ID A0A0J1GJK2_9GAMM Unreviewed; 605 AA.
AC A0A0J1GJK2;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:KLU99745.1};
GN ORFNames=ABT58_16010 {ECO:0000313|EMBL:KLU99745.1};
OS Photobacterium aphoticum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=754436 {ECO:0000313|EMBL:KLU99745.1, ECO:0000313|Proteomes:UP000036426};
RN [1] {ECO:0000313|EMBL:KLU99745.1, ECO:0000313|Proteomes:UP000036426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25995 {ECO:0000313|EMBL:KLU99745.1,
RC ECO:0000313|Proteomes:UP000036426};
RA Machado H., Gram L.;
RT "Photobacterium galathea sp. nov.";
RL Submitted (MAY-2015) 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: 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: 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:KLU99745.1}.
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DR EMBL; LDOV01000028; KLU99745.1; -; Genomic_DNA.
DR RefSeq; WP_047875445.1; NZ_PYMF01000040.1.
DR AlphaFoldDB; A0A0J1GJK2; -.
DR PATRIC; fig|754436.4.peg.3396; -.
DR OrthoDB; 9816402at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000036426; 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}; Reference proteome {ECO:0000313|Proteomes:UP000036426};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01541}.
FT DOMAIN 70..208
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 240..454
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 76..81
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 123..126
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 159..168
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 328
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 362
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 392..395
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 410..412
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 416
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 425..428
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 525..526
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 531..535
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 567
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 605
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 605 AA; 66150 MW; F5A4910C76B2A273 CRC64;
MLLKELSALA SPLNDQKLDQ LQQAASELSP QQLAWISGYF WGLSQTAVAG EAQPAGLPVA
AVASQPAGKL TIIYASQTGN AKGVAQALKD EADAAGIAAE LFSAGDYKGK NLAKETHVII
VASTHGEGEA PDDAIELHEF LQSKKAPKLP NLEYAVIGLG DSSYEFFCQT AKDFDTYLAK
LGAKPMLDRL DCDVDYDAPA ATWRAQALEK VQATLVKADA QVVQLPVGQA AAAPSAFNKQ
NPFEASLLVS QKITGRNSGK DVRHVEIDLE GSGLTYQPGD ALGVWYSNDA ELAAAIIAKV
GLNEDDTVEV DGQSVSLIQA LINDYEITAA NPQLVTRYAE LSGSKKLAKL VEDKDKLREY
AANTQVIDVL GEKKTVLDAA QLVGLLRRLT PRLYSIASSQ EEVGEEVHLT VGLVEYAKGE
ETRQGGASSY LAQRLEEGDS VKVFVETNNH FKLPADDNTP VIMIGPGTGI APFRAFVQER
DNRDAAGKNW LFFGDRTFTE DFLYQVEWQK YLKSGIVNRL DVAFSRDQVE KVYVQHRLLE
HGAEVWQWLQ DGAHVYVCGD ANRMAKDVHD ALLTIAEQQG QQTREQAEQY LNDLRKSKRY
QKDVY
//
