ID A0A133UGY7_9EURY Unreviewed; 362 AA.
AC A0A133UGY7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=AKJ64_00485 {ECO:0000313|EMBL:KXA93464.1};
OS candidate division MSBL1 archaeon SCGC-AAA259E17.
OC Archaea; Euryarchaeota; candidate division MSBL1.
OX NCBI_TaxID=1698263 {ECO:0000313|EMBL:KXA93464.1, ECO:0000313|Proteomes:UP000070373};
RN [1] {ECO:0000313|EMBL:KXA93464.1, ECO:0000313|Proteomes:UP000070373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA259E17 {ECO:0000313|EMBL:KXA93464.1};
RX PubMed=26758088; DOI=10.1038/srep19181;
RA Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT pools of the Red Sea.";
RL Sci. Rep. 6:19181-19181(2016).
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:KXA93464.1}.
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; LHXN01000004; KXA93464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133UGY7; -.
DR PATRIC; fig|1698263.3.peg.643; -.
DR UniPathway; UPA00070; -.
DR Proteomes; UP000070373; Unassembled WGS sequence.
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; IPR017900; 4Fe4S_Fe_S_CS.
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; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF13237; Fer4_10; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS00912; DHODEHASE_2; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070373}.
FT DOMAIN 307..336
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 337..362
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 362 AA; 37828 MW; 9CF67D92A9F1DF72 CRC64;
MADLTTEIAG IKLRNPIMPA SGPTVRDGDS LVEVANSGAG GLVAKTVSLE PAKVPRPNLA
KIGDSLINAE MWSEIPLDQW IEEEYPKAKE TGLPLIASIG YTPEEVGELA SRVMEAEVDA
LEISTTRLDH DSSLLAEVVE SAKSEGDVPV FVKLNPQWGD VADCAEIAEE AGADGIVAID
AVGPSLTIEI NTERPVMGSK GGYGWLSGPA IKPIAVRCVA DIAKAVDIPV IGVGGIKDEQ
DVAEFLMAGA SAVQICTAAI IRGNKIFGLI ADNLNKFLNA RNYDSIDDVC GSALKNLPEE
QVRTSAKQPD ILTAECTGCG LCMKHCPSDA ITIIGGKARI ESTGCTGCGL CVSVCPANAL
RF
//