ID A0A240B0F4_SERFI Unreviewed; 600 AA.
AC A0A240B0F4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207};
DE Short=SiR-FP {ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207};
DE EC=1.8.1.2 {ECO:0000256|HAMAP-Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207};
GN Name=cysJ {ECO:0000256|HAMAP-Rule:MF_01541,
GN ECO:0000313|EMBL:SNV88884.1};
GN ORFNames=SAMEA4384070_00841 {ECO:0000313|EMBL:SNV88884.1};
OS Serratia ficaria.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=61651 {ECO:0000313|EMBL:SNV88884.1, ECO:0000313|Proteomes:UP000215134};
RN [1] {ECO:0000313|EMBL:SNV88884.1, ECO:0000313|Proteomes:UP000215134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC12148 {ECO:0000313|EMBL:SNV88884.1,
RC ECO:0000313|Proteomes:UP000215134};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-
CC Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207}.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01541,
CC ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01541,
CC ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|PIRSR:PIRSR000207-1};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01541,
CC ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FMN per subunit. {ECO:0000256|HAMAP-Rule:MF_01541,
CC ECO:0000256|PIRNR:PIRNR000207, ECO:0000256|PIRSR:PIRSR000207-1};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01541, ECO:0000256|PIRNR:PIRNR000207}.
CC -!- SUBUNIT: Alpha(8)-beta(8). The alpha component is a flavoprotein, the
CC beta component is a hemoprotein. {ECO:0000256|HAMAP-Rule:MF_01541,
CC ECO:0000256|PIRNR:PIRNR000207}.
CC -!- SIMILARITY: Belongs to the NADPH-dependent sulphite reductase
CC flavoprotein subunit CysJ family. {ECO:0000256|HAMAP-Rule:MF_01541}.
CC -!- SIMILARITY: Belongs to the flavodoxin family. MioC subfamily.
CC {ECO:0000256|ARBA:ARBA00038260}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
CC pyridine nucleotide cytochrome reductase family. {ECO:0000256|HAMAP-
CC Rule:MF_01541}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
CC family. {ECO:0000256|HAMAP-Rule:MF_01541}.
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DR EMBL; LT906479; SNV88884.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A240B0F4; -.
DR STRING; 1411141.GCA_001590885_00578; -.
DR KEGG; sfj:SAMEA4384070_0841; -.
DR OrthoDB; 9816402at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000215134; Chromosome 1.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0004783; F:sulfite reductase (NADPH) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR CDD; cd06199; SiR; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR HAMAP; MF_01541; CysJ; 1.
DR InterPro; IPR010199; CysJ.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR029758; CysJ_Proteobact.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR NCBIfam; TIGR01931; cysJ; 1.
DR PANTHER; PTHR19384:SF128; NADPH OXIDOREDUCTASE A; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PIRSF; PIRSF000207; SiR-FP_CysJ; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01541};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192, ECO:0000256|HAMAP-
KW Rule:MF_01541};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982, ECO:0000256|HAMAP-
KW Rule:MF_01541};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01541};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01541};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|HAMAP-Rule:MF_01541};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01541};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01541}; Reference proteome {ECO:0000313|Proteomes:UP000215134};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01541}.
FT DOMAIN 64..202
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 235..449
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 70..75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 117..120
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 153..162
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 323
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 357
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541"
FT BINDING 387..390
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 405..407
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 411
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 420..423
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 520..521
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 526..530
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 562
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 600
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01541,
FT ECO:0000256|PIRSR:PIRSR000207-1"
SQ SEQUENCE 600 AA; 66158 MW; 2ACE3AC1705E7C15 CRC64;
MTTQAPPTSL LPLTPEQLAR LQAAIGEYSP TQLAWLSGYF WGMVNQQPGA VASAPAAPAA
AAGITIISAS QTGNARRLAE QLRDDLLAAK LSATLVNAGD YKFKQIAQER LLVIVASTQG
EGEPAEEAVA LHKFLFSKKA PKLNDTAFAV FGLGDTSYEN FCQSGKDFDG KLAELGAERL
VERVDADVEY QELAAAWRKQ VVEVLKARAP AENAAPGQLA NGAVDLLDSS PYSKEQPLTA
QLAVKQKITG RGSDKDVRHI EIDLGDSGLR YRPGDALGVW FDNDPALVDE LVQLLWLKGD
EPVEVEGKTL PLAEALRSHF ELTQNTTPIV DKYAALSRDE QLIGLLADKA ALQRYAHNTP
IVDMVRQAPA DLNAEQLIGL LRPLTPRLYS IASSQAETEN EVHITVGVVR YDIDGRARAG
GASSFLADRL EEDGDVRVFI EHNDNFRLPA NPDAPVIMIG PGTGIAPFRA FMQQRDAEGA
GGKNWLFFGN PHFTEDFLYQ VEWQRYVKDG LLTRIDLAWS RDQQHKVYVQ DKLREQGAEV
WRWIQEGAHI YVCGDANRMA KDVENTLLEL VAEHGGMDTE LADEFLSELR LERRYQRDVY
//
