ID G2GNA7_9ACTN Unreviewed; 759 AA.
AC G2GNA7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:EGX55008.1};
GN ORFNames=SZN_35062 {ECO:0000313|EMBL:EGX55008.1};
OS Streptomyces zinciresistens K42.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX55008.1, ECO:0000313|Proteomes:UP000004217};
RN [1] {ECO:0000313|EMBL:EGX55008.1, ECO:0000313|Proteomes:UP000004217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K42 {ECO:0000313|EMBL:EGX55008.1,
RC ECO:0000313|Proteomes:UP000004217};
RA Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL Submitted (AUG-2011) 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:EGX55008.1}.
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DR EMBL; AGBF01000282; EGX55008.1; -; Genomic_DNA.
DR RefSeq; WP_007504395.1; NZ_AGBF01000282.1.
DR AlphaFoldDB; G2GNA7; -.
DR PATRIC; fig|700597.3.peg.6836; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000004217; 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; 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:UP000004217}.
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; 82919 MW; 793D37F429E41FCC CRC64;
MASKPPQGDP VQDAPEVAEP QHAAAGLPAV GHTLRIAQRQ MGVKRTALTL LRVNQKDGFD
CPGCAWPEAE HRHKAEFCEN GAKAVAEEAT LRRVTPEFFA AHSVADLATR SGYWLGQQGR
LTHPVHLPEG GTHYEPVSWE RAFDMIAEDI AALGSPDEAV FYTSGRTSNE AAFLYQLFAR
ELGTNNLPDC SNMCHESSGS ALSETIGVGK GSVLLDDLHQ AELIIVAGQN PGTNHPRMLS
ALEKAKANGA RIITVNPLPE AGLERFKNPQ TAQGMLKGAA LTDLFLQIRL GGDQALFRLL
NKLILETEGA VDEAFVREHT HGFEEFAEAA RAADWDETLT ATGLTRADID KALSMVLASR
RTIVCWAMGL TQHKHSVPTI REVVNFLLLR GDIGRPGSGV CPVRGHSNVQ GDRTMGIFER
PAPAFLDALE REFGFAPPRE HGFDVVRAIR ALRDGEAKVF FAMGGNFVAA TPDTDVTEAA
MRRARLTVHV STKLNRSHAV TGARALILPT LGRTERDLQG GGEQFVTVED SMGMVHASRG
RLEPASTHLL SEPAIVCRLA RRVLGEESRT PWEEFEKDYA TVRDRIARVI PGFEDFNARV
ARPGGFTLPH APRDERRFPT ATGKANFTAA PVEYPELPEG RLLLQTLRSH DQYNTTIYGL
DDRYRGIRNG RRVVLVNPED AERLGVADGS YVDLVGEWRD GVERRAPGFR VVHYPTARGC
AAAYYPETNV LVPLDATADT SNTPASKSVV VRLEQSATD
//
