ID A0A4R2MV95_9BURK Unreviewed; 900 AA.
AC A0A4R2MV95;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN ORFNames=EV674_13916 {ECO:0000313|EMBL:TCP12181.1};
OS Simplicispira metamorpha.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=80881 {ECO:0000313|EMBL:TCP12181.1, ECO:0000313|Proteomes:UP000295182};
RN [1] {ECO:0000313|EMBL:TCP12181.1, ECO:0000313|Proteomes:UP000295182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1837 {ECO:0000313|EMBL:TCP12181.1,
RC ECO:0000313|Proteomes:UP000295182};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAR-2019) 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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
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:TCP12181.1}.
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DR EMBL; SLXH01000039; TCP12181.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2MV95; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000295182; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR041460; Molybdopterin_N.
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 PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000295182};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 56..97
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 101..561
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 674..790
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 900 AA; 99517 MW; 70D16CDC5CFB20F7 CRC64;
MNFTRRQWMG AGAAGMLGTV ATGMKLNPLA QAMAATEMDA NAQLAALKSF TGKVPHATHY
GPLVATVEQG RIVHIEAQAS DKMPTAMLTE GVLDRTYDKT RVVGPMVRKS YLEWEQNGRK
GSNKPELRGK DEWVQVGWDT ALGLTAKAIL DTIEKYGNEG CFSSSYGGWS HAGIFRPNVL
QGRFFNLLGG SSMTTGDYSA GAGQVIMPMV IGDMEVYSAQ TAWEQLRDHT ELVVFVGCDP
DKNNRIEYTV PDHEMYSGWE AIKKAGCRFI SINPQVTTTD EKMGSEWVRI IPNTDTALFM
AMGYHLLSQN KHNQAFIDKY TVGFDKYRAH LEGKDGTPPK TPAWAAKITG IPAAKIRAMA
ELMASKRTQL CGSWAIQRAH HGEMPYWAIV NFACILGNIG LPGQGVGFSW HYGGGGMPQS
GGTAPTGLSQ GRNPVKKICP ASRISEMLLN PGQEFTYNGS KYTYPQAKLI YNAGNNAFSH
QQDLNELARA IHSVDTIICQ EPWWNGSARW ADIVLAATTT VERNDITSAG TYSIDKVYAM
KQIIAPQFDA LDDFEIFRRL ASLCGVEYAF TEGKTQMDYV KAAYEASSAA PHMPFDQFWA
EGMARIPVPP EAHKWVRHGD FRADPAKHPL HTTSGKIEMY SSTIAKMNIP DMPPMPTWQE
PGEYLGNARK GQVHVVSPHP YWRLHSQMNN SERLRKRYTI QTREPLTISV EDAKQHNIRN
GDLVELYNER GAVVVGARVS DKIMPGVVSL YEGAWPQLDS KGRCNNGLVN FLTSSRRASG
LTQATTANTC IASLRKCTDA DPGGTKAFDP PKIVKSNIQF DEKFFGVERA AALREKATAS
MSPAEKIFYQ RCTVCHGPRD PGHFTEKQWQ GITPSMFQRA GLNADEQKIV LDFLLQNAKH
//
