ID A0A316A9B3_9ACTN Unreviewed; 810 AA.
AC A0A316A9B3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:PWJ54102.1};
GN ORFNames=BXY45_1089 {ECO:0000313|EMBL:PWJ54102.1};
OS Quadrisphaera granulorum.
OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae;
OC Quadrisphaera.
OX NCBI_TaxID=317664 {ECO:0000313|EMBL:PWJ54102.1, ECO:0000313|Proteomes:UP000245469};
RN [1] {ECO:0000313|EMBL:PWJ54102.1, ECO:0000313|Proteomes:UP000245469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44889 {ECO:0000313|EMBL:PWJ54102.1,
RC ECO:0000313|Proteomes:UP000245469};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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:PWJ54102.1}.
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DR EMBL; QGDQ01000008; PWJ54102.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316A9B3; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000245469; Unassembled WGS sequence.
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 CDD; cd02787; MopB_CT_ydeP; 1.
DR CDD; cd02767; MopB_ydeP; 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:UP000245469}.
FT DOMAIN 137..510
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 666..773
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 784..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 88457 MW; B8C9DC94CF090574 CRC64;
MGWHDAVKLP WPTIPVRTGA PTDDVDDDAL RVTHPHDHAA GATAVAVALR HGVEQMGPLR
TAQTLLRLNQ VDGFDCQGCA WPDPDPKHRH TAEFCENGAK AVAEEATRRR ITRDFWARHT
LDDLAGRTDY WLGQQGRLTE PVVRRPGSDH YEPISYDDAF ELIGEQLRSL PTPDAAAFYT
SGRTSNEAAF AYQLFVRAYG TNNLPDCSNM CHESTSVALA QTIGIGKGSV HLEDFYDTDL
IIVAGQNPGT NHPRMLSALE TAKKNGAKII SVNPLPEAGL MGFKNPQTPK GMLIGERLSD
LHLPIRANGD LALFQWFGRA VVEAGRLDRA LIAERTTGFE AWEEHVRRVD RDEVLAATGL
TSAQLDEATA LVVASPRFIT CWAMGITQHK NAVSTIKEIT NLHLATGAIG VQGSGLCPVR
GHSNVQGDRT MGIWERPPQH FLDRLRDEFG FEPPREHGHD VVDTIRGMRD GHVRFFLGMG
GNFLQASPDT EATERALRNT AMTVQVSTKL NRSHAVVGET AIVLPTLGRT ERDVRGRGPQ
TREQFVTVED SMSMVHASRG RLAPPAPGVL SEVSIVAGIA AATLRDRTDA TGSIDWAGFA
QDYSTVRHHI AKVVPGCDDY DAKVRAPGGF QLPHPPRDTR TFDLPDGRAV FTVVPLDVLT
VGEDELVLQT MRSHDQYNTT IYGLDDRYRG IHQGRRVVFL NADDARDRGL ADGDHVDLVG
VWEDDVERVA PSFRVVVYDT PRGCAAAYYP ETNALVPLDS QAEHSGTPTS KGVIITLRRA
TAVSDGSAGS GSGASVGRHH KDEVQPHHLS
//
