ID R7C0X9_9BURK Unreviewed; 847 AA.
AC R7C0X9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN ORFNames=BN641_00178 {ECO:0000313|EMBL:CDD71630.1};
OS Sutterella sp. CAG:397.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=1262976 {ECO:0000313|EMBL:CDD71630.1, ECO:0000313|Proteomes:UP000018105};
RN [1] {ECO:0000313|EMBL:CDD71630.1, ECO:0000313|Proteomes:UP000018105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:397 {ECO:0000313|Proteomes:UP000018105};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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:CDD71630.1}.
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DR EMBL; CBHO010000144; CDD71630.1; -; Genomic_DNA.
DR AlphaFoldDB; R7C0X9; -.
DR Proteomes; UP000018105; 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 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; 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 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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
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:UP000018105};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 81..118
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 125..587
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 704..817
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 847 AA; 94354 MW; 80A0A08526E9FE78 CRC64;
MTELTRRSFL AGAAAVATAP VVGTAHAKDT KVPRPDVKAD YPAAEKTQAL FDRVPDVEPD
VANSGTFDFG VSNLNEGETI TATRWGIVRP VVKGGRVVEL KPFEYDYAPS PNIQGLAEIP
YCEARIRYPM VRESYLKSGP KSKEKRGEDK FVRVSWDKAL ELVAKELTRM YDTYGPSSVY
GSSYGWKSTG SVNDPCALQY RLLNFMGGFT AKRNSYSSAA VNTILPYVVG SGNPRCTAWD
DVIDHSERIV FWGCNPLVTN DIDWYTTLHN YAGYMRALKK KGTKTYSVNP IYNDTAEYMK
SEWVAVNPGT DTAVMAAMIY ELEVTGEADH AFLDKYTAGW KEFRAYLMGD EDGVKKTPEW
AAKISGIKAE TIKALAHDLK AHRTMLMIGW GIQRIDYGEQ FHWMLVTLAA ALGQIGLPGG
GFGTSYHYSS GGAPLANGPF VGGIPSKVAP VRPVKPWQGS KVLHVAAITD ALEHPGAVRD
FDGKKETYPH FRMIMWAGGN PFAHHPDTFR LERAWKKPDT VVVTDVVWTA TARHADIVLP
ACTFLEHNDI SVIGTNSCDG VVAMHQAIKP QYESRSDYWI YSQLAKKLGF EKEFTEGRTE
MQWIEKIYND ARGMSDVYDI TMPDFKTFWE KGFHLYDVPE EARRYVSFAE FRADPQANKL
NTESGLIQLY SPKIAGYKYD DCRGHAMYFK PAEGTASATK DFPLALMAPK GRYRMHSQLD
CVNNRQRGKI EDREPVWINP KDAASRKIVS GDVVLVKSRR GAMLAGAIVT ERVKPGVIVV
QHGAWFDPRK TPKGRIDVEG NSNSLTIDKP TSKLARGNVS STGNVEVTKW TDELPPVTVF
VQPRRKL
//
