ID A0A327YGN9_9RHOB Unreviewed; 775 AA.
AC A0A327YGN9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE SubName: Full=Biotin/methionine sulfoxide reductase {ECO:0000313|EMBL:RAK20054.1};
GN ORFNames=ATI53_100753 {ECO:0000313|EMBL:RAK20054.1};
OS Salipiger aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Salipiger.
OX NCBI_TaxID=568098 {ECO:0000313|EMBL:RAK20054.1, ECO:0000313|Proteomes:UP000249165};
RN [1] {ECO:0000313|EMBL:RAK20054.1, ECO:0000313|Proteomes:UP000249165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22011 {ECO:0000313|EMBL:RAK20054.1,
RC ECO:0000313|Proteomes:UP000249165};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (JUN-2018) 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:RAK20054.1}.
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DR EMBL; QLMG01000007; RAK20054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327YGN9; -.
DR OrthoDB; 9759518at2; -.
DR Proteomes; UP000249165; 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:InterPro.
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 Reference proteome {ECO:0000313|Proteomes:UP000249165}.
FT DOMAIN 7..45
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 50..506
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 621..738
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 775 AA; 84426 MW; 79898A80C86226BE CRC64;
MTRKVIHSSH WGAYYARQGK DGLDITPHEG DRAPSEILQN MRGALDHPAR VLRPAVRQSW
LRRGPGPRDR AIGDPFVEVS WDTAASLLAD EVRRVRSAHG PEAVYGGSYG WASAGRFHHA
QSQVHRFLNT AFGGYVSGVA SYSAGASAPL LPRLIGNYTE ISRNTVSWKH IEAETELFLS
FGGLPPRNSA IGNGGVSDHI EHDMMRRIAA RGGVFHLVSP IRDDIPDDIG ATWHAIRPGT
DTALMLAMAY VLQDEGLADT AFLKDYCVGY ERFRSSLLGN ADGGPRTPVW AETITGIPAD
TIATLARDLV RKRTLISVAH ALQRAEFGEQ PVWAALALAA MVGQIGLKGR GFTYALGSLA
HTGRQRVSVP IPVLSQGINR CAAFIPVAAI SEMLLNPGAP FRFMGQKQTY PDIRLLWWAG
GNPFHHHQEL HRLSRAIGRV DTFVVQEQVW TATAKSADIV LPISFSLERD DFGATRNDPR
LFAMQRLCAP SGEARSDYDA LSAVAAALGP DEHAAFTEGR SAADWLRHLY EPTRVALEAM
GLDAPDFDRF WQDGWIDLPC HPDSGGFLEA FRNDPQEHPL GTPSGKIEIH SREIAGYGLD
DVPGLPVWRP HRRPPNADYP LFLIANAPES KLHSQLDFGP TSTAAKVAGR ERLRLNSVDA
ARLGLRDGDM ARVENECGAC LAGVQITDLV RDGVVHLQTG AWFDPQPDPE GAARVFCAHG
NANVLTHDKG TSQLTHGCSG QIGRVNVRKW TGPIPRLRAF DPPPFVSDSP EGSAS
//