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Database: UniProt
Entry: C1FNR8_CLOBJ
LinkDB: C1FNR8_CLOBJ
Original site: C1FNR8_CLOBJ 
ID   C1FNR8_CLOBJ            Unreviewed;       284 AA.
AC   C1FNR8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   SubName: Full=Sulfite/nitrite reductase family protein {ECO:0000313|EMBL:ACO83724.1};
GN   OrderedLocusNames=CLM_1934 {ECO:0000313|EMBL:ACO83724.1};
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO83724.1, ECO:0000313|Proteomes:UP000001374};
RN   [1] {ECO:0000313|EMBL:ACO83724.1, ECO:0000313|Proteomes:UP000001374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2 {ECO:0000313|Proteomes:UP000001374};
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC       family. {ECO:0000256|ARBA:ARBA00010429}.
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DR   EMBL; CP001581; ACO83724.1; -; Genomic_DNA.
DR   RefSeq; WP_003358979.1; NC_012563.1.
DR   AlphaFoldDB; C1FNR8; -.
DR   KEGG; cby:CLM_1934; -.
DR   eggNOG; COG2221; Bacteria.
DR   HOGENOM; CLU_072599_0_1_9; -.
DR   Proteomes; UP000001374; Chromosome.
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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.30.70.3340; -; 1.
DR   Gene3D; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; IPR045169; NO2/SO3_Rdtase_4Fe4S_prot.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS.
DR   PANTHER; PTHR11493:SF54; ANAEROBIC SULFITE REDUCTASE SUBUNIT C; 1.
DR   PANTHER; PTHR11493; SULFITE REDUCTASE [NADPH] SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF12838; Fer4_7; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
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; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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}.
FT   DOMAIN          159..187
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          188..217
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   284 AA;  31593 MW;  04983F6A47B079E6 CRC64;
     MKMISKNEIA KLKGEGFLAQ KQEGYFSVRI LSRAGNFTSK QIIKLAEIAD NYGKGYLGVT
     TRLATEIPWI KYEDIEAVKK EIVSSGMGHG GTGKKVRPLV SCKGTVCVHG LYDTQKLCGE
     LHDKYFGYEL PSKFKITLVG CPNNCAKASI NDIGIMGQAY VEFNEEKCKA CGICTKSCRQ
     KAVTVENNKI VYKKDLCVNC GKCATVCPFE AMTIKEQGLQ VYLGGRFGRE YRIGNRLKGL
     YKEEEIPALV QKIFDVYSEM GNPGERLAKM IERVGFDKVE EAIL
//
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