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Database: UniProt
Entry: A0A2C6L1H1_9FIRM
LinkDB: A0A2C6L1H1_9FIRM
Original site: A0A2C6L1H1_9FIRM 
ID   A0A2C6L1H1_9FIRM        Unreviewed;       468 AA.
AC   A0A2C6L1H1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Dihydropyrimidine dehydrogenase subunit A {ECO:0000313|EMBL:PHJ36951.1};
GN   ORFNames=P378_19245 {ECO:0000313|EMBL:PHJ36951.1};
OS   Desulforamulus profundi.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1383067 {ECO:0000313|EMBL:PHJ36951.1, ECO:0000313|Proteomes:UP000222564};
RN   [1] {ECO:0000313|EMBL:PHJ36951.1, ECO:0000313|Proteomes:UP000222564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bs107 {ECO:0000313|EMBL:PHJ36951.1,
RC   ECO:0000313|Proteomes:UP000222564};
RA   Aullo T., Berlendis S., Lascourreges J.-F., Dessort D., Saint-Laurent S.,
RA   Schraauwers B., Mas J., Magot M., Ranchou-Peyruse A.;
RT   "Biodegradation of hydrocarbons in the deep terrestrial subsurface :
RT   characterization of a microbial consortium composed of two Desulfotomaculum
RT   species originating from a deep geological formation.";
RL   Submitted (SEP-2013) 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:PHJ36951.1}.
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DR   EMBL; AWQQ01000131; PHJ36951.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C6L1H1; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000222564; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   InterPro; IPR006004; SudA-like.
DR   NCBIfam; TIGR01316; gltA; 1.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00411; PNDRDTASEI.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000222564}.
FT   DOMAIN          20..129
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          141..449
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   468 AA;  50942 MW;  F69AB54806E5EBDF CRC64;
     MAKQIIPKKH PMPHQDPQVR AKNFDEVALG YTEELAVAEA ERCLNCKKPF CKQGCPVSVD
     IPEFIALVKE RKFDEAAKVI KRTNALPAVC GRVCPQEHQC EKFCVVGKKN EPVGIGRLER
     FVGDYIVNKE EEIEKAEPTG YKVAIVGSGP AGLACAADLA RWGHSVTIFE ALHTPGGVLM
     YGIPEFRLPK RIVQKEIENL KKMGVEIETN AIVGQIASLD ELFEEEGYDA VFLGTGAGTP
     YFMNLPGENF NGVYSANEFL TRSNLMKAYC FPECDTPIKV GKKVAVLGGG NVAMDAARTA
     LRLGAEEVYI VYRRSRAELP ARLEEIEHAE EEGVKFLFLT NPTRYIGNEE GWLTGLECIK
     MELGEPDASG RRKPVAIPGS EFVLPVDVTI VAIGQGPNPL ITKTTPDLET NKRGNIVADD
     FGKTSKEGVY AGGDVVTGAA TVIKAMGAGR VAAQSIHDYL MAKGPKKN
//
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