ID A0A1I2N982_9FIRM Unreviewed; 527 AA.
AC A0A1I2N982;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SFG00113.1};
GN ORFNames=SAMN05660649_00424 {ECO:0000313|EMBL:SFG00113.1};
OS Desulfotruncus arcticus DSM 17038.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfallaceae;
OC Desulfotruncus.
OX NCBI_TaxID=1121424 {ECO:0000313|EMBL:SFG00113.1, ECO:0000313|Proteomes:UP000199337};
RN [1] {ECO:0000313|Proteomes:UP000199337}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17038 {ECO:0000313|Proteomes:UP000199337};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FOOX01000001; SFG00113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2N982; -.
DR STRING; 341036.SAMN05660649_00424; -.
DR Proteomes; UP000199337; Unassembled WGS sequence.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd02790; MopB_CT_Formate-Dh_H; 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; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041925; CT_Formate-Dh_H.
DR InterPro; IPR006478; Formate_DH_asu.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE 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.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199337}.
FT DOMAIN 1..331
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 414..520
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 527 AA; 57649 MW; 5EED2599186B104D CRC64;
MTNSIKEISG ADFILAIGTN TTESHPIISL QVKKAQRSGA TLVVADPRRT EIAELSNIHM
QLKSGSDIAL LNAMANVIIT EKIWNKEFVS TRTEDFEALK ETVAKYTPDY AEDITGIPAD
VIREAARGYA KANNATILYT MGITQHICGT HNVFAVANLA MLCGQIGKPS SGVNPLRGQN
NVQGACDMGA LPNVYTGYQA VTVDDNRSKF AKAWNVNQMP AKPGLTVGEM MEAAAEGQVK
GMYIMGENPV LSDPDARHVE HALEKLDFLV VQDIFLTETA ALADVVLPAA SFAEKDGTFS
NTERRVQRVR KAIDPVGNAR ADWQIICDVA TAMGYPMNYA FASEVFDEIA SVTPSYAGIS
YERLEQGGIQ WPCPNSEHDG TMYLHQDKFV RGLGKFNPVE YIPPAEQPDS EFPFVLSTGR
RHFHYHTGTM TQRTGALEVH YGTEYLEINP ADAAAINITE GEMIKVQSRR GEVMVQARLT
DIVPKGMVFT SFHFPEVAIN KLTNSARDPV AKIPELKVCA VTIKKAS
//