ID   A6VMS1_ACTSZ            Unreviewed;       825 AA.
AC   A6VMS1;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   02-SEP-2026, entry version 100.
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   OrderedLocusNames=Asuc_0898 {ECO:0000313|EMBL:ABR74268.1};
OS   Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS   130Z).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Pasteurellales; Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR74268.1, ECO:0000313|Proteomes:UP000001114};
RN   [1] {ECO:0000313|Proteomes:UP000001114}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC   {ECO:0000313|Proteomes:UP000001114};
RX   PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA   McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA   Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA   Burkhart K.B., Harkins V., Vieille C.;
RT   "A genomic perspective on the potential of Actinobacillus succinogenes for
RT   industrial succinate production.";
RL   BMC Genomics 11:680-680(2010).
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=trimethylamine + 2 Fe(III)-[cytochrome c] + H2O =
CC         trimethylamine N-oxide + 2 Fe(II)-[cytochrome c] + 3 H(+);
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:ARBA00049407,
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   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000256|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312,
CC       ECO:0000256|RuleBase:RU368014}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000746; ABR74268.1; -; Genomic_DNA.
DR   RefSeq; WP_012072646.1; NC_009655.1.
DR   AlphaFoldDB; A6VMS1; -.
DR   STRING; 339671.Asuc_0898; -.
DR   KEGG; asu:Asuc_0898; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   OrthoDB; 9815647at2; -.
DR   Proteomes; UP000001114; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR   GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter.
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:0009061; P:anaerobic respiration; IEA:TreeGrafter.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   FunFam; 2.40.40.20:FF:000009; Biotin sulfoxide reductase 2; 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; 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; IPR050612; Prok_Mopterin_Oxidored.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR011887; TorA.
DR   NCBIfam; NF011682; PRK15102.1; 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};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU368014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001114};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PROSITE-
KW   ProRule:PRU00648}.
FT   CHAIN           33..825
FT                   /note="Trimethylamine-N-oxide reductase"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00648"
FT                   /id="PRO_5049188046"
FT   DOMAIN          42..82
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          86..560
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          679..799
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   825 AA;  93763 MW;  ECEEE0641B37977E CRC64;
     MQQSRRQFLK NMSIIAGSFA MPSFLIPREA NAQLPTPEWK VTGCQWGAVR AKVENGRVSE
     IKPFEFDKHP TEMINGIKDI LYGETRVRYP MVWVDWLKNR QNSDRSRRGD NRFVRVSWKE
     ALDLFYEELE RMQKDYGPWA LHTGNVGWRS SGQFHSCGNH MIRAIAMHGA SVGTVSDYST
     GAGQTILPYV LGDTEVYSQG TSWEIILKET ENLIFWASDP VKNLQVGWNC ETHEAYAYLE
     QLKQKVAEKK INVISVDPVK SKTQNFLDCE QLYVNPQADM PFMLAIAHTL YKENLYDKAF
     LDVYTLGFEK FVPYLLGETE DKIEKTPEWA VPICGISAEK IREFARMLAG KRTQLIFGWA
     IQRQQHGEQP YWMGAVLAAM LGQIGLPGGG ISYAHHYSSI GVPTSGAATP GSFPSNLGEE
     QTPKYTNKDY KGYSDVIPVA RVTDSLLQPG ESIDYNGKKI VYAPYKMAIF TGCNQWGRQS
     DLNKMKKAFQ QLETVVTLNY SWTATCRFAD IVLPACTPFE RNDIDTYGSY SNRGVLAMHK
     LVEPMYESRS DFEIFKDLCS RYGEGKAEEY CQNLDEMGWL NRLYTECRRA NRGRFKMPRQ
     FDEFWKTGYV LFPEGKPWVR HADFREDPEL HALGTPSGFI EIYSTKIANY GYDNCKGHPM
     WFEKDERSHG GPKSDKFPFW MQSVHPDKRL HSQLCEAKNL RETYSVQGRE PFYMNPQDAE
     KLGIKDGDLV RVFNERGQVL VGAVLSDDFP SGVVRLQEGA WYSPVDESIG ALDTYGCPNT
     LTLDIGASKL SQATCVSTCL VNVEKWQGDV PVPNGFTGPV EVTHQ
//