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Database: UniProt
Entry: A0A0A0M663_9GAMM
LinkDB: A0A0A0M663_9GAMM
Original site: A0A0A0M663_9GAMM 
ID   A0A0A0M663_9GAMM        Unreviewed;       265 AA.
AC   A0A0A0M663;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=NADH dehydrogenase {ECO:0000313|EMBL:KGO98565.1};
DE   Flags: Fragment;
GN   ORFNames=N791_01265 {ECO:0000313|EMBL:KGO98565.1};
OS   Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO98565.1, ECO:0000313|Proteomes:UP000030003};
RN   [1] {ECO:0000313|EMBL:KGO98565.1, ECO:0000313|Proteomes:UP000030003}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO98565.1,
RC   ECO:0000313|Proteomes:UP000030003};
RA   Wang Q., Wang G.;
RT   "Genomic analysis of Lysobacter defluvii.";
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|ARBA:ARBA00034078};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00005404}.
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:KGO98565.1}.
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DR   EMBL; AVBH01000068; KGO98565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A0M663; -.
DR   eggNOG; COG1034; Bacteria.
DR   Proteomes; UP000030003; Unassembled WGS sequence.
DR   GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0045333; P:cellular respiration; IEA:UniProt.
DR   CDD; cd02775; MopB_CT; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 1.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR   InterPro; IPR006656; Mopterin_OxRdtase.
DR   PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030003};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          41..130
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          183..251
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KGO98565.1"
SQ   SEQUENCE   265 AA;  27101 MW;  3C529E749F2BBB2B CRC64;
     TATGAALCRI PQGANAVGLS RLGVLPTGRD ARGMLAEARG AYVLYGIEPG LDFVDTAAAM
     QALGGAQVVA FSHFACESTR AVADVILPIG LLPEIEGTLV NLDGREQSTV AGGRLPREAR
     EGWKVLRALA GMLQADGFGF TDLAGLREGM AVRDVTPVAG TPVPAGEGME VAASEAIYRV
     DAVVRRSQAL QSHPLNQPPR AVVNPADAES AGLAPGGTGR FSTASGTATL PVELNPRVAP
     GTVWIETGHA ATAPLRAGRL QVGRA
//
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