ID L8JK19_9GAMM Unreviewed; 847 AA.
AC L8JK19;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN ORFNames=C942_00064 {ECO:0000313|EMBL:ELR67757.1};
OS Photobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR67757.1, ECO:0000313|Proteomes:UP000011134};
RN [1] {ECO:0000313|EMBL:ELR67757.1, ECO:0000313|Proteomes:UP000011134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK15 {ECO:0000313|EMBL:ELR67757.1,
RC ECO:0000313|Proteomes:UP000011134};
RA Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT "Genome Assembly of Photobacterium sp. AK15.";
RL Submitted (DEC-2012) 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:ELR67757.1}.
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DR EMBL; AMZO01000001; ELR67757.1; -; Genomic_DNA.
DR RefSeq; WP_007461169.1; NZ_AMZO01000001.1.
DR AlphaFoldDB; L8JK19; -.
DR PATRIC; fig|1056511.3.peg.65; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000011134; 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 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:SF4; TRIMETHYLAMINE-N-OXIDE REDUCTASE 1; 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 Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..40
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 41..847
FT /note="trimethylamine-N-oxide reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003993112"
FT DOMAIN 54..94
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 98..568
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 688..804
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 847 AA; 94516 MW; 1D0F24107CA67DDD CRC64;
MATQILNKGV SRRRFLSGMV AASAASVVGT SLLAPRKAMA ASHEKANFTG EVLSGSHWGA
FRAKVENGVW VDTVPFEKDK HPTSMINGVR EVVYNPARVK YPMVRIDWLK HGYKSDTTQR
GDNRFVRVPW SQALDFFYHE MERIQNNFGP SALYAGHTGW QSVGKLHSAG TMMMRAIGLH
GTFLAKAGDY STGAAQVILP YVAGAMEVYE QQTSWPLVLE HSDTIVVWGS DPIKNLQVGW
LVPDHSPYAY YEQLAEKVKN KEIKVLYIDP VVSDTQKFVG GEQVPVNPQT DVPLMLAIAH
TLYKENLYNK DFIADYTTGF DKFIPYLTGE KDGVEKTPEW AEKICGIDAD KIRELARTMA
SGRTQIIGGW CLQRMQHGEQ YAWMLVVVAA MLGQIGLPGG GFGFGWHYND AGSITSNGPL
MSGFSGVTGV DPIHNGSYKG YSTYIPVARF VDCIENPGKK IQWNGHDITF PEMKMAVFCG
NNPFNHHQDR NKMIKAWRKL ETVVTIEHQW TATCRFSDIV LPATTTHERN DIEQYGNHSN
AGIIALPKVV EPMFESRDDF DIFRDLCRRF DREEAFTGGK TQMQWIEEIY NGARLQGRGL
GVRLPNFKKF WEGEGFVDFP AGKEWVRHES FRKEPDLEPL GTATGLIEIY CKTIADMGYD
DCQGHPMWFE KKERSHGGPR SDRFPINLQS THPKHRLHSQ LCSSTEHRAT YAVADREPIY
ISTEDAKARG IKSGDIVRVF NDRGELLAGA VVTDDYKPGV CRIHEGAWYS PLEGGKPGTL
CTYGDPNVLT QDIGSSKLAQ ATSAASAVVQ IEKYKGKVPA VTGFHGPTEV TDIDPLFPAM
DLKSSCR
//
