ID A0A0J9EAH0_9RHOB Unreviewed; 783 AA.
AC A0A0J9EAH0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Anaerobic dimethyl sulfoxide reductase chain A {ECO:0000313|EMBL:KMW58649.1};
DE EC=1.8.5.3 {ECO:0000313|EMBL:KMW58649.1};
GN ORFNames=AIOL_003627 {ECO:0000313|EMBL:KMW58649.1};
OS Candidatus Rhodobacter lobularis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW58649.1, ECO:0000313|Proteomes:UP000037178};
RN [1] {ECO:0000313|EMBL:KMW58649.1, ECO:0000313|Proteomes:UP000037178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGS {ECO:0000313|EMBL:KMW58649.1};
RA Jourda C., Santini S., Claverie J.-M.;
RT "Draft genome sequence of an Alphaproteobacteria species associated to the
RT Mediterranean sponge Oscarella lobularis.";
RL Submitted (JUN-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 -!- 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:KMW58649.1}.
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DR EMBL; LFTY01000002; KMW58649.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9EAH0; -.
DR STRING; 1675527.AIOL_003627; -.
DR PATRIC; fig|1675527.3.peg.3799; -.
DR Proteomes; UP000037178; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd02769; MopB_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; IPR041460; Molybdopterin_N.
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; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000313|EMBL:KMW58649.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037178}.
FT DOMAIN 25..63
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 69..525
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 640..757
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 652..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 86605 MW; 7A6548CFB11E6731 CRC64;
MSKSLQGFAT ESRTVMIKPD RDLLTSSHWG TYRVEVQDGR VTGMRPFERD PDPSPIGPAL
VDLLDDPMRI KAPMVRKSWL EGGPGTAGHM RGQEAFVQVT WEEANRLVAD ELQRVRREHG
NQAIYAGSYG WASAGRFHHA QSQLKRFLNC IGGYTSSRFT YSFAAAETIV PRILGTFRGF
LNNQTSWESI ATDCDLLVAF GGIPLKNGQI SQGGLGAHIQ RDGVLRAKAA GVEFVNISPL
RSDIDAAIGA EWLAPRPCTD VALILALCHT LLVEDLCDDE FLARYTVGME QFSAYLLGCS
DGVEKTPQWA AAITEIPAET ILELARRMAQ SRTMVSVAWA LTRQQHGEQP FWAVIALASM
LGQIGRPGTG FAFGYSAMNN TGLNRQQVNY ASLPQGKNPV AEFIPVARVT EMLERPGDAF
DFDGTRYTYP DIRVVWWAGG NPFHHHQDLN RFRRAWAKPD TVIANDWCWN SLTKHADIVL
PCTTTLERAD LALTPKDRHQ VVMDKAMEPV GQARDDHEIF RGIAARLGAE EAFTEGRSPE
EWLRWIYTVS RQRAAAEGVE MPDWDQFQRD GWMEVPAPPK LTVMMEAFIA DPDAHPLATP
SGRIEIFSET IAGFGYDDCP GHPAWMAPAE WLGAAAPDEL HLMSNQPHNK LHGQMDHGRV
SQADRPDGLE PALMNPRDAR TRDLSEGQPI RLHNARGACL ATLRLSEAIR PGVVQVATGA
WWDPDPDGDL CRHGNPNALT PDQGTSKLAQ GPAAHSCLVR VEAFEGRLPE RRAHQPPEIV
PRG
//
