ID A0A1M5W3B6_9ACTN Unreviewed; 565 AA.
AC A0A1M5W3B6;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=SAMN05444521_2073 {ECO:0000313|EMBL:SHH81996.1};
OS Streptomyces sp. 3214.6.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1882757 {ECO:0000313|EMBL:SHH81996.1, ECO:0000313|Proteomes:UP000190947};
RN [1] {ECO:0000313|Proteomes:UP000190947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3124.6 {ECO:0000313|Proteomes:UP000190947};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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=3 H2O + hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] =
CC 7 H(+) + 6 reduced [2Fe-2S]-[ferredoxin] + sulfite;
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:ARBA00000993};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT670819; SHH81996.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M5W3B6; -.
DR STRING; 1882757.SAMN05444521_2073; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000190947; Chromosome i.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.480.20; -; 1.
DR Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 2.
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 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617}; Iron {ECO:0000256|ARBA:ARBA00022617};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022617};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000190947};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT DOMAIN 101..164
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 172..327
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 349..414
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 426..562
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 62793 MW; 49F4E7969108EA64 CRC64;
MAATPQNPAA ATPRRKVSRH RGEGQWAAGH HTPLNGNEQF KKDDDGLNVR TRIETIYSKR
GFDSIDPNDL RGRMRWWGLY TQRKPGIDGG KTAILEPEEL DDKYFMLRVR IDGGRLTTQQ
LRVIGEISQE FARGSADVTD RQNIQLHWIR IEDVPEIWNR LEAVGLSTTE ACGDCPRVVI
GSPVAGIAED EIIDGTSAID EIHERYIGSK EFSNLPRKFK TAISGSPLLD VVHEINDIAF
VGVEHPEHGP GFDLWVGGGL STNPKLGVRL GAWVPLDEVP EVWAGVVGIF RDWGYRRLRT
RARLKFLVAD WGAEKFRQVL EDDYLKRKLV DGPAPAEPAG RWRDHVGVHR QKDGRFYVGF
APRVGRVDGA TLTKIAEVAE AHGSGRVRTT VEQKMIVLDV EEAQVEPLVE ALEALDLTAK
PSPFRRGTMA CTGIEYCKLA IVETKARGSQ LIDELERRIP EFDEPITINL NGCPNACARI
QVADIGLKGQ LVLNDQGEQV EGYQVHLGGA LGLEAGFGRK VRGLKVTSAE LPDYVERVLK
RFQAERTEGE RFAAWASRAS EEALS
//
