ID R9PPT7_AGAAL Unreviewed; 822 AA.
AC R9PPT7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885, ECO:0000256|RuleBase:RU368014};
DE Short=TMAO reductase {ECO:0000256|RuleBase:RU368014};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885, ECO:0000256|RuleBase:RU368014};
GN Name=torA {ECO:0000256|RuleBase:RU368014};
GN ORFNames=AALB_3419 {ECO:0000313|EMBL:GAD03339.1};
OS Agarivorans albus MKT 106.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Agarivorans.
OX NCBI_TaxID=1331007 {ECO:0000313|EMBL:GAD03339.1, ECO:0000313|Proteomes:UP000014461};
RN [1] {ECO:0000313|EMBL:GAD03339.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Yasuike M., Nakamura Y., Kai W., Fujiwara A., Fukui Y., Satomi M., Sano M.;
RT "Draft Genome Sequence of Agarivorans albus Strain MKT 106T, an Agarolytic
RT Marine Bacterium.";
RL Genome Announc. 1:e00367-13(2013).
CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC anaerobic reaction coupled to energy-yielding reactions.
CC {ECO:0000256|ARBA:ARBA00003013, ECO:0000256|RuleBase:RU368014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-
CC [cytochrome c] + 3 H(+) + trimethylamine N-oxide;
CC Xref=Rhea:RHEA:24236, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15724,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58389; EC=1.7.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00029296,
CC ECO:0000256|RuleBase:RU368014};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|RuleBase:RU368014};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000256|RuleBase:RU368014};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU368014}.
CC -!- PTM: Exported by the Tat system. {ECO:0000256|RuleBase:RU368014}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312,
CC ECO:0000256|RuleBase:RU368014}.
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:GAD03339.1}.
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DR EMBL; BARX01000026; GAD03339.1; -; Genomic_DNA.
DR RefSeq; WP_016403106.1; NZ_BARX01000026.1.
DR AlphaFoldDB; R9PPT7; -.
DR STRING; 1331007.AALB_3419; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000014461; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-UniRule.
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 InterPro; IPR011887; TorA.
DR NCBIfam; TIGR00509; bisC_fam; 1.
DR NCBIfam; TIGR02164; torA; 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; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368014};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU368014};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU368014}; Periplasm {ECO:0000256|RuleBase:RU368014};
KW Reference proteome {ECO:0000313|Proteomes:UP000014461};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368014}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|RuleBase:RU368014"
FT CHAIN 35..822
FT /note="Trimethylamine-N-oxide reductase"
FT /evidence="ECO:0000256|RuleBase:RU368014"
FT /id="PRO_5029945928"
FT DOMAIN 44..84
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 88..560
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 679..798
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 822 AA; 92639 MW; 1318DE80A9FCF595 CRC64;
MAITRRGFLK GILATSASTL IGPSLLAVSN DAAAAETAGS WKVSGSHWGA FRARVYAGKV
QEIKPFEADK YPTEMLKGIK GILYSPSRIR YPMVRYDWYL KRNKSDTSQR GDNRFIRVTW
DEALDLFYQE LERVQKDYGP WALHAGQTGW RQTGQVHSCG NHMQRAVAMH GFSVNKVGDY
STGAGQTIMP YVLGTTEVYA QGTSWPLILD NSKTVVLWAT DLMKNLQVGW ACETHESFEY
LEQLKDKVAN KQIRVISVDP VRTKTQKYLD CEQRYVNPQA DVPFMLAIAH TLYTEELYDK
EFLNTYALGF EDFIPYVTGE SKDKVEKTPE WAEAICGVPA DEIREFARLL ASDRTQLIFG
WCIQRQQHGE QPYWMGAVIA AMLGQIGLPG GGVSYAHHYS SIGVPSTGAA APGAFPRNPD
KPNERVHMNQ DFKGYSSTIP VARWIDAIME PGKVINANGA KITLPDIKMM VFSGCNPWHH
HQDRNRMKKA FQKLETVVSI DFTWTASCRF SDIVLPACTQ WERNDLDLYG SYSNRGIIAM
HKLVDPLYQS KTDFEIFTLL TQRFGKSKEY TQGKSEMEWV KQLYDECAAA NKAKFDMPDF
MTFWKEGWVD FGKGKNWTRQ ADFREDPEIN ALGTPSGFIE IFSRKIDRYG YDDCQGHPMW
FEKAERSHGG PGSEEFPIWL QSCHPDKRLH SQMCDSEEFR ATYAVQGREP LYINPEDAKK
RGIKDGDLVR VFNKRGQLLA GAVVSEDYAK GVARLQEGAW YGPVDETIGA LDTYGDPNTL
TMDIGSSQLA QATSANTCLV EYEKFTGKAP AVSSFGGPKE MS
//
