ID H6LJS1_ACEWD Unreviewed; 646 AA.
AC H6LJS1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:AFA47472.1};
GN OrderedLocusNames=Awo_c06780 {ECO:0000313|EMBL:AFA47472.1};
OS Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655
OS / WB1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=931626 {ECO:0000313|EMBL:AFA47472.1, ECO:0000313|Proteomes:UP000007177};
RN [1] {ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RA Poehlein A., Schmidt S., Kaster A.-K., Goenrich M., Vollmers J.,
RA Thuermer A., Gottschalk G., Thauer R.K., Daniel R., Mueller V.;
RT "Complete genome sequence of Acetobacterium woodii.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AFA47472.1, ECO:0000313|Proteomes:UP000007177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1
RC {ECO:0000313|Proteomes:UP000007177};
RX PubMed=22479398; DOI=10.1371/journal.pone.0033439;
RA Poehlein A., Schmidt S., Kaster A.K., Goenrich M., Vollmers J., Thurmer A.,
RA Bertsch J., Schuchmann K., Voigt B., Hecker M., Daniel R., Thauer R.K.,
RA Gottschalk G., Muller V.;
RT "An ancient pathway combining carbon dioxide fixation with the generation
RT and utilization of a sodium ion gradient for ATP synthesis.";
RL PLoS ONE 7:E33439-E33439(2012).
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; CP002987; AFA47472.1; -; Genomic_DNA.
DR RefSeq; WP_014355075.1; NC_016894.1.
DR AlphaFoldDB; H6LJS1; -.
DR STRING; 931626.Awo_c06780; -.
DR KEGG; awo:Awo_c06780; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_9; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000007177; 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:InterPro.
DR CDD; cd02775; MopB_CT; 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; IPR006657; MoPterin_dinucl-bd_dom.
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 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.
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 Reference proteome {ECO:0000313|Proteomes:UP000007177}.
FT DOMAIN 3..60
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 646 AA; 72042 MW; 5D10B91E2946F9CE CRC64;
MEENTVVTTC TRDCPNTCGL LAQVKDGKVI KLVGNKAHPI NQGRSCIKCS HFIERVYHQE
RVLHPLKKIN GQFEQISWEE ALDEIAARMK TICREKSPEA ILYYQGFGER SALKLINRRF
FNLLGNTTIT KGTICGGAGQ GSQDLDFGNR ISHDVRDYHN SQAMILWGRN PLATGVNLLP
YMKDIKKKGG KVILIDPVNT ETAPLCSMHV KPKPGTDSYL AMALSRLLHE AGAEDQEFLE
KHCINYPEYK KLVYAHSVAE YAAMCDVKIE EIKEIADVLI NQKPTALVLG WGLHRWEYAH
TTMRAIDALG AVAGSIGVSG GGVSQGFEEY APYDWSIWGD ALQPPERRKF FMQLIGSELL
AADPPIELAF VTAGNPVAMV PDANVTQKAF EKIPFLVVAG HFLDDTGIMA DLFLPVTTFL
EEKDIIASYG HDFIGPLNPA IPPVGECKSD FDIFMELGSR FDFADSYVKS VDQWLEIIMR
PTLEKGGSLA EIFRLGINNP DAPEVPYRDK VFPTETGKFQ LMTVFEQPAQ WDRDYQFQLM
SVAPREWICS EVTLESQTKL LEVKINTEKA LALGLVDGKA CVVENQFGRI RCIATFVPDQ
RPDLVVIYRG GWGQAGRNVN VLTRGLVTKV GNGTPYYETR VNVKKL
//
