ID A0A0Q4C751_9SPHN Unreviewed; 754 AA.
AC A0A0Q4C751;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Formate dehydrogenase {ECO:0000313|EMBL:KQM20650.1};
GN ORFNames=ASE49_16800 {ECO:0000313|EMBL:KQM20650.1};
OS Novosphingobium sp. Leaf2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1735670 {ECO:0000313|EMBL:KQM20650.1, ECO:0000313|Proteomes:UP000050893};
RN [1] {ECO:0000313|EMBL:KQM20650.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM20650.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM20650.1, ECO:0000313|Proteomes:UP000050893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf2 {ECO:0000313|EMBL:KQM20650.1,
RC ECO:0000313|Proteomes:UP000050893};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQM20650.1}.
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DR EMBL; LMJY01000006; KQM20650.1; -; Genomic_DNA.
DR RefSeq; WP_056769308.1; NZ_LMJY01000006.1.
DR AlphaFoldDB; A0A0Q4C751; -.
DR STRING; 1735670.ASE49_16800; -.
DR OrthoDB; 5287431at2; -.
DR Proteomes; UP000050893; Unassembled WGS sequence.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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 GO; GO:0045333; P:cellular respiration; IEA:UniProt.
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:UP000050893}.
FT DOMAIN 110..406
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 640..748
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 754 AA; 82389 MW; DCB66B0D338DA555 CRC64;
MSDEAQPRHY NKATGGWGSM EGMARVELTT KAGPSALATL KEQNKPGGYM CSSCAWAKPP
EPHVAEFCEN GAKATLWDLT PKRCTPEFFA THTVSELKTW SDFDLEDAGR LTHPLRYDAA
SDRYLPVSWE TAFAAIGATL KRLEPKSVTF YASGKAALEP SYLYALLARM YGNNNLPDSS
NMCHETTSVG LKKVLGSPVG TCTFQDLEKC DAIFYIGQNP GTNSPRILHP LNDAVKRGCK
IVAFNPLREK GLLEFTDPQN PWQMTLGKPT QIAHQYVQVA AGGDIAALMG VCKRVLELDA
QTGNVLDRAF LDEHCHGMDD FIAKVHATTW DEIEENSGVS RAELEAAGDV YAQAKNVIGI
YGMGLTQQVH GTQAIGMLVN LLLLRGNIGR PGAGCQPIRG HSNVQGQRTV GISEKPELVP
LDKLREIFGF DPPTEKGHTT VEFLEALLDG SARGFIGLGG NIVRAVPDQS RFDGAWPGLD
ITVNIATKLN HTHLRPGKES FLLPCLVRAE DDRQASGPQQ VSIEDSFSHI YGSIGRRTPA
SEHLKSELAI ITGIAKATLP PRPDWAWDEW TADYGKVREL IARTYPDEFY DMSARMDQPG
GFYRGNPAHD RIWKTESGRA EFTVPTVLTN SGLTKAAGRF TLVTLRSNDQ FNTTVYGYSD
RLRGLSGNRM IVLMSPADMA DMKLADGAVV TLVTDCGDDR RRAVSGLTVT PYDLPRGCLA
GYFPELNPLV PLDHHDELSK TPAAKGVPVR IETS
//
