ID A0A0P1GTG8_9RHOB Unreviewed; 889 AA.
AC A0A0P1GTG8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN Name=dmsA {ECO:0000313|EMBL:CUH86138.1};
GN ORFNames=PH5382_00045 {ECO:0000313|EMBL:CUH86138.1};
OS Phaeobacter sp. CECT 5382.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1712645 {ECO:0000313|EMBL:CUH86138.1, ECO:0000313|Proteomes:UP000050782};
RN [1] {ECO:0000313|EMBL:CUH86138.1, ECO:0000313|Proteomes:UP000050782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 5382 {ECO:0000313|EMBL:CUH86138.1,
RC ECO:0000313|Proteomes:UP000050782};
RG Swine Surveillance;
RL Submitted (SEP-2015) 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 ---------------------------------------------------------------------------
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; CYSG01000001; CUH86138.1; -; Genomic_DNA.
DR RefSeq; WP_058332341.1; NZ_CYSG01000001.1.
DR AlphaFoldDB; A0A0P1GTG8; -.
DR STRING; 1712645.PH5382_00045; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000050782; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
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; 1.10.760.10; Cytochrome c-like domain; 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; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-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; SSF46626; Cytochrome c; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51007; CYTC; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00433}; Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:CUH86138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050782};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 826..889
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
SQ SEQUENCE 889 AA; 98593 MW; 459D34593E9CA3EA CRC64;
MTFANPTRRS FLQGGAAAFG ATTLMGSTAL AGIDPNSFAA RTFHASHFGP FEAVVRDGKI
VAINNMMELD ARPTEMLSYG IIDRTYDKSR IDYPMVRKSY LEGWQSGDVK PELRGKEEYV
RVDWDTAWSL TAKALLDTAT NHGNEAIFSS SYGGWSNAGV FRPNVLQGRL INLMGGCTNT
AGDWSAGASQ IALPHVIGDM EVYSTQSAWE TIRDETEVFV LVGCDPIKNN RIEYRVADHG
MYAHWEEIRD AGIKFISINP QRTASDEYLK ADWLKIIPNT DVALFNAMAY HVLEQGLDDK
EYMAKYTTGA DKWIAYVMGE TDGTPKTPAW AAAITGMDEA EIKALAELLA TSKTEIAGAW
SLQRAQHGEM THWAIVNFAA LTGKIGKPGQ GVGFSWHYGN GGMPASGKST PSGLSQGRNF
VKTICPASRI TEMLENPGLE MSYNGNKNVY PDVKMIFNAG NNFMSHQQDT NRLIRALEKV
ETIVSVDVWW TAATRWADIV MPAASTLEQD DITSGGTYSN DRVYAMKKVI EPIGDALPDY
EIFEGLADKL GLWAQFTDSE DKMYHIKMAY ERSTAAKTTP FEEFWEQGYA LMEVEDEARK
WTRHGAFYDD PDANPLHTTS GKIEMFCNTI ADMQIEDCPG MPVWMEKHEY LGNAKEGQLH
VVSPHPWYRL HSQMDQSSTL RGIYKVQGRE PVRINSQDAE KRGIADGDLV ELYNDRGAVL
AGAVVSDDIM PGVISIYEGC WPQVDSKGRC NSGLINFLTS TQRSSGLSQA TTANTTLVSI
KKCEDPDGPN LAYEKPAFID NMELTEIDED GLGLERLEAL TASLYADMTP GEKIYYERCT
VCHAPREVTH YTRQQWQGIT PSMFPRAGLD DEESALVLDY LMKNAADAN
//
