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Database: UniProt
Entry: A0A384I709_9ACTN
LinkDB: A0A384I709_9ACTN
Original site: A0A384I709_9ACTN 
ID   A0A384I709_9ACTN        Unreviewed;       757 AA.
AC   A0A384I709;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FdhF/YdeP family oxidoreductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=DNK56_10625 {ECO:0000313|EMBL:PZT82478.1};
OS   Streptomyces sp. AC1-42W.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2218666 {ECO:0000313|EMBL:PZT82478.1, ECO:0000313|Proteomes:UP000249154};
RN   [1] {ECO:0000313|EMBL:PZT82478.1, ECO:0000313|Proteomes:UP000249154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AC1-42W {ECO:0000313|EMBL:PZT82478.1,
RC   ECO:0000313|Proteomes:UP000249154};
RA   De Leon M.P., Montecillo A.D., Siringan M.A.T., Kim S.-G., Rosana A.R.R.;
RT   "Near complete genome sequences of Streptomyces sp. strains AC1-42W
RT   isolated from bat guano of Cabalyorisa Cave, Pangasinan, Philippines.";
RL   Submitted (JUN-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:PZT82478.1}.
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DR   EMBL; QKWY01000001; PZT82478.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A384I709; -.
DR   Proteomes; UP000249154; 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:UP000249154}.
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..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   757 AA;  81778 MW;  BA65785BCF59D4E0 CRC64;
     MAGKPPAGDP VQDAPQVGPA KHAAAGLPAV AESLRVAQRQ MGLRRSAQTL LKVNQKDGFD
     CPGCAWPEGD KRHVAEFCEN GVKAVAEEAT LRRVTPDFFA AHPVGDLAGR SGYWLGQQGR
     ITQPVYLPEG ADRYQAVTWE RAFEIIAEEL GALSSPDEAV FYTSGRTSNE AAFLLQLFAR
     EFGTNNLPDC SNMCHESSGS ALTETIGVGK GSVSLEDLHH ADLIIIAGQN PGTNHPRMLS
     ALEQAKAAGA KIISVNPLPE AGLERFKNPQ TPHGMVRGTP LNDLFLQIRI GGDQALFRLL
     NKLILDTEGA VDERFVAEHT HGYEEFAAAA AAADWDETLA ATGLDRAAIE QALALVLASE
     RTVVCWAMGL TQHKHSVPTI REIVNFLLLR GNIGRPGAGV CPVRGHSNVQ GDRTMGIFER
     PSTAFLDALD TEFGITSPRH HGYDVVRAIR ALRDGDAKVF FAMGGNFVAA TPDTDVTEAA
     MRNARLTVHV STKLNRSHAV TGTRALILPT LGRTDKDVQA SGKQFVTVED SMSKVHASRG
     NLTPASPHLL SEPAIVARLA RAVLGPGSAT PWEDFEHDYA TIRDRISRVV PGFENFNARI
     AHPGGFTLPH APRDSRRFPT DTGRANFTAA PVEYPKPPEG RLLLQTLRSH DQYNTTIYGL
     DDRYRGIKGG RRVVLVHPDD ATALGLADGS YTDLVSEWKD GVERRAPGFR VVHYPTARGC
     AAAYYPETNV LVPLDSTADT SNTPASKSVV VRFEPAR
//
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