ID A0A085JME9_9GAMM Unreviewed; 771 AA.
AC A0A085JME9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Biotin sulfoxide reductase {ECO:0000313|EMBL:KFD21645.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:KFD21645.1};
DE EC=1.8.99.- {ECO:0000313|EMBL:KFD21645.1};
GN ORFNames=GTPT_0744 {ECO:0000313|EMBL:KFD21645.1};
OS Tatumella ptyseos ATCC 33301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD21645.1, ECO:0000313|Proteomes:UP000028602};
RN [1] {ECO:0000313|EMBL:KFD21645.1, ECO:0000313|Proteomes:UP000028602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD21645.1,
RC ECO:0000313|Proteomes:UP000028602};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFD21645.1}.
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DR EMBL; JMPR01000013; KFD21645.1; -; Genomic_DNA.
DR RefSeq; WP_029990694.1; NZ_JMPR01000013.1.
DR AlphaFoldDB; A0A085JME9; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000028602; 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; cd02793; MopB_CT_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; IPR041954; CT_DMSOR/BSOR/TMAOR.
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:KFD21645.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028602}.
FT DOMAIN 8..47
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 52..507
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 624..744
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 706..739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 771 AA; 85492 MW; 7681131CBED47FB2 CRC64;
MKTEQLLTST HWGTYEVETS GDKVTAMKPV PWDKNPSRIG QSMPDAITGN TRIRRPAVRL
GYLKHGPDSR EGRGKEPFVE VSWEEALSLV ARDLQSVKAR HGNEAIFGGS YGWGSAGRFH
HVQSQLHRFL KGFGGYTAST NTYSSAAGER ILPHIIGPLS PLHKKHTHFS VLAEHCEVFV
AIGGLPVRNS QVNVGGASDH MLKHWLETMQ GNGVKFINVS PVKNDLSAVS NAEWLPVRPG
TDTALLLALC QTLVSENLHD QAFIDSHTVG FGPLRRYLSG ETDGVVKNAA WAAPITGLST
EQITGLARTL ASHRSMVNIS WSIQRSRQGE QAYWATVALT ALLGQIGTPG GGLAFGYACT
NLAGADRVGF SGPRLPAGEN KVKTEIPVAR ISDLLLNPGG EYQFDGQDCR YPDIRLVYWA
GGNAFHHHQD LNRLVEAWRR PETVVVHEQY WTAQAKFSDI VLPATTVLER NDIGSGSHDG
FMVAMRQHIP PVSEARDDYE IFSGLAEQLG FAEQFTENRD PDQWLRHIYE ESRPRAEEDG
ITLPAFDDFW EQGKLEFERP SRPQIFLADF RADPEKHPLS TPSGKIELYS DTIAAFGYRE
CPGYPFWDPQ EEQFQQEQAQ TWPLHMLSSQ PRSRLHSQYD HGSFSRSTKV QGREPVWMHP
QDAAERGITE GSVVRVFNQR GAMLAGVHIS DQILAGVVQI STGAWYDPQD PSTPGSLDKH
GNPNVLTEDR GSSRLGQGCS AQSCKVEIER WEQPLPEITA FSPPPFCDRS E
//
