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Database: UniProt
Entry: A0A1M3M1Y1_9PROT
LinkDB: A0A1M3M1Y1_9PROT
Original site: A0A1M3M1Y1_9PROT 
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
//
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