ID   A0A1M4XHD5_9FIRM        Unreviewed;       527 AA.
AC   A0A1M4XHD5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Formate dehydrogenase (NADP) alpha subunit {ECO:0000313|EMBL:SHE92811.1};
GN   ORFNames=SAMN02745218_01095 {ECO:0000313|EMBL:SHE92811.1};
OS   Desulfofundulus australicus DSM 11792.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulfofundulus.
OX   NCBI_TaxID=1121425 {ECO:0000313|EMBL:SHE92811.1, ECO:0000313|Proteomes:UP000184196};
RN   [1] {ECO:0000313|EMBL:SHE92811.1, ECO:0000313|Proteomes:UP000184196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11792 {ECO:0000313|EMBL:SHE92811.1,
RC   ECO:0000313|Proteomes:UP000184196};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FQUW01000011; SHE92811.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M4XHD5; -.
DR   Proteomes; UP000184196; 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:SF15; FORMATE DEHYDROGENASE H; 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.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027}.
FT   DOMAIN          1..330
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;  57294 MW;  78FBC2ABB286E60D CRC64;
     MTNPIGDIGG ADFILAIGTN TTESHPIIGL QVKKAVRNGA TLVVVDPRRT EVAGLAHYHL
     RLKSGTDIAL LNGLANVIIS EDLVNKEFVD TRTEGFEALK ETVARYTPEY VEQITGISAD
     IIREVARGYA TAKNATILYT MGLTQHVCGT HNVFAVANLA MLCGHIGKPH SGVNPLRGQN
     NVQGACDMGA LPNVLTGYQS VTLEEVRSKF AEAWGVGELP ATPGLTVGEM LEAAARGEIK
     GMYIMGENPV LSDPDADHVI HALEKLDFLV VQDIFLTETA RLADVVLPAA SFAEKDGTFT
     NTERRVQRVR KAIEPVGEAK PDWQIICLVA TAMGYPMQYG SPAEIMEEIA RLTPSYGGIS
     YQRLENGSLV WPCPAPDHPG TPILHAGKFA RGLGKFHPVE YVPPAEQPDE EYPLILNTGR
     RHFHYHTGTM TLRTGALEEY YGREHLEINP ADARALGIAD GERVRVVSRR GQVEVTARVV
     DTVPPGVVFT SFHFPDVAIN RLTNPARDPV ARIPELKVCA VRVEKIA
//