ID O27609_METTH Unreviewed; 666 AA.
AC O27609;
DT 01-JAN-1998, integrated into UniProtKB/TrEMBL.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Catalytic subunit of nitrate reductase (Flp) {ECO:0000313|EMBL:AAB86041.1};
GN OrderedLocusNames=MTH_1567 {ECO:0000313|EMBL:AAB86041.1};
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420 {ECO:0000313|EMBL:AAB86041.1, ECO:0000313|Proteomes:UP000005223};
RN [1] {ECO:0000313|EMBL:AAB86041.1, ECO:0000313|Proteomes:UP000005223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H
RC {ECO:0000313|Proteomes:UP000005223};
RX PubMed=9371463;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-i., Rice P., Nolling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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DR EMBL; AE000666; AAB86041.1; -; Genomic_DNA.
DR PIR; B69076; B69076.
DR RefSeq; WP_010877176.1; NC_000916.1.
DR AlphaFoldDB; O27609; -.
DR STRING; 187420.MTH_1567; -.
DR PaxDb; 187420-MTH_1567; -.
DR EnsemblBacteria; AAB86041; AAB86041; MTH_1567.
DR GeneID; 77402087; -.
DR KEGG; mth:MTH_1567; -.
DR PATRIC; fig|187420.15.peg.1530; -.
DR HOGENOM; CLU_000422_13_3_2; -.
DR InParanoid; O27609; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd02766; MopB_3; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005223}.
FT DOMAIN 1..57
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 666 AA; 74026 MW; BCF49A546155E4C5 CRC64;
MKVLTTCTRD CPGSCGLTVN VSRGKVNSIE GSSIHPHTRG FICKNTARYH VRRLYSDRRV
LKPLKRDGRQ WKTISWDEAL HVISDKLNEC MDEHGAESIV YYQGFGARTA LRLLNRRFFN
LIGATTLRGT LCGGAAIAAQ SKDFGRRLSH DPSDHLNSRN IFIWGRNPAV TDINLWRIIK
RAQKHGTRVI TIDPIRTQTA VKSDIHCQIE AGKDLYLAIA MAKIIMAEEL HDSGFIEKHA
ENFDSYIEIL DEFNLNQLSE LSGVPLKIIS KLAHLYSDGP SSIILGWGLQ RYFNSYMACR
FIDALAAISG YIGVSGGGVS SGFDEYGAFD ESVTLEGAGN GRKVSMPLFG REIVNMNSPT
VNCVFITAGN PVTLGPNSIQ TLNALREVDF VVMVDLFLND TAHTADLFLP ATTFLEETDL
VGSYGHPYVS PVNAAVKPLG ESHSEFWILQ RLSEIMGFAD MEGTRMEWLE IIASKVLDYH
GIEICDLLEK PYRSPGFPPV PFEGPLFYTD NGRFNLPSDR PYEMEQHDGA HPENSIRLLT
VMSPQWVGSV EPTFHKGLVE IYLNPGTLSQ LGFNDGEISV AESNAGKSCV IVRSSEDVHP
LCALSFRGTW LSKGGCINTV IEDRETIMGH GTAYNETRIK LKKVSGGVSV HEMCHETHKY
KSRHYE
//
