ID   A0A0Q5HC29_9BURK        Unreviewed;       456 AA.
AC   A0A0Q5HC29;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Dihydropyrimidine dehydrogenase {ECO:0000313|EMBL:KQQ92050.1};
GN   ORFNames=ASF77_07150 {ECO:0000313|EMBL:KQQ92050.1};
OS   Massilia sp. Leaf139.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1736272 {ECO:0000313|EMBL:KQQ92050.1, ECO:0000313|Proteomes:UP000051760};
RN   [1] {ECO:0000313|EMBL:KQQ92050.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ92050.1,
RC   ECO:0000313|Proteomes:UP000051760};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQQ92050.1, ECO:0000313|Proteomes:UP000051760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf139 {ECO:0000313|EMBL:KQQ92050.1,
RC   ECO:0000313|Proteomes:UP000051760};
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=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:KQQ92050.1}.
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DR   EMBL; LMOJ01000012; KQQ92050.1; -; Genomic_DNA.
DR   RefSeq; WP_056339017.1; NZ_LMOJ01000012.1.
DR   AlphaFoldDB; A0A0Q5HC29; -.
DR   STRING; 1736272.ASF77_07150; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000051760; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000051760}.
FT   DOMAIN          32..65
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   456 AA;  48392 MW;  B4C10C7940C5EE6A CRC64;
     MIETLQHLPP AADSHGALAA QFTDLAPPLT SRQAAIEAAR CLYCYDAPCM RACPTGIDVA
     SFIRNIHDQN INGAAIGILK ANIFGGSCAR VCPTEILCES ACVRNHYAER EPVKIGLLQR
     HAIDNASFAG HPFTRAPATG KTIAVVGAGP AGLACAHRLA MLGHDVVVFE ARPKAGGLNE
     YGIAKYKLPG EFAQQEVDFL LQIGGIDIQY GQALGENLQL RDLHARFDAV FLGLGLGASR
     RLGLTGEDAP GLMAATDYIA ALRQADDLST LPVPRRAIVI GAGNTAIDMA VQIKRLGADE
     VTLVYRRGFD AMSATAHEIE IAKLNFVCIR TWASPLEVLL DDAGRVAGMR FEETRMEEGR
     LARTGAFVEI AADAVFKAIG QAMAPPSEFD LVAQDLWQDG GRIAVDGALR TKVPGIYAGG
     DCVALGQDLT VQAVQHGKLA ALAIHNDIVS EAAWPT
//