ID   A0A075JFH6_9MICO        Unreviewed;       878 AA.
AC   A0A075JFH6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:AIF40042.1};
GN   ORFNames=HX89_02640 {ECO:0000313|EMBL:AIF40042.1};
OS   Dermacoccus nishinomiyaensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermacoccaceae;
OC   Dermacoccus.
OX   NCBI_TaxID=1274 {ECO:0000313|EMBL:AIF40042.1, ECO:0000313|Proteomes:UP000027986};
RN   [1] {ECO:0000313|EMBL:AIF40042.1, ECO:0000313|Proteomes:UP000027986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M25 {ECO:0000313|EMBL:AIF40042.1,
RC   ECO:0000313|Proteomes:UP000027986};
RA   Hong K.W., Chan K.G.;
RT   "Genome Sequencing of Dermacoccus nishinomiyaensis.";
RL   Submitted (JUL-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; CP008889; AIF40042.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A075JFH6; -.
DR   KEGG; dni:HX89_02640; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_1_2_11; -.
DR   OrthoDB; 9759518at2; -.
DR   Proteomes; UP000027986; 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   CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 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; 2.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR048158; Formate_DH_Act.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   NCBIfam; NF041513; formate_DH_Act; 1.
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; 2.
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:UP000027986}.
FT   DOMAIN          2..405
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          431..473
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          720..831
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          108..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   878 AA;  96886 MW;  359EBEE3DE4737AB CRC64;
     MANADLILIE GSNMAECHPV GFQWVTEAKA RGAKVIHIDP RFTRTSAVAD KHIPIRGGSD
     IVFLGALINH VLTAESYFRD YVVAYTNAAT IVSDDFVDTE ELDGLFSGYD PSTGQYDQSS
     WQYKTPPGKP DQGTSSDEKS GSSGHQASGG AETHGSGGPT LAHSAVLRDE TLTDPMCVLQ
     IMKRHYARYT PEMVEEVCGV SKEDFALVAR EVVANSGRER TTMFAYAVGW TQHVGGAQMI
     RTAAILQLLM GNVGRPGAGI MALRGHATIQ GSTDIPTLFN LLPGYLPMPR VSDHETLEDY
     IDSIVSKDAK GYWANADKYA VSLFKAWYGE KATSANNFGL DYMPRLSGAH GTYQTVMGMI
     ENQVEGYFVL GQNPAVGSAN ARMQREGLRH LKWLVVRDFQ LIETATFWKD APEIASGEWR
     SEDIDTEVFF FPAATHVEKA GTFTQTQRLV QWRHKAVNPP GDAQSELDFF HEVGVRIRAR
     LADSSDPIDE PLKAITWDYP KDEHGEVIAE SVMAEINGTD AEGKPLATYA DLKADGSTTS
     GCWIYAGIYK DGVNQAARRK PGYEQDETAA EWAWAWPANR RTLYNRASAD REGKPWSERK
     KLIWWDEEKG QWVGKDNPDF PLKTAPSYRP KEGVGGPDGL AGDDPFIMMA DGKGWLYAPL
     GLVDGPMPTH YEAAESPMRN PLYSQQSNPT RVTFRRKDNL NAPSEGMPGG DVYPYVFQIG
     RLTEHHTAGG MSRWLPYLSE LQPSMFIEVS PDLAAEKGLE NGDWATVVSA RAAIEARVLV
     TDRMVPLKIG GRMVHQIGMP YHWGSAKSAE VHGDSANDLL GVVLDRNTQI QEGKMGMCDI
     RPGRRPQDRD EYEQLVSEYQ SRAGVTVETG NEICQECD
//