ID   A0A1L7D6F5_9CORY        Unreviewed;       877 AA.
AC   A0A1L7D6F5;
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 {ECO:0000313|EMBL:APT93746.1};
GN   ORFNames=CPHO_07980 {ECO:0000313|EMBL:APT93746.1};
OS   Corynebacterium phocae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161895 {ECO:0000313|EMBL:APT93746.1, ECO:0000313|Proteomes:UP000185491};
RN   [1] {ECO:0000313|EMBL:APT93746.1, ECO:0000313|Proteomes:UP000185491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M408/89/1 {ECO:0000313|EMBL:APT93746.1,
RC   ECO:0000313|Proteomes:UP000185491};
RA   Ruckert C., Albersmeier A., Winkler A., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium phocae M408/89/1(T)(=DSM
RT   44612(T)), isolated from the common seal (Phoca vitulina).";
RL   Submitted (AUG-2014) 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}.
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DR   EMBL; CP009249; APT93746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L7D6F5; -.
DR   STRING; 161895.CPHO_07980; -.
DR   KEGG; cpho:CPHO_07980; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000185491; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
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:UP000185491}.
FT   DOMAIN          2..368
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          681..752
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          632..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          841..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        645..661
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   877 AA;  97796 MW;  2DCECB0EA8E82521 CRC64;
     MANADLIVIQ GSNMAECHPV GFQWVVEAKK RGARIIHVDP RYTRTSASAN RHIAIRGGTD
     IVLFGALIKY MIDNDLYFHD YVVNYTNAAH IISPDFRDAE DLGGLFSGYN PETGKYVTDS
     WQFVQKPEGS SWNVEKDPTL QDPNCVFQVL RRHYSRYTPE MVEEMCGISQ EDFEYLARSV
     AENSNPERTT CFAYALGFTQ HTMGVQFIRS LAILQLLMGN IGRPGSGIMA LRGHASIQGS
     TDIPTLFNSL PGYLPMPHVL TQTWKEYLDS FRKEDQKGFW QIGEAYAVSL MKAYFGDAAQ
     PVNNWGLDLM PRINGSHSTY ETLLGMLEGD VEGYIVFGQN PAVAQSNGGM QRRGLAALKW
     LVVRDFQEIE TASFWYDSPE VRSGELKTED IGTEVFLMPA ATHVEKAGTF TQTQRMLQWR
     FQALNPPEDA TSEAWFFYEL GKRIKARLAD SDDPRDKPIQ AMTWDYAVDE HGDPDSEDIL
     REINGYHLEG PKKGQLLSSF TEMKADGSTM GGCWIYTGVF AGGINHAATK KPGSADEWGW
     VWPANRRILY NRASAKPDGT PWSERKKYIW WDAEAGRWTG QDVPDFPVTK APDYRAKVDA
     VGPDSLDGID PFIMQSDGKG WLYAPAGLSD GPLPTHYEPH ESPVENQLYK QQQSPTRLSI
     KRPDNLSAPA PGEPGADVYP FTFSTYRLTE MYTSGAMSRR LPFLAELQPG LFCEVSRELA
     QLRGLENGQW ATIISPRGVI EAQVLVSGRI EKLTINGKDF HQIGIPYHYG ESETAPVAGD
     GVNDLLGLTL EPNVFIQNSK VSACDIIPGR RPRGQARLEL MREYQRRAQL TLDSGNKLLD
     VDDSFTLAPE PGESGQDNTG QDNTAGNVAD YEGKEGQ
//