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Database: UniProt
Entry: A0A238LFB2_9RHOB
LinkDB: A0A238LFB2_9RHOB
Original site: A0A238LFB2_9RHOB 
ID   A0A238LFB2_9RHOB        Unreviewed;       758 AA.
AC   A0A238LFB2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Dimethyl sulfoxide/trimethylamine N-oxide reductase {ECO:0000313|EMBL:SMY08094.1};
DE            EC=1.7.2.3 {ECO:0000313|EMBL:SMY08094.1};
GN   Name=dorA {ECO:0000313|EMBL:SMY08094.1};
GN   ORFNames=LOM8899_02242 {ECO:0000313|EMBL:SMY08094.1};
OS   Flavimaricola marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Flavimaricola.
OX   NCBI_TaxID=1819565 {ECO:0000313|EMBL:SMY08094.1, ECO:0000313|Proteomes:UP000201613};
RN   [1] {ECO:0000313|EMBL:SMY08094.1, ECO:0000313|Proteomes:UP000201613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8899 {ECO:0000313|EMBL:SMY08094.1,
RC   ECO:0000313|Proteomes:UP000201613};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR   EMBL; FXZK01000004; SMY08094.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A238LFB2; -.
DR   Proteomes; UP000201613; Unassembled WGS sequence.
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; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
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; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000313|EMBL:SMY08094.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000201613}.
FT   DOMAIN          50..502
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          616..734
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   758 AA;  82761 MW;  3C0880AF2C19FA98 CRC64;
     MGQKYTAAHW GSYRLAGEGE DLSLTPVDTD LNPSRIGRGW VSAMRNSDAR IARPSIREGW
     LKHRDHDRSG DAVFREVPWD EALDMLAEEL RRVIDTHGNE AIYAGSYGWA SAGRFHHAQS
     QLRRFLNGIG GYVSSRDTYS HAAAEVLFPF VVGMSLNAVQ DQTTSWSSVA EHCELFVAFG
     GVSARTAQVS SAGTTTHEVE TWMGRARANG MACVNVSPLA TDLPGAEWLA IRPGTDTALI
     LALAHEIFAA GLADRDFLAR YTHGADRFET YVMGTDDGLP KTAEWAAQIC DVSAEAIRAL
     AARMAKSRTM IAVTWSLQRA DHGEQAMWAA LALAAMLGQI GQPGTGYGFG YGCTTPVGRP
     ARLVPWPSVP QGQNRVTDFI PVARVADMLE APGAPYTYAG TDRTYPDARL VWWAGGNPFH
     HHQDLQRLDA AWRRPETVVV MDHSWTATAR RADFVLPTTS PLERDDLMLN RRDAGLIYMS
     AAMPQFAEAR DDYAILAGLA ERMGTADAFT KGRSVDEWLR HLWERCAPVA KVAGLDLPAF
     DDFRREGMIR VPDEEQAKVL FADFVADPEA HPLPTESGKI DIFSPKIADA DLPDCPAHPT
     WLEPVEWLGA AAEDELHLLS IQPDTRLHAQ LDQGSEALAS KIEGREVCTM HPDAAAARGL
     TAGDIVLLEN ARGACLAGLA LSDQMRPDCV ILPTGAWLDL QEIDGRMICV SGNVNVLTID
     KGTSGLGQGN IAHTALVRVR KWDKPLPELR VTKPPRFA
//
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