING         404..406
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: [ST]-V-[GAS]
FT   BINDING         419..422
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: G-[GV]-[AS]-S
FT   BINDING         519..520
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: S-[RQ]
FT   BINDING         525..529
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: K-[IV]-Y-V-Q
FT   BINDING         322
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: T
FT   BINDING         356
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         410
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Optional; Condition: Y
FT   BINDING         561
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   Condition: D
FT   BINDING         599
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Optional; Condition: Y
XX
Size: 595-623;
Related: None;
Template: P38038; P38039;
Scope:
 Bacteria; Pseudomonadota
Fusion:
 Nter: None
 Cter: None
Duplicate: in NEIMB
Plasmid: None
Comments: None
XX
# Revision 1.21 2023/06/01
//