ID A0A1M3M1Y1_9PROT Unreviewed; 686 AA.
AC A0A1M3M1Y1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:OJX79592.1};
GN ORFNames=BGO92_14145 {ECO:0000313|EMBL:OJX79592.1};
OS Magnetospirillum sp. 64-120.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=1895778 {ECO:0000313|EMBL:OJX79592.1, ECO:0000313|Proteomes:UP000184435};
RN [1] {ECO:0000313|EMBL:OJX79592.1, ECO:0000313|Proteomes:UP000184435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=64-120 {ECO:0000313|EMBL:OJX79592.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OJX79592.1}.
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DR EMBL; MKVK01000014; OJX79592.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3M1Y1; -.
DR STRING; 1895778.BGO92_14145; -.
DR Proteomes; UP000184435; Unassembled WGS sequence.
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; cd02766; MopB_3; 1.
DR CDD; cd02786; MopB_CT_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; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR037920; YoaE_C.
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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 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}.
FT DOMAIN 1..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 686 AA; 74163 MW; 88909726F62B96E8 CRC64;
MRTFASVCPH DCPSACPLDV VVDDDGRVGR LHGAAMPYTE GVICAKVARY SERIHHPDRI
LTPLRRVGDK GEGRFAPISW DEALDEIAQR FTTAAANWGL ESVWPYFYAG TMGLVQMGAT
NRLRRAMGYS GQRKTICAAI AGAGWLAGNG AKYSVDSREM ADSQLIVIWG ANPAATQVHL
MGLAAKARKA HGAKLVVIDP YRTPTAEKAD LHLMLRPGTD AALACAVMHV LFRDGLVDQD
YMDRYAAGTE ALRDHVAGRD PHWAAAITGL SATQIEDFAR LYGTTQRSLI RVGYGMSRSR
NGAVNVHAVS CLPVLTGAWQ HRGGGATQSL SAGFQLDRTL MEALDLPEPA VRQLDMSRIG
AILTGESQAL INGPPVMAML IQNSNPATVA PETAKVWRGL ARPDLFVAVH EQVMTQTARF
ADLVLPATTF VEHDDLYTSY GHTFLQAAKK VIEPLGEARS NHWLVAQLAR RLGARHASFE
MTEWQMVDAC LRASSLPGAD DLHARRWLDC APSFEKSHYL DGFGHGGRFR FAADWASVGP
DHAGLPSLPD HLGIIESADA EHPFRLITPP SRHFLNSSFS ETATSRRMAA RPTVLLHRDD
ALKLDVKDGD VVRLGNRRGS VMVHAALTDG IAKGVVAVEG IWPDECFPGG IGVNALVGDD
PVPPSGGAAF HDSAIWIKPV SFGENA
//