ID A0A1I3T3Z5_9PSEU Unreviewed; 759 AA.
AC A0A1I3T3Z5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Biotin/methionine sulfoxide reductase {ECO:0000313|EMBL:SFJ65774.1};
GN ORFNames=SAMN05421835_107132 {ECO:0000313|EMBL:SFJ65774.1};
OS Amycolatopsis sacchari.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=115433 {ECO:0000313|EMBL:SFJ65774.1, ECO:0000313|Proteomes:UP000199025};
RN [1] {ECO:0000313|EMBL:SFJ65774.1, ECO:0000313|Proteomes:UP000199025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44468 {ECO:0000313|EMBL:SFJ65774.1,
RC ECO:0000313|Proteomes:UP000199025};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FORP01000007; SFJ65774.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3T3Z5; -.
DR STRING; 115433.SAMN05421835_107132; -.
DR OrthoDB; 7376058at2; -.
DR Proteomes; UP000199025; 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 InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199025}.
FT DOMAIN 10..48
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 53..508
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 618..729
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 759 AA; 82677 MW; FDFB36FC8BD603D9 CRC64;
MPEPAAFRSH SSHWGAFDAA LTPAGLAVRP DAGDPAPAAL LRNVPAALDE RLRVLAPYAR
RGWLERGPGP DPARGRDEYV RISWAEALDR AAAELDRVRT RYGNTAIFGG SYGWGSAGRF
HHAQSQLHRF LAVAGGYVRS VNTYSSGAAE VLLPHVVGDH APIERPTTWA VLAEHTGHFV
CFGGLPDKNA QVNAGGVTRH GMAEELRRAK RRGARFTLVS PLRDDLADDL GADWLPLAPG
TDTALMLALC FTLVERGLHD EEFLHTHCEG FPELWRYLSG SVDGVPKSPQ WAEARCGIPA
GKIVELAESM AAHRTMITVS WSLQRSRHGE QPLWAGVALA CVLGQIGLPG GGFGHGYASM
AGIGAGSLPF PLPTLRRGLN PVREFIPVAR VADMLLHPGE EYDYNGQRLR YPDIRLVHWA
GGNPFHHHQD LARLGRAFTR PDTVLVHEQF WTATARHADL VLPVTTTLER EDLGAARQDA
ALVAMARVSP PLGEAKSDFE ILSGLAKRLG VEHEFTEGRD ERQWLEWLYE SWRAKLPPEA
DPGLDFAEFW RKGRIELREA RPEHVLYADF RADPHRHRLP TPSGRIELFS RRIASFGYDD
CPGHPTWFEP EEEPGFPLTL VANNPATRLH SQLDHGAESA GAKVAGREPV RMHPGDAAAR
GLSTGDVVLV RSPRGSALAG LVVSDAVRPG VVQLSTGAWF DPTAPEVATC VHGNPNALTR
DVGSSRLAQG CTGQLTRVEV VAFRGEVPPV RAHEPPVPG
//
