ID I7KZ04_METBM Unreviewed; 293 AA.
AC I7KZ04;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Nitrite and sulphite reductase 4Fe-4S region {ECO:0000313|EMBL:CCJ35990.1};
GN OrderedLocusNames=BN140_1067 {ECO:0000313|EMBL:CCJ35990.1};
OS Methanoculleus bourgensis (strain ATCC 43281 / DSM 3045 / OCM 15 / MS2)
OS (Methanogenium bourgense).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=1201294 {ECO:0000313|EMBL:CCJ35990.1, ECO:0000313|Proteomes:UP000009007};
RN [1] {ECO:0000313|Proteomes:UP000009007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43281 / DSM 3045 / OCM 15 / MS2
RC {ECO:0000313|Proteomes:UP000009007};
RX PubMed=22965103; DOI=10.1128/JB.01292-12;
RA Maus I., Wibberg D., Stantscheff R., Eikmeyer F.G., Seffner A., Boelter J.,
RA Szczepanowski R., Blom J., Jaenicke S., Konig H., Puhler A., Schluter A.;
RT "Complete genome sequence of the hydrogenotrophic, methanogenic archaeon
RT Methanoculleus bourgensis strain MS2T, isolated from a sewage sludge
RT digester.";
RL J. Bacteriol. 194:5487-5488(2012).
CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S domain
CC family. {ECO:0000256|ARBA:ARBA00010429}.
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DR EMBL; HE964772; CCJ35990.1; -; Genomic_DNA.
DR AlphaFoldDB; I7KZ04; -.
DR STRING; 1201294.BN140_1067; -.
DR KEGG; mbg:BN140_1067; -.
DR PATRIC; fig|1201294.9.peg.1180; -.
DR HOGENOM; CLU_072599_0_1_2; -.
DR BioCyc; MBOU1201294:BN140_RS05330-MONOMER; -.
DR Proteomes; UP000009007; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000009007}.
FT DOMAIN 156..184
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 185..214
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 293 AA; 32695 MW; E39AD158E1333F2B CRC64;
MMNNYGLYTR GGVITERNAD YATIRLRVPG GVLSAAQVKQ LAKISEKYGD GTLHLTMRQT
AEIPHVNPAN LKRIAKALEK NGTPLGAEQN EVVNIMACPG TERCKYANCE TIDLARKVDA
RVFGKELPIR LRIAISGCTY MCNSPLLNDI GIIGRIRPLR IPGLCTGCGT CVEYCKERAI
TLKNGISVLD ESKCVQCGVC IHSCPYHLLK SEYDHYQITV GGRRGANPCV GRELVTVETE
EEVVEVIDRV VYWVYRTAWS GRFLADQMDE IGYEKFREDI RKEFGPKEQA AEE
//