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Database: UniProt
Entry: A0A108UDF1_9GAMM
LinkDB: A0A108UDF1_9GAMM
Original site: A0A108UDF1_9GAMM 
ID   A0A108UDF1_9GAMM        Unreviewed;       783 AA.
AC   A0A108UDF1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Putative formate dehydrogenase oxidoreductase protein {ECO:0000313|EMBL:KWS07183.1};
GN   ORFNames=AZ78_4744 {ECO:0000313|EMBL:KWS07183.1};
OS   Lysobacter capsici AZ78.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS07183.1, ECO:0000313|Proteomes:UP000023435};
RN   [1] {ECO:0000313|EMBL:KWS07183.1, ECO:0000313|Proteomes:UP000023435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ78 {ECO:0000313|EMBL:KWS07183.1,
RC   ECO:0000313|Proteomes:UP000023435};
RX   PubMed=24762937;
RA   Puopolo G., Sonego P., Engelen K., Pertot I.;
RT   "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT   to Plant-Pathogenic Oomycetes.";
RL   Genome Announc. 2:0-0(2014).
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:KWS07183.1}.
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DR   EMBL; JAJA02000001; KWS07183.1; -; Genomic_DNA.
DR   RefSeq; WP_036110566.1; NZ_JAJA02000001.1.
DR   AlphaFoldDB; A0A108UDF1; -.
DR   OrthoDB; 5287431at2; -.
DR   Proteomes; UP000023435; 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; 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}.
FT   DOMAIN          109..491
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          649..756
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   783 AA;  86853 MW;  481E9BAFF317C16F CRC64;
     MSKNPIRPYN GPAGGWGALR SVATQLIEQD IPVSGARTLL SANQPDGFDC PGCAWPDRDH
     TSTFEFCENG AKAVAAEATK HRATPELFAQ HTVADLARYS DHWLENQGRL THPMRWDAAS
     DKYLPITWDE AFSRIGAHLN ALASPDQALF YTSGRCSNEA AFLYQLFVRE YGTNNFPDCS
     NMCHEPSGTA MKAQLGIGKG TVQLRDFEIA EAIFIFGQNP GTNHPRMLGE LRQASKRGAA
     IVSFNPLRER GLERFADPQD KLEMLHNGST RISSDYFQLR IGGDLAAVKG MIKRVLELDA
     QARRDGRERV VDLDFIAEHT RGFEAFVAEV ESESWDTIVA ESGLTRAELE RAGDIYARAK
     SVICCWGMGI TQHKHSVATI QMIVNLMLLR GNIGRPGAGP CPVRGHSNVQ GDRTMGIYEK
     PSPAFLDRLR DVFGFEPPRE HGHDTVGAIE AMLDGRCKTF FGLGGNFATA TPDTEATHRA
     LRRCDLTVHV TTKLNRSHLV HGRDAYILPC LGRTEIDMQE TGPQSVTVED SMSMVHLSAG
     INAPADPMLL SEPAIVARLA HATLGARSKV PWLWLIGDYD RIRDRIADVF DDFYDFNLRV
     RVPGGFHLTN AAAERRWLNR EAKALFKPHA VPTDLPVHRA RASREQPVFT LATTRSHDQY
     NTTIYGMNDR YRGVFGERRV LFINAQDIAE LNMQAGDWVD LESLCDDGVR RVAKRFLLVE
     YNIPRGCLAA YYPETNSLVP LSSFADEART PTSKSIPVIV YAHVAQPGAN LQSAKDIGLV
     RVD
//
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