ID A0A1Q5DMA6_9ACTN Unreviewed; 757 AA.
AC A0A1Q5DMA6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Molybdopterin oxidoreductase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMK18_25340 {ECO:0000313|EMBL:OKI96978.1};
OS Streptomyces sp. CB01249.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703929 {ECO:0000313|EMBL:OKI96978.1, ECO:0000313|Proteomes:UP000186839};
RN [1] {ECO:0000313|EMBL:OKI96978.1, ECO:0000313|Proteomes:UP000186839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01249 {ECO:0000313|EMBL:OKI96978.1,
RC ECO:0000313|Proteomes:UP000186839};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI96978.1}.
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DR EMBL; LISW01000006; OKI96978.1; -; Genomic_DNA.
DR RefSeq; WP_073864666.1; NZ_LISW01000006.1.
DR AlphaFoldDB; A0A1Q5DMA6; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000186839; 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:UP000186839}.
FT DOMAIN 122..489
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..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 757 AA; 81765 MW; D88BF054C727730F CRC64;
MASKPPAGDP VQDAPRVGPA QHSAAGLPAV AQSLRVAQQQ MGLRRTAQTL LKVNQKDGFD
CPGCAWPEGD KRHTAEFCEN GVKAVAEEAT LRRVTPDFFA EHPVSDLAGR SGYWLGQQGR
VTQPVHLPEG ADRYEAITWE RAFEIMAEEL GALASPDEAV FYTSGRTSNE AAFLLQLFAR
EFGTNNLPDC SNMCHESSGS ALTETIGVGK GSVSLEDLHH ADLIIIAGQN PGTNHPRMLS
ALGQAKAAGA KIISVNPLPE AGLERFKNPQ TPQGMLKGTP LNDLFLQIRI GGDQALFRLL
NKLILETEGA VDQAFVTEHT HGYEEFAAAA AEADWDATLA ATGLDRAAVE QALAMVLESE
RTVVCWAMGL TQHKHSVPTI REVVNFLLLR GNIGRPGAGV CPVRGHSNVQ GDRTMGIFER
PAPAFLDALD KEFGITSPRH HGYDVVRAIR ALRDGEAKVF FAMGGNFVAA TPDTDVTEAA
MRNARLTVHV STKLNRSHAV TGARALILPT LGRTDKDVQA GGKQFVTVED SMSKVHASRG
NLTPASPHLL SEPAIVARLA RAVLGPESAT PWEEFEKDYA TIRDRISRVV PGFENFNARI
AHPGGFTLPH GPRDSRRFPT ATGKANFTAA PVEFPELPEG RLLLQTLRSH DQYNTTIYGL
DDRYRGIKGG RRVVLVHPQD AQALGLPDGS YTDLVSEWKD GVERRAPGFR VVHYPTARGC
AAAYYPETNV LVPLDSTADT SNTPASKSVV VRFEPAS
//
