ID A0A4R2N1C5_9PAST Unreviewed; 828 AA.
AC A0A4R2N1C5;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN ORFNames=EV697_102246 {ECO:0000313|EMBL:TCP13365.1};
OS Bisgaardia hudsonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Bisgaardia.
OX NCBI_TaxID=109472 {ECO:0000313|EMBL:TCP13365.1, ECO:0000313|Proteomes:UP000294841};
RN [1] {ECO:0000313|EMBL:TCP13365.1, ECO:0000313|Proteomes:UP000294841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 28231 {ECO:0000313|EMBL:TCP13365.1,
RC ECO:0000313|Proteomes:UP000294841};
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:TCP13365.1}.
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DR EMBL; SLXI01000002; TCP13365.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R2N1C5; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000294841; 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 NCBIfam; TIGR00509; bisC_fam; 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; PS00932; MOLYBDOPTERIN_PROK_3; 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:UP000294841};
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 682..803
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 828 AA; 92095 MW; 3C31A0EEA3FF9851 CRC64;
MKKENKVNIK RREFLKNSSL GIAGVSLSGG IASSVVSQNT LASEMKTVVT AAHWGPLGVV
VENGKVVKSG PAIPPVIENE LQSVVADQLY SETRIKYPMI RKGYLENPGK SDTTMRGRDE
WVRVSWDQAL DLIAKEFKRV RSEGSFENIF GGSYGWQSAG SLHSGRTLLH RYLNATGGFV
GHKGDYSTGA AQVIMPHVLG TIEVYEQQTS WETILESTDI IVLWSANPLT TMRIAWTSTD
QKGIEYFKKY QATGKRIICI DPIKSETCKA LNAEWIPTNT ATDVPLMLGM AHTLVIQNKH
DKAFLKKYTT GYAKFEDYLL GKVDGQIKDA EWASKICGVP ADVIKQLAND FSSKRTMLMA
GWGMQRQQHG EQTHWMLVTL ASMLGQIGLP GGGFGFSYHY ANGGVPTTTG GVIGSMSATL
DNDTSNTGQS WLSKAAKLSF PLARIADVLL NPGKTIQYNG TEITYPDIKL VYWAGGNPFV
HHQNTNTLVK AWQKPETIIV NEINWTPTAR MADIVLPITT SYERNDLTMT GDYSMMHIVP
MKQVVEPQFE ARNDYDVFVE LSKRAGVEDV FTDGKTEMDW LKSFYQSAFD AARKNRVLMP
KFEKFWEENK PITFTASEKA KKWVRYGEFR EDPLLNPLGT PSGKIEIYSD TIAKMNYDDC
RGYPSWFEPE EFAGNVTEEY PLALVTPHPY YRLHSQLANT SLRQKYVVKD REPALIHPED
AKAHGIVDGD IIRIFNKRGQ VLAGAVVTDD IIKGTIGLHE GAWYDPLDLG VSEKPLCKNG
CPNVLTMDIG TSKLAQGNSP NTCIVQVEKF TGETPEVTVF KQPKQANA
//
