ID A0A1G5P7V0_AFIMA Unreviewed; 832 AA.
AC A0A1G5P7V0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN ORFNames=SAMN03080610_03345 {ECO:0000313|EMBL:SCZ45161.1};
OS Afifella marina DSM 2698.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Afifellaceae; Afifella.
OX NCBI_TaxID=1120955 {ECO:0000313|EMBL:SCZ45161.1, ECO:0000313|Proteomes:UP000199347};
RN [1] {ECO:0000313|EMBL:SCZ45161.1, ECO:0000313|Proteomes:UP000199347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2698 {ECO:0000313|EMBL:SCZ45161.1,
RC ECO:0000313|Proteomes:UP000199347};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; FMVW01000010; SCZ45161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5P7V0; -.
DR STRING; 1120955.SAMN03080610_03345; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000199347; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
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; IPR006658; BisC.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
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 InterPro; IPR019546; TAT_signal_bac_arc.
DR NCBIfam; TIGR00509; bisC_fam; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
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; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
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:UP000199347};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 50..90
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 94..564
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 686..799
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 832 AA; 91492 MW; 0274B2D6A53B8099 CRC64;
MSTTSTPQRP AVSRRHFLQG AAALGALGMA GSSLLTKGAL AQSASKDTIS ACHWGVFRGH
KEDGRLTALT PWEKDPFPSP QLPGVLDSIY SPTRIKYPMV RRAFLEQGPG ADPEGRGTGD
FVRVSWEKAI ELVANELVRV RDTYGPTGIF GGSYGWKSPG KMHNCQTLLR RLLKLNGGFT
NSSGDYSTGA AQVILPYVVG SIEVYEQCTT WPVLAENTEL MVFWGANPLR NSEICWQVAD
HGSFVGVDLL KKAGTKAICI DPVRTETAQR LDAEWIAPRP QTDVAMMLGI AHTLYSEGLH
DQGFLDKYTT GFDKFLPYLT GEVDGQPKSA EWASAICEIP ADTIKDLARR FASHRTMLAL
GYSTQRQHHG EQVHWMLITL TSMLGQIGLP GGGYGLSYHY ASGGAPTHNS PILTAMSDQP
GGGTVAVGEP AWLAGGGTAS IPVSRLVETL LNPGKKMDFN GHEIELPTIK LAYWVGGNPF
SHHQDRNEMV RAWRNLETFI VHDFQWTATA RHADIVLPAT TSYERNDISQ VGDYALSHIV
PMKKLIDPVF ESRTDYDIFT AIAHKLGKGY EYTEGKTEMD WIRGFYEAAM IEARAKGMEM
PVFDAFWDSD EALEFPLLDE QKNFVRYADF RADPLLNALG TASGKIEIFS RNIEKMHYDD
CPPHPSWMEP VERLDGPTTR YPLHIAANHP VKRLHSQLCG TSLREDYAVK GREPCWIHPE
DAAARGLVDG DIVRVFNDRG QILAGLVVTD VIRKGVVRIN EGGWFDPVDP RTPGSLCRYG
DVNNLTVGIG TSKLAQGNCG QTAVAEVEKF EGPVPEIMVF SEPAAQKDAS KT
//
