ID A9BIU8_PETMO Unreviewed; 363 AA.
AC A9BIU8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN OrderedLocusNames=Pmob_1743 {ECO:0000313|EMBL:ABX32436.1};
OS Petrotoga mobilis (strain DSM 10674 / SJ95).
OC Bacteria; Thermotogota; Thermotogae; Petrotogales; Petrotogaceae;
OC Petrotoga.
OX NCBI_TaxID=403833 {ECO:0000313|EMBL:ABX32436.1, ECO:0000313|Proteomes:UP000000789};
RN [1] {ECO:0000313|EMBL:ABX32436.1, ECO:0000313|Proteomes:UP000000789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10674 / SJ95 {ECO:0000313|Proteomes:UP000000789};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Meincke L., Brettin T., Bruce D., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Noll K., Richardson P.;
RT "Complete sequence of Petroga mobilis SJ95.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway.
CC {ECO:0000256|ARBA:ARBA00004725}.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; CP000879; ABX32436.1; -; Genomic_DNA.
DR RefSeq; WP_012209533.1; NC_010003.1.
DR AlphaFoldDB; A9BIU8; -.
DR STRING; 403833.Pmob_1743; -.
DR KEGG; pmo:Pmob_1743; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1145; Bacteria.
DR HOGENOM; CLU_042042_4_3_0; -.
DR OrthoDB; 9794954at2; -.
DR UniPathway; UPA00070; -.
DR Proteomes; UP000000789; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 2.30.26.10; Dihydroorotate Dehydrogenase A, chain A, domain 2; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR023359; Dihydro_DH_chainA_dom2.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR InterPro; IPR001295; Dihydroorotate_DH_CS.
DR PANTHER; PTHR48109:SF1; DIHYDROOROTATE DEHYDROGENASE (FUMARATE); 1.
DR PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 3: Inferred from homology;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975}.
FT DOMAIN 304..333
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 335..363
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 363 AA; 39010 MW; C0A8A6C633709B52 CRC64;
MADISVDLLG MLLKTPVMPA AGPPIKDGES AHKAKEGGAG AIVTKTVSAR AAKVPKPNMA
QVKGGFINTE LWSELSLEQW IEKEYPQVVE TGLPVIIGVG YTSEDIKEVI PKVERFADAF
ELSTHYLGND PTPMINSIRA AKETTDLPVM VKLSPQVDIP KFAKEAENAG ADGLVLINSF
GPTLDIDLES GKPLLGSENG FGWLSGQAIF PLALRSVFEA VRSVNIPVVG VGGINTGKEA
IKMIMAGAQA VQVCTAAILN GPQIYKKITN EIEKYLDDHD FKSLEEIRGI AQKNIVNEAN
YNLIFPAVND EKCTECALCV KSCVYDAIHL IKELHSVRID TNKCAGCGLC VTRCNFNALS
LSL
//
