ID A0A0N0TTV2_9ACTN Unreviewed; 846 AA. AC A0A0N0TTV2; DT 09-DEC-2015, integrated into UniProtKB/TrEMBL. DT 09-DEC-2015, sequence version 1. DT 29-SEP-2021, 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=ADL06_11810 {ECO:0000313|EMBL:KOX30841.1}; OS Streptomyces sp. NRRL F-6491. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1519495 {ECO:0000313|EMBL:KOX30841.1, ECO:0000313|Proteomes:UP000037743}; RN [1] {ECO:0000313|EMBL:KOX30841.1, ECO:0000313|Proteomes:UP000037743} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NRRL F-6491 {ECO:0000313|EMBL:KOX30841.1, RC ECO:0000313|Proteomes:UP000037743}; RA Noorani M.; RL Submitted (JUL-2015) 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=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000256|ARBA:ARBA00001974, CC ECO:0000256|PIRNR:PIRNR037149}; CC -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). CC {ECO:0000256|ARBA:ARBA00005096}. 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:KOX30841.1}. 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; LGEE01000115; KOX30841.1; -; Genomic_DNA. DR RefSeq; WP_053646518.1; NZ_LGEE01000115.1. DR EnsemblBacteria; KOX30841; KOX30841; ADL06_11810. DR PATRIC; fig|1519495.3.peg.2504; -. DR UniPathway; UPA00653; -. DR Proteomes; UP000037743; Unassembled WGS sequence. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule. DR GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:UniProtKB-UniRule. DR GO; GO:0050311; F:sulfite reductase (ferredoxin) activity; IEA:UniProtKB-EC. DR GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.10.1100; -; 1. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR007419; BFD-like_2Fe2S-bd_dom. DR InterPro; IPR041854; BFD-like_2Fe2S-bd_dom_sf. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf. DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer. DR InterPro; IPR036136; Nit/Sulf_reduc_fer-like_dom_sf. DR InterPro; IPR012744; Nitri_red_NirB. DR InterPro; IPR017121; Nitrite_Rdtase_lsu. DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom. DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS. DR InterPro; IPR041575; Rubredoxin_C. DR Pfam; PF04324; Fer2_BFD; 1. DR Pfam; PF01077; NIR_SIR; 1. DR Pfam; PF03460; NIR_SIR_ferr; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF18267; Rubredoxin_C; 1. DR PIRSF; PIRSF037149; NirB; 1. DR PRINTS; PR00397; SIROHAEM. DR SUPFAM; SSF51905; SSF51905; 2. DR SUPFAM; SSF55124; SSF55124; 1. DR TIGRFAMs; TIGR02374; nitri_red_nirB; 1. DR PROSITE; PS00365; NIR_SIR; 1. PE 4: Predicted; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485}; KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR037149}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, KW ECO:0000256|PIRNR:PIRNR037149}; Heme {ECO:0000256|ARBA:ARBA00022617}; KW Iron {ECO:0000256|ARBA:ARBA00023004}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Nitrate assimilation {ECO:0000256|ARBA:ARBA00023063, KW ECO:0000256|PIRNR:PIRNR037149}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Reference proteome {ECO:0000313|Proteomes:UP000037743}; KW Thioether bond {ECO:0000256|ARBA:ARBA00022784}. FT DOMAIN 13..302 FT /note="Pyr_redox_2" FT /evidence="ECO:0000259|Pfam:PF07992" FT DOMAIN 332..390 FT /note="Rubredoxin_C" FT /evidence="ECO:0000259|Pfam:PF18267" FT DOMAIN 431..473 FT /note="Fer2_BFD" FT /evidence="ECO:0000259|Pfam:PF04324" FT DOMAIN 561..621 FT /note="NIR_SIR_ferr" FT /evidence="ECO:0000259|Pfam:PF03460" FT DOMAIN 633..769 FT /note="NIR_SIR" FT /evidence="ECO:0000259|Pfam:PF01077" SQ SEQUENCE 846 AA; 89721 MW; 3FD3DCC46D96D2C0 CRC64; MSADADTAAH TPTIVLVGHG MVGQRFLEAL ADRGVTGRAR IVVLCEEPRP AYDRVQLTSY FSGKTPDDLS VVGAGFMAEH GIELYVGDAA ASVDREARTV TARSGRVFAY DTLVLATGSY PFVPPVPGKD ARGCFVYRTI EDLLAIEEYA KTATTGAVVG GGLLGLEAAG ALKGLGLETH VVEFAPRLMP VQVDEGGGAA LLRTIERMGL GVHTGTGTQE VVTADGAVTG MRLSDGSELA VDMVVFSAGV RPRDQLARDC GLAVGERGGI AVDELCRTSD PAVFAIGECA LAVDGRVYGL VAPGYEMAQT VAAVLSEGAE EAGDGFTGAD MSTKLKLLGV DVASFGDAHG TAEGCLDVVY ADSRSGVYKK LVVDREGVLL GGVLVGDADS YGLLRPLTGT VPPVSPEQLV LPAGAGAPVA LGPSSLPDDA VICSCHNVTK HAIGQCSSLA EVKKCTKAGT GCGSCVKVIE KLLPAPTDRG LCRCFSYGRS ELYEIARTLR VTSFAALLDS HGRPEARGGE GCEVCKPTVG SILASLNNGY ILDGEQASLQ DTNDHFLANM QRNGSYSVVP RIPGGEITPD KLIVIGEVAR DYGLYTKITG GQRIDLFGAR VDQLPAIWTR LVDAGFESGH AYGKSLRTVK SCVGQTWCRY GVQDSVKMAI HLELRYRGLR APHKLKSAVS GCARECAEAQ SKDFGIIATA NGWNLYVGGN GGATPRHADL LAQDLSDAEL IRLIDRFLMF YIRTADRLER TSTWLERLEG GLEHLKDVVV HDSLGLCDEL EALMAAHVDA YRDEWAQTLD DPERLRRFVS FVNAPDAPDP SVRFVPERDQ IKPDLTFLTL EGVASR //