ID C8WM50_EGGLE Unreviewed; 911 AA.
AC C8WM50;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ACV54604.1};
GN OrderedLocusNames=Elen_0619 {ECO:0000313|EMBL:ACV54604.1};
OS Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 /
OS KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B) (Eubacterium lentum).
OC Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC Eggerthella.
OX NCBI_TaxID=479437 {ECO:0000313|EMBL:ACV54604.1, ECO:0000313|Proteomes:UP000001377};
RN [1] {ECO:0000313|EMBL:ACV54604.1, ECO:0000313|Proteomes:UP000001377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 /
RC NCTC 11813 / VPI 0255 / 1899 B {ECO:0000313|Proteomes:UP000001377};
RX PubMed=21304654; DOI=10.4056/sigs.33592;
RA Saunders E., Pukall R., Abt B., Lapidus A., Glavina Del Rio T.,
RA Copeland A., Tice H., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Chain P., Meincke L., Sims D., Brettin T., Detter J.C.,
RA Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Eggerthella lenta type strain (IPP VPI
RT 0255).";
RL Stand. Genomic Sci. 1:174-182(2009).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001726; ACV54604.1; -; Genomic_DNA.
DR RefSeq; WP_015760060.1; NC_013204.1.
DR AlphaFoldDB; C8WM50; -.
DR STRING; 479437.Elen_0619; -.
DR PaxDb; 479437-Elen_0619; -.
DR KEGG; ele:Elen_0619; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_11; -.
DR OrthoDB; 9796486at2; -.
DR BioCyc; ELEN479437:G1GFY-627-MONOMER; -.
DR Proteomes; UP000001377; 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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR43742:SF9; TETRATHIONATE REDUCTASE SUBUNIT A; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 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.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 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:UP000001377};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 56..112
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 911 AA; 100348 MW; CC7A1A8E475154FF CRC64;
MENRSNIAAP GGITRRSFVK GGAAAAAIGA TGALVGCAPQ GDGKASDAAA PAEDEGVWLP
SQCNMCFNAC SILGHVVDGK LVEIKGDDRS PAGWGHLCGK GTAGIMQLYD ENRITKPMKR
TNPKKGVGID PGWEEISWDE AYDLILEKLD EQKQKNKPVI VFALITSIIS WIDSMNWLGS
NGNIPIPFKA DICGAPTHPI SALLTGCGNA LPDYAHCKYL MQFGTQAGVA TRHGTSITAK
VFADARANGC KLVNFDPHMS GAAEKADEWV PIRPGTDAAV ALAMANLLVN EYDLYDKEFL
AARTNGPSLV DPATQRIVRD ASKGNKALYW DLSDNTAKPY DEVKEPALEG DFEVDGIPVR
TAFSIFKDSV AKYTPEYAEE VTTIPADTTR RLAKEFGEAA CIGQTVEVDG LTVPYRPVAV
DTFSGIARHK HGFITHWAIL QLNTLVGSTF SRGGYLGFYT RNKYGFYEGD KDHAWEFTIW
EEDGLIEDLN MAHGWPSNGS HYKHIREASY TPTSEAMEEL QPLTMDQHFG YIAQVQPEVY
GTEPSEVAFC MASNPLKNWC NHDYQAKVLE SFDWIFGMDI YLNDSSYYYD LIIPEPCYLE
RFDPLPLSFN NHRVPGLPEV PYIVAGRMPI VEAKDNCPSA LDTFGALAAK AGKTAEYSAA
LNDYYKLADE YKLDGKEQIT AERVCDAALK SLAGKDRGID WFRENGVLTR ERKADEVYVF
AAGMEGRIPL YFDFMLEAKE KIEAEVDKLG IYWETDDYIP LPEFMPCLDH EVEEEGFDLF
PVYWTNAINT DTWQVENAWI NEINELDDTT YFLEINAATG AAKGIKSGDK VRLSNRDGDV
VEGVAVLTEF VHPECVASVG GHLNAKSDYQ PIGKTKGTAV NHLVPAGDPK RMEYVGSGVD
QCVRCKLEKI S
//
