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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//