ID A0A1B1M7N9_STRLN Unreviewed; 759 AA.
AC A0A1B1M7N9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=FdhF/YdeP family oxidoreductase {ECO:0000313|EMBL:QMV06368.1};
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:ANS64544.1};
GN ORFNames=GJU35_12245 {ECO:0000313|EMBL:QMV06368.1}, SLCG_6093
GN {ECO:0000313|EMBL:AXG57248.1}, SLINC_2320
GN {ECO:0000313|EMBL:ANS64544.1};
OS Streptomyces lincolnensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1915 {ECO:0000313|EMBL:ANS64544.1, ECO:0000313|Proteomes:UP000092598};
RN [1] {ECO:0000313|EMBL:ANS64544.1, ECO:0000313|Proteomes:UP000092598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2936 {ECO:0000313|EMBL:ANS64544.1,
RC ECO:0000313|Proteomes:UP000092598};
RA Meng S.C.;
RT "Enhancement of antibiotic productionsby engineered nitrateutilization in
RT actinobacteria.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AXG57248.1, ECO:0000313|Proteomes:UP000253884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC-G {ECO:0000313|EMBL:AXG57248.1,
RC ECO:0000313|Proteomes:UP000253884};
RX PubMed=29574602; DOI=10.1007/s10295-018-2029-1;
RA Xu Y., Tan G., Ke M., Li J., Tang Y., Meng S., Niu J., Wang Y., Liu R.,
RA Wu H., Bai L., Zhang L., Zhang B.;
RT "Enhanced lincomycin production by co-overexpression of metK1 and metK2 in
RT Streptomyces lincolnensis.";
RL J. Ind. Microbiol. Biotechnol. 45:345-355(2018).
RN [3] {ECO:0000313|EMBL:QMV06368.1, ECO:0000313|Proteomes:UP000515335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B48 {ECO:0000313|EMBL:QMV06368.1,
RC ECO:0000313|Proteomes:UP000515335};
RX PubMed=32322696;
RA Wang R., Kong F., Wu H., Hou B., Kang Y., Cao Y., Duan S., Ye J., Zhang H.;
RT "Complete genome sequence of high-yield strain S. lincolnensis B48 and
RT identification of crucial mutations contributing to lincomycin
RT overproduction.";
RL Synth Syst Biotechnol 5:37-48(2020).
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}.
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DR EMBL; CP016438; ANS64544.1; -; Genomic_DNA.
DR EMBL; CP022744; AXG57248.1; -; Genomic_DNA.
DR EMBL; CP046024; QMV06368.1; -; Genomic_DNA.
DR RefSeq; WP_067430749.1; NZ_CP046024.1.
DR AlphaFoldDB; A0A1B1M7N9; -.
DR STRING; 1915.SLINC_2320; -.
DR KEGG; sls:SLINC_2320; -.
DR PATRIC; fig|1915.4.peg.2580; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000092598; Chromosome.
DR Proteomes; UP000253884; Chromosome.
DR Proteomes; UP000515335; Chromosome.
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; 2.40.40.20; -; 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:UP000092598}.
FT DOMAIN 120..492
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..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 83119 MW; F55D8D05FA724D82 CRC64;
MASKPPKSDP VQDAPQVAEP QHAAAGLPAI GHTLRMARQQ MGVKRTALTL LRVNQKDGFD
CPGCAWPEPD HRHAAEFCEN GAKAVAEEAT LRRVTPEFFA AHSVADLATR SGYWLGQQGR
LTHPVYLPEG GDRYEPVTWE RAFDIVAEEI AALGSPDEAL FYTSGRTSNE AAFLYQLFAR
ELGTNNLPDC SNMCHESSGS ALSETIGIGK GSVLLEDLYQ ADLIIVAGQN PGTNHPRMLS
ALEKAKANGA KIISVNPLPE AGLERFKNPQ TAKGLTTGAA LNDLFLQIRI GGDQALFRLL
NKLILETEGA VDEDFVREHT HGYEEFAAQA RAADWDETLT ATGLSQKEIE EALRMILASK
RTIVCWAMGL TQHKHSVPTI REVVNFLLLR GNIGRPGAGV CPVRGHSNVQ GDRTMGIFER
PAPAFLDALE REFGFAPPRE HGYDVVQAIR ALRDGKAKVF FAMGGNFVSA SPDTEVTEAA
MRRARLTVHV STKLNRSHAV TGARALILPT LGRTERDLQG GGEQFVTVED SMGMVHASRG
RLEPASTHLL SEPAIVCRLA RRVLGEDSRV PWEEFEKDYA TIRDRIARVI PGFEDFNARV
AHPGGFTLPH APRDERRFPT ATGKANFTAA PVEYPKLPEG RLLLQTLRSH DQYNTTIYGL
DDRYRGIKNG RRVVLVNPED AGRLKIADGS YVDLVSEWTD KVERRAPGFR VVFYPTARGC
AAAYYPETNV LVPLDATADV SNTPASKSVV VRLEQSATD
//
