ID B0PC95_9FIRM Unreviewed; 799 AA.
AC B0PC95;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=ANACOL_02404 {ECO:0000313|EMBL:EDS10850.1};
OS Anaerotruncus colihominis DSM 17241.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Anaerotruncus.
OX NCBI_TaxID=445972 {ECO:0000313|EMBL:EDS10850.1, ECO:0000313|Proteomes:UP000003803};
RN [1] {ECO:0000313|EMBL:EDS10850.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10850.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Anaerotruncus colihominis(DSM 17241).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS10850.1, ECO:0000313|Proteomes:UP000003803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17241 {ECO:0000313|EMBL:EDS10850.1,
RC ECO:0000313|Proteomes:UP000003803};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS10850.1}.
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DR EMBL; ABGD02000019; EDS10850.1; -; Genomic_DNA.
DR AlphaFoldDB; B0PC95; -.
DR STRING; 169435.ERS852551_03015; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG0493; Bacteria.
DR HOGENOM; CLU_351854_0_0_9; -.
DR Proteomes; UP000003803; 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; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
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 769..798
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 799 AA; 83622 MW; 438CFF7A0D80B89F CRC64;
MVEDIRIPVK VGGVTFKNPF YVASGPTTKN VRQLQRIEET GWAAASIKLS IDPAPYINRK
PRYGLFDETN ALAFTAEKRL TFQEGLTLIE DAKKVLSDLI LMANITYAGD RGAAGWVNMA
KQFEAVGADI IELNMCCPNM SYNVSLSSGG AASTSQQTGA SLGRQAGVVA EIVRAIKKEI
HIPLFVKLTP EGGEVAQVAA ALYAAGADAV GSTGNRLGLP PIDLNDPGRA VYHLQDEISM
SCYCGSWLKP LAQRDAYEIR KVCGMEPKMM AAGGITDWRS AVEMVLCGGN LLGVCAETLI
SGYDIVRPMI RGLKDYMDTH GYRSIDDFCG KVVSAVRTAP ELTLHDGYAH IREPNLAGPC
KAACPHHVPV QAYVQSIARG DFHHAYELIT GKGVLQGACA YICPHPCEDA CVRGRTGRPV
AIKALKRFVL ELGRAEGWQP TAAQAVQNGR RAAVIGSGPA GLACADELRK AGYAVTIFEQ
AAALGGGLND AVAAGQLPAE NLKALLETIA GSGVELRCGV QADPQRLLED GFAGVCTAVG
RTGVNPWAAL PGGEGVRSVL DMAREQSLCG TAAVIGPPQA AADGARCALH MGAAAAVVIP
TGTMPEKKAA LLRGEGITVL NGYKPAALED GALILSGPAG SRVSLPCGSV WSAQSEEVRL
AAGDGVFTAG GANIIAAAAS GYNAAVRLDQ WVMGEKAVLK PSPRPVPVAA EQVLKRAGYV
GDSPDAPVIA SKEQAIAEAG RCLNCGCGEG CQLCKTICTD FAPLVTGPDQ LAIDRTQCVA
CGMCYNRCPN KNIEMLPIK
//
