ID C8WGB9_EGGLE Unreviewed; 954 AA.
AC C8WGB9;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:ACV55160.1};
DE Flags: Precursor;
GN OrderedLocusNames=Elen_1190 {ECO:0000313|EMBL:ACV55160.1};
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:ACV55160.1, ECO:0000313|Proteomes:UP000001377};
RN [1] {ECO:0000313|EMBL:ACV55160.1, 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 -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; CP001726; ACV55160.1; -; Genomic_DNA.
DR RefSeq; WP_015760450.1; NC_013204.1.
DR AlphaFoldDB; C8WGB9; -.
DR STRING; 479437.Elen_1190; -.
DR PaxDb; 479437-Elen_1190; -.
DR KEGG; ele:Elen_1190; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_11; -.
DR OrthoDB; 9815647at2; -.
DR BioCyc; ELEN479437:G1GFY-1192-MONOMER; -.
DR Proteomes; UP000001377; Chromosome.
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; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10518; TAT_signal; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
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 121..627
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 794..871
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 954 AA; 106334 MW; 3130AC115FEE46F5 CRC64;
MSLLDKSLKR RDFLKGTAAA AAATAAFGLS GCSTGSAQAA GSDGAHVVAS DASILADAGE
WMPIHCHQNC NQMCLNMGYV VDGVVVRQKT DDAREDSFDC PQQRGCLRGR SLRQQVYNAD
RIKYPMKRKS WQPGGAENAH GELRGKDEWE RISWEEALDY IADELKRVYA EYGQDAVICN
GWRWAPGSAM FPVIGGAVYD TETESFGCWA FQTEALGLYS WGDHPDIMMG PDKYDLPNAD
TIVLYGCNPA WAQHSSMYWL NNAKESGTGF VYVGPSYNVT AAQLGARWIR VRPGTDTAFL
LAVIYEMIRL DGERGDIIDW DFVNERTVGF TPETMPEDAT TDENYRDYIL GAYDGTPKTP
EWASEICGTP VEDITWYAEL AAKDNKVIFF HSYAASRYLG AENLPQAFMT VSALGGHYGK
SGHGSAAIYT WDAGDSGYRL IQHAGGEYAY IDNLVGSPGA TGPNRCIEGN SWWSSLAEGK
YLSTSEGPYD LGSGDDPTKL RANTPTYHAA REMPVNPRLM FATCSNFMQT RGNLPTAIEV
MRAADTCISL EIKYSLTASF ADIILPVATH WEGNDDESWG ELCWPSPFGD GNGQKQRKDA
LLAWRPLVKP MYEAREEKRI CRDIVERMGF DADDAYPKSN YDQWLGYFLG MRELSEDLSR
WEPVITWTAD DNRKHHANYP EQQGKISFDQ FMADGSYVVR RSPDDRRNYI GYRDDKLRIG
ENGEVVVADT AWPRPSRSGK LEIYCQFKAD NVNRTGLNPE PIKPYANYFV PNRGYQDTFA
DWDAKVKGAY PLQAYTPHYM RRAHTCYDNM TWTQEAFRNP VFMNAQDAEE RGIEAGDTVV
CYNDFGRMLR IAQPLQGMMP GTVGIPHGVR SLFDESDPAG IVDRGGSEQM LSDGQQSNYF
PQVDGYNSLL IEIEKYDGEA LVEDCDRGPF LAAGIDAEGT PAYVAEGMYE GKEA
//