ID A0A3N9TA86_9VIBR Unreviewed; 609 AA.
AC A0A3N9TA86;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=EES38_21300 {ECO:0000313|EMBL:RQW61057.1};
OS Vibrio viridaestus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2487322 {ECO:0000313|EMBL:RQW61057.1, ECO:0000313|Proteomes:UP000281112};
RN [1] {ECO:0000313|EMBL:RQW61057.1, ECO:0000313|Proteomes:UP000281112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LJC006 {ECO:0000313|EMBL:RQW61057.1,
RC ECO:0000313|Proteomes:UP000281112};
RA Liang J.;
RT "Vibrio LJC006 sp. nov., isolated from seawater during the bloom of the
RT enteromorpha.";
RL Submitted (NOV-2018) 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:RQW61057.1}.
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DR EMBL; RJVQ01000019; RQW61057.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N9TA86; -.
DR OrthoDB; 9816402at2; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000281112; 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:UP000281112};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01541}.
FT DOMAIN 74..212
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 244..458
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 80..85
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 127..130
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 163..172
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 332
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 366
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 396..399
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 414..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 420
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 429..432
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 529..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 535..539
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 571
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 609
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 609 AA; 66747 MW; B10852DFBD7802F0 CRC64;
MSSANNNPNE LAALASPLND SQANLLQQAA SQLSPSQLAW VSGYFWGVSQ SQSATAGVTQ
SIQPGGQPQA AGKLTIIYAS QTGNAKGVAE ALEQEAEALS IPVQLFDASD YKGKDLAKET
HVIFVSSTNG EGEAPDNALE LHEFLQSKKA PKLPNLKYGV LGLGDSSYEF FCQTGKDFDA
FLSKQGATSF IERVDCDVDY EEQAAEWRKE ALSRVKESLG ETQTATAPLF SANATPSASQ
YNKQNPFAAT LLTSQKITGR DSGKDVRHIE VDLEGSGLTY QPGDALGVWY ENDCDLANDV
LSAVGLSGAE SVEVDGESLS IHSALVSKYE ITASNPQLIT KLAELSDAKA LTALVENKDA
LREFSANHQV VDVLKLAETK LTAEQLISLL RRLTPRLYSI ASSQSEVDQE VHLTVGVVEY
EQDGETRLGG ASGFLGRQLE EGENVKVFIE NNNNFKLPQD TNTPVIMVGP GTGIAPFRSF
IQERDNLGAE GKNWLFFGDR TFTQDFLYQV EWQKYLKSGL LTRLDVAFSR DQQEKVYVQH
RILENAEQVW AWIQEGAYIY VCGDATRMAK DVNDALITVA EQQGNMSHDK AEEFINDLRK
AKRYQRDVY
//
