ID A0A0F2T7E1_STRR3 Unreviewed; 761 AA.
AC A0A0F2T7E1;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=VM95_34525 {ECO:0000313|EMBL:KJS58245.1};
OS Streptomyces rubellomurinus (strain ATCC 31215).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=359131 {ECO:0000313|EMBL:KJS58245.1, ECO:0000313|Proteomes:UP000033699};
RN [1] {ECO:0000313|EMBL:KJS58245.1, ECO:0000313|Proteomes:UP000033699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31215 {ECO:0000313|EMBL:KJS58245.1,
RC ECO:0000313|Proteomes:UP000033699};
RA Ju K.-S., Doroghazi J.R., Metcalf W.;
RL Submitted (FEB-2015) 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:KJS58245.1}.
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DR EMBL; JZKH01000126; KJS58245.1; -; Genomic_DNA.
DR RefSeq; WP_045704540.1; NZ_JZKH01000126.1.
DR AlphaFoldDB; A0A0F2T7E1; -.
DR PATRIC; fig|359131.3.peg.1316; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000033699; 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:UP000033699}.
FT DOMAIN 120..488
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 642..749
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 82510 MW; 2D19D395328CACB8 CRC64;
MAKQAPQSDP AQDAPEVSAP KHSAVGLPAV GHTVRMAAEQ MGARRAVSTL LKVNQHTGFD
CPGCAWPEPD KPHAVEFCEN GAKAVAEEAT ERRIRAEFFA AHPVAELAER SGYWLGQQGR
LTQPMLLDEG ATHYTPVSWD DAFALIAEEL RALDTPDAAA FYTSGRTSNE AAFAYQLFAR
RLGTNNLPDC SNMCHESSGS ALTETLGVGK GSVSLQDLYQ ADLIIVAGQN PGTNHPRMLA
ALERAKRAGA TIVSVNPLPE AGLERFKNPQ NVRGVVGNGT KLTDLFLQIR LGGDLALFRA
VNRMILEQDG VDRAFVAEHC HGFEEFEAQA LKTDRDEVLA ATGLPWEQIE ELGRLVLASR
KVIVCWAMGL TQHKHSVPTI REVVNFLLLR GNVGRPGAGV CPVRGHSNVQ GDRTMGIFER
PSAAFLDALG AEFDFEPPRE HGHDAVDTIR AMRDGRVKVF LAMGGNFVAA TPDTEVTEAA
MRRCRLTVHV STKLNRSHLV TGARALILPT LGRTDRDTTA AGDQFVSVED SMGQVHASRG
RLRPPADDLL SETAIVCRVA QAVFGPEDSV PWAEFAADYD TLRDRIARVV PGFEDYNTKL
HRPGGFTLPH GPRDSRTFPT ATGKANFTVN PLTAPEVPPG RLLLQTLRSH DQYNTTIYGL
DDRYRGIKGG RRVVLVNPAD AAELGLTEGG YTDLVSEWTD GSERRAPHFR VVHYPVARGG
AAAYYPETNV LVPLDSTADI SNTPTSKAVV VRFEPDSGPV A
//
