ID   A0A0Q5PAQ0_9SPHN        Unreviewed;       757 AA.
AC   A0A0Q5PAQ0;
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:KQR81296.1};
GN   ORFNames=ASG07_12665 {ECO:0000313|EMBL:KQR81296.1};
OS   Sphingomonas sp. Leaf343.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736345 {ECO:0000313|EMBL:KQR81296.1, ECO:0000313|Proteomes:UP000051323};
RN   [1] {ECO:0000313|EMBL:KQR81296.1, ECO:0000313|Proteomes:UP000051323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf343 {ECO:0000313|EMBL:KQR81296.1,
RC   ECO:0000313|Proteomes:UP000051323};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQR81296.1, ECO:0000313|Proteomes:UP000051323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf343 {ECO:0000313|EMBL:KQR81296.1,
RC   ECO:0000313|Proteomes:UP000051323};
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:KQR81296.1}.
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DR   EMBL; LMPG01000014; KQR81296.1; -; Genomic_DNA.
DR   RefSeq; WP_055847652.1; NZ_LMPG01000014.1.
DR   AlphaFoldDB; A0A0Q5PAQ0; -.
DR   STRING; 1736345.ASG07_12665; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000051323; 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   CDD; cd02787; MopB_CT_ydeP; 1.
DR   CDD; cd02767; MopB_ydeP; 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; 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   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:UP000051323}.
FT   DOMAIN          109..410
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
SQ   SEQUENCE   757 AA;  83719 MW;  30C2F84AE790043A CRC64;
     MSDIEITKYT GAAGGWGSMK GMAKVLPKEG ISPDLLDALR RQNKPEGVMC VSCAWGKPAK
     PHIAEFCENG AKATAWELTR ERVTPEFFQQ HSVTELESWP DHDLEQSGRL THPMRYDRTT
     DRYVAASWDE AFAAIGAKLR TCDPKKVVLY ASGRASLETS YMYALFARMW GSQNLPDSSN
     MCHETTSVGL KNAIGSPVAT IQMDDYEKCD AIFAFGQNVG TNSPRMLHTL RDCVKRGVEI
     VNFNPLRERG WERFTDPQNP VEMTTGGSTR ISSQYHQLRA GGDIAAILGI CKIVIEADDI
     ALASGAPRVV DHHFVEQHTV RFEEFAAFCR KADWPDIVRE SGLSREAIEA AARVYMEAER
     VIAVYGMGIT QHRYGIDSLY MIVNLLLLRG NIGRDGAGPG PVRGHSNVQG QRTVGITEKT
     ELAPVERLRE LFEFEPPTEK GWDTVDACRK IIAGECQGFV QLGGNFLRAT PEHGAMKEGW
     AKLPIAVHIA TKLNKSHLIP GEESWILPCL GRMEQDMQAG GRQAVSMEDS FSHIYGSVGK
     ATPAADTLLS EPAIVAGIAN AVLEPNPNVP WDDWVGDYGL VRTAIEDTYP DKFSNFNERL
     FTPGGFWKGN PASHRQWETE SGKAEFNVPR ALNAAGFADA DGRFRLVTLR SNDQFNTTIY
     GYDDRFRGIS GTRMVAMMNR GDLARMGLKK GDMIALESDA EDATDRVVEG LRVVEYDIPA
     GCIAGYYPEL NYLIPVEHHA LDSHVPAAKS IPVRIRR
//