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Database: UniProt
Entry: A0A316TM87_9ACTN
LinkDB: A0A316TM87_9ACTN
Original site: A0A316TM87_9ACTN 
ID   A0A316TM87_9ACTN        Unreviewed;       841 AA.
AC   A0A316TM87;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   27-MAR-2024, 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=DJ010_21225 {ECO:0000313|EMBL:PWN00856.1};
OS   Nocardioides silvaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=2201891 {ECO:0000313|EMBL:PWN00856.1, ECO:0000313|Proteomes:UP000245507};
RN   [1] {ECO:0000313|EMBL:PWN00856.1, ECO:0000313|Proteomes:UP000245507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCTCC AB 2018079 {ECO:0000313|EMBL:PWN00856.1,
RC   ECO:0000313|Proteomes:UP000245507};
RA   Li C., Wang G.;
RT   "Nocardioides silvaticus genome.";
RL   Submitted (MAY-2018) 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   -!- COFACTOR:
CC       Name=siroheme; Xref=ChEBI:CHEBI:60052;
CC         Evidence={ECO:0000256|ARBA:ARBA00001929};
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:PWN00856.1}.
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DR   EMBL; QGDD01000014; PWN00856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316TM87; -.
DR   OrthoDB; 9768666at2; -.
DR   Proteomes; UP000245507; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
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   CDD; cd19944; NirB_Fer2_BFD-like_2; 1.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 1.10.10.1100; BFD-like [2Fe-2S]-binding domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
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; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   InterPro; IPR041575; Rubredoxin_C.
DR   NCBIfam; TIGR02374; nitri_red_nirB; 1.
DR   PANTHER; PTHR43809; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 1.
DR   PANTHER; PTHR43809:SF1; NITRITE REDUCTASE (NADH) LARGE SUBUNIT; 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; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   PRINTS; PR00397; SIROHAEM.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
DR   SUPFAM; SSF56014; Nitrite and sulphite reductase 4Fe-4S domain-like; 1.
DR   SUPFAM; SSF55124; Nitrite/Sulfite reductase N-terminal domain-like; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|PIRNR:PIRNR037149};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR037149};
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   Nitrate assimilation {ECO:0000256|PIRNR:PIRNR037149};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245507};
KW   Thioether bond {ECO:0000256|ARBA:ARBA00022784}.
FT   DOMAIN          8..290
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
FT   DOMAIN          324..384
FT                   /note="NADH-rubredoxin oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18267"
FT   DOMAIN          551..613
FT                   /note="Nitrite/Sulfite reductase ferredoxin-like"
FT                   /evidence="ECO:0000259|Pfam:PF03460"
FT   DOMAIN          623..759
FT                   /note="Nitrite/sulphite reductase 4Fe-4S"
FT                   /evidence="ECO:0000259|Pfam:PF01077"
SQ   SEQUENCE   841 AA;  89903 MW;  64E8EC2BE7E85897 CRC64;
     MAPQLRKQLV VVGHGMVGHR FVESAISRGL TEAYDITVLG AEPRPAYDRV ALTSFFEVGA
     EALSLLPSGT YDDPRVRLRT HAEVVAVSPR QRIVTLASGE DLHYDELVLA TGAAPFVPPV
     PGADLANVFG YRTIEDLEAI RSASKGGRRK VGAVIGGGLL GLEAANALHQ LGVETHVVEL
     APRLMAVQID DLGGRTLNQH IGKLGLTVHT GAMTEAILGD RRNRVERLAL KDRNPLDVDL
     VVFSAGIRPR DALARAAGLD VADRGGVLVD GSLRTSDEHI WAIGECAAVQ GVMYGLVAPG
     YDMAEIVVDR LLGGAGEFTG ADMSTKLKLL GVDVASFGDA HGTTKGALEL TYADALSGVY
     KKLVISEDGK RLLGGVLVGD AAAYGVLRPM VASGMELPEN PEELILPASR GGANLELPDD
     AQVCSCNDVT KAEITAAAAD GTITRAGATC GSCKTLVKKI VEDYFAATGK EIDRSLCEHF
     RMTRQELFDV VAVHGYTRFD DIVEGHGTGR GCDICKPAVA SILASLLNQH VLAPGNRQLQ
     DTNDAYLGNL QKNGTYSVVP RVPGGEITPD KLIVIGQVAK DFGLYTKITG GQRIDLFGAR
     MEDLPAIWKR LVEAGMESGH AYGKSLRTVK SCVGSTWCRY GVQDSVGLAI ELELRYRGLR
     SPHKLKGGVS GCARECAEAR SKDFGIIATE KGWNLYVCGN GGAMPAHAQL LAGDLSKEEL
     VRYLDRFLMY YIRTADRLQR TSSWMDAVDG GLDRIREVVV DDVLGLGDQL EAAMARHVDS
     YFDEWKATIE DPEKLARFVS FVNAPGTPDP NITFREERGQ VQAATTDGPV SLGTTIPVGA
     P
//
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