ID A0A0M6YEK7_9RHOB Unreviewed; 443 AA.
AC A0A0M6YEK7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=NAD-dependent dihydropyrimidine dehydrogenase subunit PreT {ECO:0000313|EMBL:CTQ48781.1};
DE EC=1.3.1.1 {ECO:0000313|EMBL:CTQ48781.1};
GN Name=preT {ECO:0000313|EMBL:CTQ48781.1};
GN ORFNames=JDO7802_00786 {ECO:0000313|EMBL:CTQ48781.1};
OS Jannaschia donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Jannaschia.
OX NCBI_TaxID=420998 {ECO:0000313|EMBL:CTQ48781.1, ECO:0000313|Proteomes:UP000049222};
RN [1] {ECO:0000313|EMBL:CTQ48781.1, ECO:0000313|Proteomes:UP000049222}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7802 {ECO:0000313|EMBL:CTQ48781.1,
RC ECO:0000313|Proteomes:UP000049222};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CXSU01000005; CTQ48781.1; -; Genomic_DNA.
DR RefSeq; WP_055082731.1; NZ_CXSU01000005.1.
DR AlphaFoldDB; A0A0M6YEK7; -.
DR STRING; 420998.JDO7802_00786; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000049222; Unassembled WGS sequence.
DR GO; GO:0004159; F:dihydropyrimidine dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; 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; 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; PR00419; ADXRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:CTQ48781.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000049222}.
FT DOMAIN 21..130
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 144..427
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 443 AA; 46350 MW; 9D14F695380BCDFB CRC64;
MTEALRLDGI RAGRLGPEDL AKNFADLHPA LTSHEATIAA DRCYFCHDAP CVTACPTDID
IPLFIRQIAT GTEEAAAKTI FDQNILGGMC ARVCPTETLC EQVCVREVAE GKPVEIGRLQ
RFATDAMMAD GEHPFTRAPD TGKSVAVVGA GPAGLAAAHR LALHGHSVTM FDARPKAGGL
NEYGIAAYKT PHDYAQAEVD WLLKIGGITV ETGKALGDGL TLSALRSDFD AVFLGIGLGG
VGALGLDGED MTGTENAVDF IATLRQTDDL TTLPVGRHVV VIGGGMTAVD AAVQSKLLGA
ETVTIAYRRN QAKMPASRYE QDLAATHGVR LMFGVVPVAL RGDAQLREVE LGYVDTDTKP
TGETLILRAD QLLRAIGQKL ETMEGLTLDG GKIAVDASGK TSLADVWAGG DCASGGEDLT
VTAVAEGRDA AMDIHASLTQ SAP
//