ID A0A1E3GTT5_9GAMM Unreviewed; 599 AA.
AC A0A1E3GTT5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Sulfite reductase [NADPH] flavoprotein alpha-component {ECO:0000256|PIRNR:PIRNR000207};
DE Short=SiR-FP {ECO:0000256|PIRNR:PIRNR000207};
DE EC=1.8.1.2 {ECO:0000256|PIRNR:PIRNR000207};
GN Name=cysJ {ECO:0000313|EMBL:ODN67460.1};
GN ORFNames=A9E74_00804 {ECO:0000313|EMBL:ODN67460.1};
OS Methylophaga muralis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=291169 {ECO:0000313|EMBL:ODN67460.1, ECO:0000313|Proteomes:UP000094379};
RN [1] {ECO:0000313|EMBL:ODN67460.1, ECO:0000313|Proteomes:UP000094379}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bur 1 {ECO:0000313|EMBL:ODN67460.1,
RC ECO:0000313|Proteomes:UP000094379};
RA Vasilenko O.V., Doronina N.V., Shmareva M.N., Tarlachkov S.V.,
RA Mustakhimov I., Trotsenko Y.A.;
RT "Draft Genome Sequence of Methylophaga muralis Bur 1.";
RL Submitted (JUL-2016) 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.
CC {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;
CC Evidence={ECO:0000256|PIRNR:PIRNR000207};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000207,
CC ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRNR:PIRNR000207,
CC ECO:0000256|PIRSR:PIRSR000207-1};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR000207,
CC ECO:0000256|PIRSR:PIRSR000207-1};
CC Note=Binds 1 FMN per subunit. {ECO:0000256|PIRNR:PIRNR000207,
CC ECO:0000256|PIRSR:PIRSR000207-1};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; hydrogen
CC sulfide from sulfite (NADPH route): step 1/1.
CC {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|PIRNR:PIRNR000207}.
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:ODN67460.1}.
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DR EMBL; MCRI01000005; ODN67460.1; -; Genomic_DNA.
DR RefSeq; WP_069295342.1; NZ_MCRI01000005.1.
DR AlphaFoldDB; A0A1E3GTT5; -.
DR STRING; 291169.A9E74_00804; -.
DR PATRIC; fig|291169.3.peg.806; -.
DR UniPathway; UPA00140; UER00207.
DR Proteomes; UP000094379; Unassembled WGS sequence.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
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-EC.
DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
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 InterPro; IPR010199; CysJ.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001226; Flavodoxin_CS.
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; PS00201; FLAVODOXIN; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR000207};
KW Cysteine biosynthesis {ECO:0000256|ARBA:ARBA00023192,
KW ECO:0000256|PIRNR:PIRNR000207};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000207};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR000207};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000207};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000207};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR000207};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000207};
KW Reference proteome {ECO:0000313|Proteomes:UP000094379};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000207}.
FT DOMAIN 63..201
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 233..448
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 116..119
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 152..161
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 321
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 386..389
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 404..406
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 410
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 419..422
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 519..520
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 525..529
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 561
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
FT BINDING 599
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000207-1"
SQ SEQUENCE 599 AA; 66931 MW; CCF7A43A1A72E53E CRC64;
MNIRLPNAPL TDEQLQQLNN LLQGLEGWQV DWLSGYLSGY RAAQVGTAVM EAGPSLAEQA
IKLTVLYGSQ TGNTEAVAGQ LAEKAKASGI EVKLWDMAEY KPRELKNEQY LAVLTSTHGE
GEPPDNAMDL YEFLNSRKAP GLKGLHYSVL SLGDSSYEFF CQTGKDFDER LQKLGATAVI
PRVDCDVDYD DLAEKWIAEF VGALTSSMQA SAAPPSASAA MSQLETSVQY DRKHPFSAPL
LENQLLSGRG SSKEVRHIEI SLEGSGLQYE PGDALGVYPQ NDPALVSMLI DALGFDADSS
VELDEQQETL TNALMHHREI TVLTRPLVEK WAELAQSDEL NKLMESKAAV TEWIRGRDVL
DLVQSYPLAD IDANGFIKLL RKLPPRLYSI ASSQAAVDEE VHITVATVRY NAHNRERGGV
ASTWLADRLA EDATIPVYID PNKNFKLPAD DNAPIIMIGP GTGVAPFRSF MQEREERGAR
GPNWLFFGDQ HFLTDFLYQT EWLAWRKSGL LTHLDVAFSR DQTEKIYVQH RIREKSIEIW
NWLQDGAHIY VCGDADNMAP DVNEALIDII SQQGNKSRED ATEYLRQLTR DKRYQRDVY
//
