ID C1FVF9_CLOBJ Unreviewed; 321 AA.
AC C1FVF9;
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=Anaerobic sulfite reductase, subunit C {ECO:0000313|EMBL:ACO85531.1};
GN Name=arsC {ECO:0000313|EMBL:ACO85531.1};
GN OrderedLocusNames=CLM_1110 {ECO:0000313|EMBL:ACO85531.1};
OS Clostridium botulinum (strain Kyoto / Type A2).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=536232 {ECO:0000313|EMBL:ACO85531.1, ECO:0000313|Proteomes:UP000001374};
RN [1] {ECO:0000313|EMBL:ACO85531.1, 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; ACO85531.1; -; Genomic_DNA.
DR RefSeq; WP_012704805.1; NC_012563.1.
DR AlphaFoldDB; C1FVF9; -.
DR KEGG; cby:CLM_1110; -.
DR eggNOG; COG2221; Bacteria.
DR HOGENOM; CLU_072599_1_0_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; 3.30.413.10; Sulfite Reductase Hemoprotein, domain 1; 1.
DR Gene3D; 3.90.480.10; Sulfite Reductase Hemoprotein;Domain 2; 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 InterPro; IPR014261; Sulphite_reductase_C.
DR NCBIfam; TIGR02912; sulfite_red_C; 1.
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 PRINTS; PR00397; SIROHAEM.
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 163..193
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 195..224
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 321 AA; 36438 MW; C10F7BF7BB2B77F1 CRC64;
MDINTKAIKK NAFRVTKHRG KTALRVRVPG GDLPVKYFAI LAKIAEEYGN GKVHVTTRQG
FEIPDLDFNK MDEINKLIQP VIEGLNINQD EVGKGYSAAG TRNITSCVGN EVCPFANYNT
AKFAKRIEKA IFPNDYHVKV ALTGCPNDCI KARMHDFGIL GMTEPQYDKY RCIGCMACIN
NCKKRVTGAL RFENFKVIRD HEKCIGCGEC VGKCPTGAWT RSKEKYYKLA IMGRTGKKNP
RLAEDFIKWV DEDSIVKIIV NTYDYIHEYI DKDAPGGKEH IGYIVDRTGY QEFKKWALKD
VNLKEKAELV KNINWSGIKY K
//
