ID   A0A239E922_9ACTN        Unreviewed;       839 AA.
AC   A0A239E922;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SNS40533.1};
GN   ORFNames=SAMN05216276_10095 {ECO:0000313|EMBL:SNS40533.1};
OS   Streptosporangium subroseum.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Streptosporangium.
OX   NCBI_TaxID=106412 {ECO:0000313|EMBL:SNS40533.1, ECO:0000313|Proteomes:UP000198282};
RN   [1] {ECO:0000313|EMBL:SNS40533.1, ECO:0000313|Proteomes:UP000198282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNS40533.1,
RC   ECO:0000313|Proteomes:UP000198282};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FZOD01000009; SNS40533.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239E922; -.
DR   Proteomes; UP000198282; 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: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; 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:UP000198282}.
FT   DOMAIN          14..384
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          414..458
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          694..806
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   REGION          120..158
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   839 AA;  92991 MW;  E7B99BDC5B229003 CRC64;
     MAECHPVGFQ WVVEARARGA KVFHIDPRFT RTSAIADRYI PIRAGSDIVL LGALVNHVLT
     HELDFREYVL AYTNASTIVS EDFQDTEDLD GLFSGFDPET RAYDPSSWAY EGTEEAAAGL
     RGEQLEGGRH HAEAAGAEQY GSGGAPAPSK SPTDPTLTHP RCVYQVLKRH FARYTPELVA
     ELCGISPEDF AELADAITAN SGRERTTAWA YAVGWTQHTV GAQYIRTASI LQLLLGNMGR
     PGGGILALRG HASIQGSTDI PTLFNILPGY LPMPHAHRHE GLDDYLSQAG PDTGFWGRKR
     SYTVSLLKAW WGDAATEEND FCFDYLPRLT GDHGHYTTVM GQIDGTVKGY FVVGENPAVG
     SSGGKAQRLG LANLDWLVVR DLTLVETATF WKDGPELQTG EMRTEDIATE VFFLPAASHV
     EKEGTFTNTQ RLLQWREKAL EPPGDCRSDL SFYYHLGKRI RQRVGDDEID RPLRELTWDY
     PEHGEQREPS GEAVLREING TGPDGRTLSA YTELKADGST RCGCWIYCGV YADEVNQAAR
     RKPGSEQTWV APEWGWAWPA NRRMLYNRAS ADPEGRPWSE RKAYIWWDAD KGEWTGHDVP
     DFEKNKPPDY LPPDGALAEA ALAGTDPFIM QPDGRGWLYA PAGLADGPMP AHYEPHESPV
     RNPLYGQQSN PAREIYPRAE SPYNPPESPR FPHVLTTYRL TEHHTAGAMS RPLAHLAELQ
     PALFCEVSPL LAAELGLVNG GWATIVTTRT AIEARVLVTD RVRPLRIQGR VIHQIGLPYH
     WGWGSGGLTT GDAVNDLLPI VLDPNVYIQE GKAVTCDLRP GRRPRGRALL DLIEEYRRG
//