ID A0A2S9I903_9GAMM Unreviewed; 600 AA.
AC A0A2S9I903;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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:PRD14280.1};
GN ORFNames=CQW29_17055 {ECO:0000313|EMBL:PRD14280.1};
OS Pantoea coffeiphila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1465635 {ECO:0000313|EMBL:PRD14280.1, ECO:0000313|Proteomes:UP000239181};
RN [1] {ECO:0000313|EMBL:PRD14280.1, ECO:0000313|Proteomes:UP000239181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342 {ECO:0000313|EMBL:PRD14280.1,
RC ECO:0000313|Proteomes:UP000239181};
RA Siqueira K.A., Liotti R.G., Mendes T.A., Soares M.A.;
RT "Draft genome of two endophytic bacteria isolated from 'guarana' Paullinia
RT cupana (Mart.) Ducke.";
RL Submitted (OCT-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01541}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRD14280.1}.
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DR EMBL; PDET01000012; PRD14280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S9I903; -.
DR OrthoDB; 9816402at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000239181; Unassembled WGS sequence.
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};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01541}.
FT DOMAIN 63..201
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 69..74
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 116..119
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; 66358 MW; 03C1AD2BC6342C1F CRC64;
MTTQAPLNML PLNPDQLARL QAATGDYTPT QLAWLSGYFW GMVNQAPGAV VAAAPAPVEV
PTITILSASQ TGNARRLSEQ LRDDLLAAKL NVNLVNAGDY KFKQIAQEKL LVVVTSTQGE
GEPPEEGVAL HKFLMSKKAP KMDASAFAVF GLGDTSYEFF SQAGKDFDNR LAELGATRLL
DRVDADVEYA AAAEAWRKQL VDILQARVPK EAPAAAAATA AGSVNEIHSS PYTKEAPLTA
SFAVNQKITG RDSDKDVRHI EIDLGESGLR YKPGDALGVW FENDPALVKE LLELLWLKGD
EPVSVHGETL PLAEALQKHY ELTVNTPQIV EQYAKLSHNE ALLAQITDKA SLQQYAQNTP
IVDMARFAPT ELNAEQLTGL LRPLTPRLYS IASSQAENET EVHITVGVVR YEIEGRARAG
GASSYLGDRL VEDDEIRVFI EHNDNFRLPA NPETPVIMIG PGTGIAPFRA FMQQRDSEGA
GGKNWLFFGN PHFTEDFLYQ VEWQRYVKDG LLTNIDLAWS RDQKHKIYVQ DKIRAKGAEV
WSWIQEGAHI YVCGDANRMA KDVEQALLEV VAEYGGMDIE TADEFLSDLR IERRYQRDVY
//
