ID A0A2Z6I922_9BURK Unreviewed; 733 AA.
AC A0A2Z6I922;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:BBF22975.1};
GN ORFNames=SUTMEG_08660 {ECO:0000313|EMBL:BBF22975.1};
OS Sutterella megalosphaeroides.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF22975.1, ECO:0000313|Proteomes:UP000271003};
RN [1] {ECO:0000313|EMBL:BBF22975.1, ECO:0000313|Proteomes:UP000271003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF22975.1,
RC ECO:0000313|Proteomes:UP000271003};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; AP018786; BBF22975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6I922; -.
DR KEGG; sutt:SUTMEG_08660; -.
DR OrthoDB; 9796486at2; -.
DR Proteomes; UP000271003; Chromosome.
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 CDD; cd02775; MopB_CT; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 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:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000271003};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..733
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016300757"
FT DOMAIN 94..514
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 620..723
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 733 AA; 82217 MW; FCCF981D3721C701 CRC64;
MTVHLTRRAL FESAALAALA PSASPVFAAT DPKADDEWTG YTFCDSCNHG PHCGIKFHAR
GNTCHRIENW AENPNHFLCS KGWATLQRLY NPNRLLYPMK RTNPKGSKDP GWVRISWDEA
YRTIASKMIA TREKYGADSV MFYAGDPKEP RAPIQRLARY FGSSTWCTES SAACRSGCLL
GETLDFGVEN IGSAPGPKTK VFMICATNCW SKPIGWWNMV LAAKARGVKI ITVDPRRTKA
AEIADVHLQL KVGTDAALAA GITHVLIKEN LYDRAFVEKW THGFEAYAKY CEAFTPEKTA
EITGVPAEKI VEAARLWAQG PGVYISTPQS LSHNSNGVQN TRALLMLIAT MGYVDVEGGL
PFPILPKGLL LHAFGLHEDM IDPAWWNDPE RRRARLDSKA VPVWNYMMDQ CSPNDFPEWV
EEGKVKMFCG WGFNVNIWPQ PETYRKAFEK LDFGFAADYF YRPASHDALD IILPAAINYE
RYAPFGAYGA RVAARRPLKP LGEAKEDWRI ALELGCIVDK PENFFEGDPV KCLDWILRKF
DGCSWEKFET MLPKVGDLPS GVKGFKKYET GAMRPDGKPG FNTPSGKIEY ESEILRKFGV
DPLPTYKPMM PLTEEFPLRF INGTRKPYIT HSKTRRDQPY LMEIEDRLTI DINPKDAEAR
GIREGDDVLL TSAFGGPVRA RATVTILVPA GTIGGQYGWL GDMNTQTLMT REHRDPITGY
PCYFEVPVNV KKA
//
