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Database: UniProt
Entry: A0A074TBC2_9RHOB
LinkDB: A0A074TBC2_9RHOB
Original site: A0A074TBC2_9RHOB 
ID   A0A074TBC2_9RHOB        Unreviewed;       759 AA.
AC   A0A074TBC2;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KEP69009.1};
GN   ORFNames=DL1_06040 {ECO:0000313|EMBL:KEP69009.1};
OS   Thioclava dalianensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thioclava.
OX   NCBI_TaxID=1185766 {ECO:0000313|EMBL:KEP69009.1, ECO:0000313|Proteomes:UP000027725};
RN   [1] {ECO:0000313|EMBL:KEP69009.1, ECO:0000313|Proteomes:UP000027725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DLFJ1-1 {ECO:0000313|EMBL:KEP69009.1,
RC   ECO:0000313|Proteomes:UP000027725};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Thioclava dalianensis DLFJ1-1.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KEP69009.1}.
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DR   EMBL; JHEH01000019; KEP69009.1; -; Genomic_DNA.
DR   RefSeq; WP_038067529.1; NZ_JHEH01000019.1.
DR   AlphaFoldDB; A0A074TBC2; -.
DR   STRING; 1185766.SAMN05216224_101741; -.
DR   eggNOG; COG0243; Bacteria.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000027725; Unassembled WGS sequence.
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; 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; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027725}.
FT   DOMAIN          110..491
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          645..752
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   759 AA;  84262 MW;  FCA87A8098626E17 CRC64;
     MSKTDDLPET SGPSGGWGSL KGITRIFGET WPSADAVRTL KRQNKPGGYM CASCAFPKPA
     NYHPFEFCEN GAKSTLWDMT RARCTPEFWE DHTVAGLRDW SDHELEKTGR LTAPMRYDPA
     RDRYVEVSWD DAFAEIGATL KDLPREQVVF YSSGHAGLEA SYLWALMARA YGNNNLPQSS
     NMCHETTSVG LKKVIGSSVG TVLWEDLEET DCYFFFGQNP GTNAPRFLHP LKEAKDRGAK
     IVTFNPVREQ GLISFVDPQN MHDMLTGSET KISDQYHQLK AGSDIAALTG LCKAVIEADE
     KAEAQGRAPI IDWAFLREHC NDYEGFLRFC RSTEWQALCD ECGLSETELR QAAEVYIKAE
     RVIGVYGMGL TQHAHGATNI GMLVNFLALR GNIGRKGAGC CPVRGHSNVQ GQRTVGIAEK
     TALIPMDRLR DLFGFEPPQK DGMHIVDAAQ AMLEGKVSAT LSMGGNLLRA LPDTDRIEAA
     WPQQKLTVMV STKLNRSHLY PGEVAYILPC LSRSEVDEQE TGNQYVSVED SFSMIHGSLG
     KHPPAAKTLK SELEITCRIA QAACAPNDKL CWLDWIKDYS VVRDLIEATY PDDFRDFNAR
     MNEPGGFWRG NAAHERVWKT ESGKLEFTTP DRLNALGFED APGRFRMITM RSNDQFNTTI
     YGYSDRFRGI EGTRDVLLMN KIDIADLGLK HGDEITVRGD MGDGVDRIKT GLSLCQFDMP
     RGTVGGYYPE CNVLIPVGLH DQLSKTPGSK GVPVRIEKA
//
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