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Database: UniProt
Entry: A0A0Q4XNL6_9BURK
LinkDB: A0A0Q4XNL6_9BURK
Original site: A0A0Q4XNL6_9BURK 
ID   A0A0Q4XNL6_9BURK        Unreviewed;       318 AA.
AC   A0A0Q4XNL6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Molybdopterin dehydrogenase {ECO:0000313|EMBL:KQP14035.1};
GN   ORFNames=ASF43_14380 {ECO:0000313|EMBL:KQP14035.1};
OS   Pseudorhodoferax sp. Leaf267.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP14035.1, ECO:0000313|Proteomes:UP000051560};
RN   [1] {ECO:0000313|EMBL:KQP14035.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14035.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP14035.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP14035.1,
RC   ECO:0000313|Proteomes:UP000051560};
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   -!- 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:KQP14035.1}.
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DR   EMBL; LMMV01000022; KQP14035.1; -; Genomic_DNA.
DR   RefSeq; WP_056184674.1; NZ_LMMV01000022.1.
DR   AlphaFoldDB; A0A0Q4XNL6; -.
DR   STRING; 1736316.ASF43_14380; -.
DR   OrthoDB; 9814706at2; -.
DR   Proteomes; UP000051560; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR42659:SF5; ALDEHYDE OXIDOREDUCTASE FAD-BINDING SUBUNIT PAOB; 1.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051560}.
FT   DOMAIN          1..223
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   318 AA;  33551 MW;  829D8B9038F875DB CRC64;
     MKAFTFERAR TPAEAAAAVA RTPGARFIAG GTNLVDLMKL QIETPGHLVD VNGLALDKIE
     PAPGGGLRIG ALVRNTDLAA DMRVRRDYAV LSRALLSGAS GQLRNKATTA GNLLQRTRCP
     YFYDTAQACN KRSPGSGCSA LDGVNRQHAI LGTSDTCIAT HPSDMAVAMR VLDAQVETVR
     GDGQARTIPI ADFHRLPGNT PQRETALEAG ELITAVTLPP PVGGRHMYRK VRDRASYAFA
     LVSVAAIVQP DGRGRLALGG VAHKPWRVDA ADAALPRGAA AAGEQLLAGA RTTEHNAFKP
     PLVQRLLAAV LAEARRPA
//
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