ID A0A3N0CLF3_9ACTN Unreviewed; 575 AA.
AC A0A3N0CLF3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=assimilatory sulfite reductase (ferredoxin) {ECO:0000256|ARBA:ARBA00012353};
DE EC=1.8.7.1 {ECO:0000256|ARBA:ARBA00012353};
GN ORFNames=EFK50_06455 {ECO:0000313|EMBL:RNL64169.1};
OS Nocardioides marmoriginsengisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=661483 {ECO:0000313|EMBL:RNL64169.1, ECO:0000313|Proteomes:UP000267128};
RN [1] {ECO:0000313|EMBL:RNL64169.1, ECO:0000313|Proteomes:UP000267128}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 097 {ECO:0000313|EMBL:RNL64169.1,
RC ECO:0000313|Proteomes:UP000267128};
RA Li F.;
RL Submitted (NOV-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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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:RNL64169.1}.
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DR EMBL; RJSE01000005; RNL64169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N0CLF3; -.
DR OrthoDB; 3189055at2; -.
DR Proteomes; UP000267128; Unassembled WGS sequence.
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:UP000267128};
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 173..328
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT DOMAIN 348..413
FT /note="Nitrite/Sulfite reductase ferredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF03460"
FT DOMAIN 424..550
FT /note="Nitrite/sulphite reductase 4Fe-4S"
FT /evidence="ECO:0000259|Pfam:PF01077"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63182 MW; BFA085589D6C934D CRC64;
MPDLRFDSQP PRATEIPRPK RAEGQWSLGQ REPLNKNEQS KKDDDPLNVR DRILYTYSKK
GFDSIDPADL RGRFRWMGLY TQRKPGIDGG RTGSMEEEEL DDRFFMMRVR SDGALLNAKA
LRALGSIGTD FARNSADISD RQNIQFHWIQ IEDVPAIWER LDEAGLSSLE ACGDGPRPFL
GSPVAGVAAD EIIDGTPALE EIKRRYLNNK DFSNLPRKFK TSVTGHPSLD TVPAINDVSF
VGVVHPEHGP GFDLWVGGGL STNPMFAQKL GVWIPLDEVP DAWAGVTGIF RDYGYRRLRS
KARLKFLVAD WGVEKFREVL ENEYLEKKLV SMDSPPVSTE SGDHVGVHAQ KDGNFYIGAA
PVVGRINGET LTGLGDLVEK FALAGARLTA QQKLVVLGVA PADVDAVVAG LLELGLDAKP
SNWRRNTMAC TGIEYCKLAI VDTKERSRAL IAELEKRFPE LDTPITVNVN GCPNACARTQ
TADIGLKGMI ALDEDGNQVE GFQVHLGGGI GMHDTFGKKL RAHKVTSAGL DDYITNVVTA
YLADRTDGES FAAWVVRADE VLLRGEKALE PEPVA
//
