ID   F7T0J5_9BURK            Unreviewed;       809 AA.
AC   F7T0J5;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   SubName: Full=Formate dehydrogenase-N subunit alpha {ECO:0000313|EMBL:EGP46284.1};
GN   ORFNames=AXXA_12285 {ECO:0000313|EMBL:EGP46284.1};
OS   Achromobacter insuavis AXX-A.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1003200 {ECO:0000313|EMBL:EGP46284.1, ECO:0000313|Proteomes:UP000004853};
RN   [1] {ECO:0000313|EMBL:EGP46284.1, ECO:0000313|Proteomes:UP000004853}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AXX-A {ECO:0000313|EMBL:EGP46284.1,
RC   ECO:0000313|Proteomes:UP000004853};
RA   Bador J., Amoureux L., Neuwirth C.;
RL   Submitted (JUN-2011) 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:EGP46284.1}.
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DR   EMBL; AFRQ01000042; EGP46284.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7T0J5; -.
DR   PATRIC; fig|1003200.3.peg.2437; -.
DR   eggNOG; COG0243; Bacteria.
DR   eggNOG; COG3383; Bacteria.
DR   HOGENOM; CLU_000422_1_2_4; -.
DR   Proteomes; UP000004853; 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}.
FT   DOMAIN          2..378
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          685..802
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   809 AA;  90563 MW;  FCAE8EEAA02304A8 CRC64;
     MTNHWVDIKN ADVVLIMGGN AAEAHPCGFK WVTEAKAHNK AKLIVVDPRF TRSASVADFY
     APIRTGTDII FLGGVIKYLL DHDKIQHEYV RNYTDFSYIV REDFTFDAGL YSGYNAEKRT
     YDKASWDYER GDDGFVKTDP TLEHPRSVYQ LLKKHYSRYT EEMVERVCGT PRDKFLKVCE
     MLASTATTNR AATILYALGW TQHSIGSQII RTGAMVQLLL GNIGIAGGGM NALRGHSNIQ
     GLTDLGLMSN LLPGYMTLPN EPEQDYGKYI ATRALKPLRP NQLSYWQNYS KFHVSLMKAW
     WGKAATAENN WAFDYLPKLD KLYDMLQVYE LMNQGKMNGY LAQGFNPLAA APNKAKLNAG
     FAKLKFLVIM DPLVTETSEF WRNAGEANDV DPKQIQTEVF RLPTTCFAEE DGALVNSGRW
     LQWHWKGAEP PGEAKSDIEI MSLIFTRLRK MYQEEGGKYP DPIVNLSWPY SNPQSPTAEE
     LAKEYSGKAL VDLVDPKDPT KVTRKGGEQL AGFAELRDDG STASGCWIFA GAWSPAGNLM
     ARRDNSDPTG IGQTLNWAWA WPANRRILYN RASCDVSGKP FDPRRNLISW NGKAWVGADI
     PDFKGDENPD GGMGPFIMNP EGVARFFARA GMAEGPFPEH YEPFETPLGY NPLYPKAKGV
     TSNPAARVFK DDLAAMGTVD KFPYVATTYR LTEHFHYWTK NVRINAILQP EQFVEISEVM
     AKELGIANGS RVKVSSNRGY IKAVALVTKR LRPLTIEGKT VYHVGIPIHW GFVGLAKPGF
     LTNTLTPFVG DGNSQTPEFK SFLVQVEKI
//