ID A0A5N5W6V6_STRMB Unreviewed; 568 AA.
AC A0A5N5W6V6;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 28-JAN-2026, entry version 23.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=FRZ00_16805 {ECO:0000313|EMBL:KAB7843629.1};
OS Streptomyces mobaraensis (Streptoverticillium mobaraense).
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=35621 {ECO:0000313|EMBL:KAB7843629.1, ECO:0000313|Proteomes:UP000327000};
RN [1] {ECO:0000313|EMBL:KAB7843629.1, ECO:0000313|Proteomes:UP000327000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=US-43 {ECO:0000313|EMBL:KAB7843629.1,
RC ECO:0000313|Proteomes:UP000327000};
RX PubMed=31615513; DOI=.1186/s12934-019-1225-7;
RA Shi Y., Gu R., Li Y., Wang X., Ren W., Li X., Wang L., Xie Y., Hong B.;
RT "Exploring novel herbicidin analogues by transcriptional regulator
RT overexpression and MS/MS molecular networking.";
RL Microb. Cell Fact. 18:175-175(2019).
CC -!- FUNCTION: Catalyzes the reduction of sulfite to sulfide, a step in the
CC biosynthesis of sulfur-containing amino acids and cofactors.
CC {ECO:0000256|ARBA:ARBA00003247}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] + 3 H2O =
CC sulfite + 6 reduced [2Fe-2S]-[ferredoxin] + 7 H(+);
CC Xref=Rhea:RHEA:23132, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17359,
CC ChEBI:CHEBI:29919, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.8.7.1;
CC Evidence={ECO:0000256|ARBA:ARBA00049518};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- COFACTOR:
CC Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC Evidence={ECO:0000256|ARBA:ARBA00001929};
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
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:KAB7843629.1}.
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DR EMBL; VOKX01000032; KAB7843629.1; -; Genomic_DNA.
DR RefSeq; WP_004949406.1; NZ_VOKX01000032.1.
DR AlphaFoldDB; A0A5N5W6V6; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000327000; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR FunFam; 3.90.480.20:FF:000002; Sulfite reductase; 1.
DR FunFam; 3.30.413.10:FF:000009; Sulfite reductase [ferredoxin]; 1.
DR FunFam; 3.30.413.10:FF:000013; Sulfite reductase [ferredoxin]; 1.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
DR InterPro; IPR051329; NIR_SIR_4Fe-4S.
DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf.
DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom.
DR InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR PANTHER; PTHR32439; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR PANTHER; PTHR32439:SF0; FERREDOXIN--NITRITE REDUCTASE, CHLOROPLASTIC; 1.
DR Pfam; PF01077; NIR_SIR; 2.
DR Pfam; PF03460; NIR_SIR_ferr; 2.
DR PRINTS; PR00397; SIROHAEM.
DR SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 2.
DR SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 2.
DR PROSITE; PS00365; NIR_SIR; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000327000};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 104..167
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 175..331
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 352..417
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 428..567
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 568 AA; 62759 MW; E774CF3FD2E72171 CRC64;
MAATAQPPAA AAPATPRRKA GRHRGEGQWA VGHFTPLNAN EQVKKDDDGL NVRTRIETIY
AKAGFASIDP ADLRGRMRWW GLYTQRRPGI DGGKTAVLAP EELDDEYFML RVRIDGGRLT
TAQLRVIGEV SQEFARGTAD ITDRQNIQYH WIRIEDVPEI WRRLEAVGLS TTEACGDTPR
VVLGSPVAGI AEDEIVDGTP AIEEIQRRFI GNKDFSNLPR KFKTAISGSP LLDVVHEIND
VAFVGVRHPE HGPGFDLWVG GGLSTNPKIG VRLGAWVPLE DVPDVFGGVI GIFRDYGYRR
LRNRARLKFL VADWGPERFR EVLEREYLGR PLLDGPAPER PAERWRDHVG VHRQRDGRYY
VGFAPRVGRV DGSTLTKIAE LAEAHGSGRL RTTAEQKMIV LDVPEDRVAS LTAGLEALDL
RVAPSPFRRG TMACTGIEFC KLAIVETKAR GASLIDELER RLPEFDEPLT INLNGCPNAC
ARIQVADIGL KGQLVTDARG RQAEGYQVHL GGALGLEAGF GRKVRGLKVT ADELPDYIER
VLRRYLAGRA DGERFAAWAA RAGEEELS
//
