ID E3C5C4_9LACO Unreviewed; 431 AA.
AC E3C5C4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=HMPREF9265_0088 {ECO:0000313|EMBL:EFQ54026.1};
OS Limosilactobacillus oris PB013-T2-3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=908339 {ECO:0000313|EMBL:EFQ54026.1, ECO:0000313|Proteomes:UP000003070};
RN [1] {ECO:0000313|EMBL:EFQ54026.1, ECO:0000313|Proteomes:UP000003070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB013-T2-3 {ECO:0000313|EMBL:EFQ54026.1,
RC ECO:0000313|Proteomes:UP000003070};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
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:EFQ54026.1}.
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; AEKL01000006; EFQ54026.1; -; Genomic_DNA.
DR RefSeq; WP_003711328.1; NZ_AEKL01000006.1.
DR AlphaFoldDB; E3C5C4; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000003070; 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:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR CDD; cd02940; DHPD_FMN; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01180; DHO_dh; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:EFQ54026.1}.
FT DOMAIN 337..367
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 371..400
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 431 AA; 46790 MW; FE867AA3CB5EA4A3 CRC64;
MIKKDLSIDF LGVHFENPFC LSSSPVGNCY EMCKNAYDAG WGGIVYKTLS PDHFVIDEVS
PRFAQLAKED TPFIAFKNME QLAEHPMAQD LAAMRRLKEE YPDKVLIASI MGETPQDWTD
LAKLVTAAGA DMIELNFSCP QMTSHTMGSD VGTNPELCKT NCAAVKKGTD LPVLAKMTPN
ITTMIPVVKA CLAGGADGVS SINTVKSITD VDLDNKVALP NINGKSAVSG LSGKSVKPIA
LRFLQQIRSA AGLEQLPVSG IGGIETWEDA AEFILLGAST LQVTTAIMQY GYRIIDDLTN
GLMHYMDEQG VDQLKDLVGI ANQNIVPTNQ LDRDYKVYPK IDWDKCIGCG RCFISCQDGA
HQAMGWDDDK RLPTFDQSKC VGCQLCALVC PVGAIKLGLV KMKPGRDGNP KDVDASSFQL
PNYDEAPVHS H
//
