ID A0A133V7C6_9EURY Unreviewed; 541 AA.
AC A0A133V7C6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 05-FEB-2025, entry version 19.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=AKJ43_01895 {ECO:0000313|EMBL:KXB02359.1};
OS candidate division MSBL1 archaeon SCGC-AAA261D19.
OC Archaea; Methanobacteriati; Methanobacteriota; candidate division MSBL1.
OX NCBI_TaxID=1698273 {ECO:0000313|EMBL:KXB02359.1, ECO:0000313|Proteomes:UP000070400};
RN [1] {ECO:0000313|EMBL:KXB02359.1, ECO:0000313|Proteomes:UP000070400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC-AAA261D19 {ECO:0000313|EMBL:KXB02359.1};
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 -!- 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}.
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:KXB02359.1}.
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DR EMBL; LHXX01000017; KXB02359.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A133V7C6; -.
DR Proteomes; UP000070400; 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 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; IPR050074; DHO_dehydrogenase.
DR InterPro; IPR005720; Dihydroorotate_DH_cat.
DR PANTHER; PTHR48109; DIHYDROOROTATE DEHYDROGENASE (QUINONE), MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF01180; DHO_dh; 1.
DR Pfam; PF00037; Fer4; 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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000070400}.
FT DOMAIN 425..456
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 474..503
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 541 AA; 62142 MW; 275F6F49F9011ED3 CRC64;
MSFKTEPGIY QEARENLKKI REIFGENREK LKENKLAKML CKSSECAEAE NLGIKFADEE
FRNPVWIAAS PITGAKKTKT LEEKIKFLWE LGAGAIVLKS AYLEEEKKEF RMITRDIKAE
MKTRVWREEK PGDRVTLFNT GRTLAETVLP HEIPEVVSGL KKIDVIPSIG SHGYNRKTWK
KLFERLKEGP KLIEVNARHP IRRMIEESRV PSTTQEQLKR LNEYLKDADE YFSSSIPSSF
YGFWSKFREW TRDIHRIGSR NGKKIIIKLP YRSDLNMLAW ICESVEKEFE SKFGIRALTL
INTIKTPYWD YKDYDYPKIP MASGDALTDL RDRSLFYISK VTDLDISASG GIFSAEDILK
CARMGASSVQ LCTSVLYNGF YEIPRRLVEL HEKLGGIIYY QGLRNGKSLI EKSRRTRKPL
LANREVAEID QNACKKCGKC FKTAYCDAIA NRFQDLENLR NQLEGSNKTD LYDTPPDIIP
DRCSGCGLCV LKCPKDAIKL ELKSSKKYEC PICGNEELIE YGTVEKIIYG CEKCGGIFKI
E
//
