ID G2I2C8_KOMMN Unreviewed; 767 AA.
AC G2I2C8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Formate dehydrogenase alpha subunit {ECO:0000313|EMBL:BAK82544.1};
GN OrderedLocusNames=GLX_01320 {ECO:0000313|EMBL:BAK82544.1};
OS Komagataeibacter medellinensis (strain NBRC 3288 / BCRC 11682 / LMG 1693 /
OS Kondo 51) (Gluconacetobacter medellinensis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Komagataeibacter.
OX NCBI_TaxID=634177 {ECO:0000313|EMBL:BAK82544.1, ECO:0000313|Proteomes:UP000009044};
RN [1] {ECO:0000313|Proteomes:UP000009044}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 3288 / BCRC 11682 / LMG 1693
RC {ECO:0000313|Proteomes:UP000009044};
RX PubMed=22123756; DOI=10.1128/JB.06158-11;
RA Ogino H., Azuma Y., Hosoyama A., Nakazawa H., Matsutani M., Hasegawa A.,
RA Otsuyama K., Matsushita K., Fujita N., Shirai M.;
RT "Complete genome sequence of NBRC 3288, a unique cellulose-nonproducing
RT strain of Gluconacetobacter xylinus isolated from vinegar.";
RL J. Bacteriol. 193:6997-6998(2011).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
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}.
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DR EMBL; AP012159; BAK82544.1; -; Genomic_DNA.
DR RefSeq; WP_014104133.1; NC_016027.1.
DR AlphaFoldDB; G2I2C8; -.
DR STRING; 634177.GLX_01320; -.
DR KEGG; gxy:GLX_01320; -.
DR PATRIC; fig|634177.7.peg.134; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_16_1_5; -.
DR Proteomes; UP000009044; Chromosome.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR037951; MopB_CT_YdeP.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR010046; Mopterin_OxRdtse_a_bac.
DR InterPro; IPR041953; YdeP_MopB.
DR NCBIfam; TIGR01701; Fdhalpha-like; 1.
DR PANTHER; PTHR43105:SF4; PROTEIN YDEP; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 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:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 112..486
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 642..749
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 767 AA; 84818 MW; 72A1DD7CAABD56AA CRC64;
MSNEKTPEYK PYHHPAGGWG AAGATAKVLM EQSVLVKGSR GLLSMNQPGG FKCPSCAFPD
PDHRKTLEFC ENGAKALAHE ATKGRVTREF FEKYTVTELM QKSDYWLEMQ GRLTEPMRYD
AQSDRYVPVA WDDAFALIGQ HLRALDSPHQ AEFYTSGRTA NETAFLYSIF VREFGTNNFP
DCSNMCHEPT SRGLPPAIGI GKGTIVMGDF EHAEAIFVVG QNTGTNSPRM MTNLVEARKR
GVPIVLINPM PERALIRFTE PQDMLQMGTF GSTPISSEFV HVRIGGDLAI FKGMMKALFE
AEARGETVLD LDFIHEHTAG LDAVRDDAIG CSWGEITQIS GITEAQIRKI ADIYMKSNAT
IICYGMGLTQ HQEGSRLIQQ VANLLLLRGN FGKPGAGIAP IRGHSNVQGD RTVGIDEKPT
DAYLDRVRDA FGFEPPREHG HHVLEAVEAM EAGTAKVFFG MGGNFIRAVP DTDRSYAAMR
NLNLTVGVAT KLNRGHLVHG KDALILPVVA RSEIIRTEAG EQFVTIEDAM ANVTASRGVF
EPVTGHVRPE TEIVCRMAMA TLPNSRTPWA DYMVDYTLIR DKIAEVYPEI YANFSERIKN
PHGFHLDIPP RRRVWNTPNG KANFLVLPGL EVNMPVKDAA MLRLATIRSH DQYNTTIYSN
SDRYRGVYNT RLVIFMNKDD MAERGLANGD VIGLETYSDD GIRRYVDGLH VLDYPMPRGA
IAGYYPELNP LLPLDYFDEI SGTPAAKSIP VKVVESVASA PPIQIAG
//