ID E2NC81_9BACE Unreviewed; 494 AA.
AC E2NC81;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=BACCELL_01888 {ECO:0000313|EMBL:EEF90484.1};
OS Bacteroides cellulosilyticus DSM 14838.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=537012 {ECO:0000313|EMBL:EEF90484.1, ECO:0000313|Proteomes:UP000003711};
RN [1] {ECO:0000313|EMBL:EEF90484.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF90484.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEF90484.1, ECO:0000313|Proteomes:UP000003711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14838 {ECO:0000313|EMBL:EEF90484.1,
RC ECO:0000313|Proteomes:UP000003711};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides cellulosilyticus (DSM 14838).";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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:EEF90484.1}.
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DR EMBL; ACCH01000149; EEF90484.1; -; Genomic_DNA.
DR RefSeq; WP_007211263.1; NZ_JANSWE010000061.1.
DR AlphaFoldDB; E2NC81; -.
DR HOGENOM; CLU_042042_4_2_10; -.
DR Proteomes; UP000003711; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF14691; Fer4_20; 1.
DR Pfam; PF14697; Fer4_21; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022827};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 432..462
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 464..493
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 494 AA; 54483 MW; CAD74C9D9746A331 CRC64;
MAKNKTRIAD ATRCLMCYQP ICDIACQKKV FPAGIIHALH LKNEAGAYLR SAENVSCLHC
DDAKCEKACA RGRVDSPIRI QEICRYVSQM ENISRESTQA ELSVNFCGIR CENPFFLASS
PVASSFEMCC HAFDAGWAGV SYKTISFYQS REVSPRFDAL PGEHPFSFCG FKNLEQLSPH
SAEENFEIIR RLKERYPEKV IIASIMGRNC DEWTVLARMA EEAGADLIEC NFSCPQMAKQ
GLGSDIGQDQ DLIALYTRAT RKGSRLPIIA KMTPNIGNME LPAMTAIANG ANSLAAINTV
KSITRINTEN FSSYPDIGGQ SAVGGYSGQA VKPIALRFIR DLASYPPLKG IPLFGIGGIT
TWQDALDFIL LGCTALQVCT SVMEYGYRII DHLKEGLSIY MKQHDIASLD ELRGLALPNL
VQPEQLDRER KLHCEIDSRR CIHCGRCYIS CLDGGHQAIG WEKRTPMIDK SLCVGCGLCT
LVCPTEAISL VNSL
//
