ID K5YNA7_9PROT Unreviewed; 423 AA.
AC K5YNA7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=MXAZACID_05896 {ECO:0000313|EMBL:EKN00322.1};
OS Acidocella sp. MX-AZ02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1214225 {ECO:0000313|EMBL:EKN00322.1, ECO:0000313|Proteomes:UP000006217};
RN [1] {ECO:0000313|EMBL:EKN00322.1, ECO:0000313|Proteomes:UP000006217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MX-AZ02 {ECO:0000313|EMBL:EKN00322.1,
RC ECO:0000313|Proteomes:UP000006217};
RX PubMed=23405365;
RA Servin-Garciduenas L.E., Garrett R.A., Amils R., Martinez-Romero E.;
RT "Genome Sequence of the Acidophilic Bacterium Acidocella sp. Strain MX-
RT AZ02.";
RL Genome Announc. 1:E00041-12(2013).
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:EKN00322.1}.
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DR EMBL; AMPS01000071; EKN00322.1; -; Genomic_DNA.
DR RefSeq; WP_008493251.1; NZ_JH976207.1.
DR AlphaFoldDB; K5YNA7; -.
DR STRING; 1214225.MXAZACID_05896; -.
DR PATRIC; fig|1214225.3.peg.1141; -.
DR HOGENOM; CLU_042042_4_2_5; -.
DR Proteomes; UP000006217; 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:EKN00322.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006217}.
FT DOMAIN 334..366
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 370..400
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 423 AA; 45804 MW; 5F376D08F593D479 CRC64;
MADLHIDFAG IKAPNPFWLA SAPPTDKAYN VERAFKAGWG GVVWKTLGED PPVVNVSSRY
GAIGYNGQRL MGMNNIELIT DRPLHLNLDE IRTVKRNWPD RAVVVSLMVP CEEESWKRIL
PLVEATGADG IELNFGCPHG MSERGMGAAV GQVPDYVEMV TRWCKQYSRM PVIVKLTPNI
TDILKPAEAA RRGGADAVSL INTITSITGV DLDNMVPEPA VDGLGTHGGY CGPAVKPIAL
RMVGEIARSL KGLPISGIGG ISSWRDAAEF LALGAGSVQV CTAAMHYGFR IVEDMISGLS
NWMDEKGYAC IEDVTGRAVK NFVHWNDLNL AWKTIASIDP TACIGCGLCH IACEDTAHQA
IKLQETGEKR IYEVIDDECV GCNLCSHVCP VSGCITMVPQ ATATHLTWKQ HPNNPMRVAE
PAQ
//
