ID   A0A4R0YK60_9GAMM        Unreviewed;       810 AA.
AC   A0A4R0YK60;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=Formate dehydrogenase-N subunit alpha {ECO:0000313|EMBL:TCI08838.1};
GN   Name=fdnG {ECO:0000313|EMBL:TCI08838.1};
GN   ORFNames=EZM97_21540 {ECO:0000313|EMBL:TCI08838.1};
OS   Dyella soli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Dyella.
OX   NCBI_TaxID=522319 {ECO:0000313|EMBL:TCI08838.1, ECO:0000313|Proteomes:UP000291822};
RN   [1] {ECO:0000313|EMBL:TCI08838.1, ECO:0000313|Proteomes:UP000291822}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KACC 12747 {ECO:0000313|EMBL:TCI08838.1,
RC   ECO:0000313|Proteomes:UP000291822};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Dyella amyloliquefaciens sp. nov., isolated from forest soil.";
RL   Submitted (FEB-2019) 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:TCI08838.1}.
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DR   EMBL; SJTG01000003; TCI08838.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R0YK60; -.
DR   Proteomes; UP000291822; 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:UP000291822}.
FT   DOMAIN          1..374
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          680..797
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   810 AA;  90289 MW;  C02BCA0FEC091693 CRC64;
     MTNTWQDIKN ANVVIVMGGN AAEAHPCGFK WVIEAKIENG AKLVVVDPRF TRTASVADYY
     APIRPGTDIA FLNGVIHYLL EKDAIQHQYV RAYTNASLIV KDSFSFQDGL FSGYNEETHS
     YDRSSWDYEL DQDGFARSDD TWQDPHCVIN LLKQHVSRYT PEMVSRICGT PQDKFLHVCE
     LIASTAAPDK AMTSLFALGW TQHSVGAQNI RNMAMVQLLL GNIGVAGGGM NALRGHSNIQ
     GLTDVGLLSN QMPGYLNLPT EKEPSFDIYM STRQFKPLRP GQISYYQNTR KFVVSLMKAL
     YGDAATAENN WAYDWLPKLD IPLYDIIKAF EMMNNDQITG YFCQGFNPLQ AFPDRGKIRR
     GLSKLKFLVT MDPLDTETSR FWQDFGPQNP AKSAEIQTEV FQLPTTCFAE ENGSLVNSAR
     WLQWHWKAAD GPGQAMSDIW IMSGIFHRLR ELYRKEGGAF PDPILNLTWK YTDPTSPDPE
     DLAKEMNGRA LADLTDPVTG VVTKAGTLLD GFAQLRDDGT TSSGCWIFSG SFTEKGNQMA
     RRDATDPREQ GIAPNWAWAW PANRRILYNR ASADPDGKPW NPAKPVISWN GTRWVGIDVP
     DYTPTLNPAA GASPFIMNDE GLGRLFARKL MAEGPFPEHY EPLESPVENV LHPKVKNNPA
     ARVFANDRAA FGSPKDFPYV ATTYRLTEHF HFWTKHALIN AILQPEEFVE VGEVLAKEKG
     IEQGGWVKVS SKRGEVICKA YVTKRIKPLT VDGKPTHVIG VPLHWGFTGQ ARKGYGANTL
     TPSVGDANTQ TPEFKAFLVN IEKASPPVAA
//