ID   A0A069PLE5_9BURK        Unreviewed;       809 AA.
AC   A0A069PLE5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KDR41523.1};
GN   ORFNames=BG61_16550 {ECO:0000313|EMBL:KDR41523.1};
OS   Caballeronia glathei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR41523.1, ECO:0000313|Proteomes:UP000027466};
RN   [1] {ECO:0000313|EMBL:KDR41523.1, ECO:0000313|Proteomes:UP000027466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR41523.1,
RC   ECO:0000313|Proteomes:UP000027466};
RA   Liu X.Y., Li C.X., Xu J.H.;
RT   "Draft Genome Sequences of Four Burkholderia Strains.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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:KDR41523.1}.
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DR   EMBL; JFHC01000026; KDR41523.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069PLE5; -.
DR   STRING; 60547.GCA_000751215_06392; -.
DR   Proteomes; UP000027466; Unassembled WGS sequence.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR   GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR   CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 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; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006443; Formate-DH-alph_fdnG.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   NCBIfam; TIGR01553; formate-DH-alph; 1.
DR   PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR   PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 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   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027466}.
FT   DOMAIN          2..377
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          687..802
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   809 AA;  90635 MW;  85749815789EAD7B CRC64;
     MTNHWVDIKN ADVILVMGGN AAEAHPCGFK WVTEAKAHRK ARLIVVDPRF TRTASVADFY
     APIRTGTDIV FLGGVINYLL THDKIQHEYV KNYTDFSFIV REDFAFNEGI YSGYNPEKRN
     YDKSTWDYER GDDGFAKVDP TLQHPRCVYN LMKQHYSRYT PEQVEKTCGT PKDKFLKVCE
     MLASTAVPGR AGTILYALGW THHSVGAQMI RTGAMVQLLL GNIGIAGGGM NALRGHSNIQ
     GLTDLGLMSN LLPGYMTLPM EGEQDYEAYI TKRAAQPLRP NQLSYWKNYR AFHVSFMKSW
     WGDNATAENN FGFDYLPKLD KSYDMLQVFE LMAQGKMNGY IAQGFNPLAA APNKAKISLG
     LSKLKWLVIM DPLATETSEF WKNFGEFNDV DPAKIQTEVF RLPTSCFAEE RGSLVSSSRV
     LQWHWQGAQP PGEARSDLEI MSGLWLRMRQ AYREKGGKYP DPILKMTWPY ADPESPTPEE
     IAMEFNGKAL ADVTDPVDKT RVIAKKGEQL ASFAQLRDDG STASGCWIFC GSWTQAGNQM
     GRRDNSDPTG IGQTLGWAWA WPANRRVLYN RASCDLAGKP FDPTRKLIAW NGKTWSGPDI
     PDFKADEPPE NGMNPFIMNA EGVARFFARD GMNEGPFPVH YEPFENPLGY NPLYPNTKEA
     VSNPAARVFP DDRAAFGTAK DFPHTATTYR LTEHFHYWTK HARMNAIIQP EQFVEIGEEL
     AKEVGVVAGD RVKVSSNRGH IVAVAVVTKR IRTLTIEGKK VQTVGLPLHW GFKGLTQPGY
     LVNTLTPSVG DGNSQTPEFK SFLVKVEKA
//