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Database: UniProt
Entry: A0A0S8B6D2_9CHLR
LinkDB: A0A0S8B6D2_9CHLR
Original site: A0A0S8B6D2_9CHLR 
ID   A0A0S8B6D2_9CHLR        Unreviewed;       564 AA.
AC   A0A0S8B6D2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Formate dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AMJ56_13760 {ECO:0000313|EMBL:KPK07091.1};
OS   Anaerolineae bacterium SG8_19.
OC   Bacteria; Chloroflexota; Anaerolineae.
OX   NCBI_TaxID=1703386 {ECO:0000313|EMBL:KPK07091.1, ECO:0000313|Proteomes:UP000050892};
RN   [1] {ECO:0000313|EMBL:KPK07091.1, ECO:0000313|Proteomes:UP000050892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_19 {ECO:0000313|EMBL:KPK07091.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
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:KPK07091.1}.
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DR   EMBL; LJNN01000183; KPK07091.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8B6D2; -.
DR   Proteomes; UP000050892; Unassembled WGS sequence.
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: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; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
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.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          1..344
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          436..543
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   564 AA;  62429 MW;  799B255A5CBCA3C0 CRC64;
     MTNSISEIRD ADCIFITGSN TAESHPVISY EVVRAAKRGA HVIIVDPRRI PLVRQATLFL
     QVKPGTDIYV FLAMMHTIIR EGWADEAFIA ERTEGYEAFK AVVEEYTPER AALMSGVPAE
     QIELAARIYA FGERVDGPSV YEEDRGHSTI LYAMGITQRS NGTDMVMTLA NLAMLCGQVG
     QPSTGVNPLR GQANVQGACD LGCLVNVFPG YQRVTDDEKR LALAQAWEVE ELPGQVGLTI
     VEAMHAVAEG KIRAAYIMGE NPMMSDPNTS HVEQALRGLD FLVVQDIFPS ETAQLAHVIL
     PAASSLEKHG SFTNTERRVQ LIEPVLPAPG EARPDWQITA EIAARYDKKM GVDRQLDYWR
     YPSAAAIFEE LATVTPIYAG MSVDRLRGEG LQWPCPDAEH PGTSILHVGK FSRGLGKFNP
     VEAIDPAEQP DEEYPLILTT GRVLYHYHTG TMTRRSEPLD WIEPHGYVEV NAQDAAAVGV
     EDDGFVVVKS RRGQVNTRIK YSEGVSPGTV FLAFHWREAP ANMLTQDFKL DPVAKIPEYK
     VCAVRLENPP EKNLVSRRES EKVR
//
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