ID J2MUM5_9PSED Unreviewed; 424 AA.
AC J2MUM5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=PMI18_02460 {ECO:0000313|EMBL:EJM01709.1};
OS Pseudomonas sp. GM102.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144321 {ECO:0000313|EMBL:EJM01709.1, ECO:0000313|Proteomes:UP000007514};
RN [1] {ECO:0000313|EMBL:EJM01709.1, ECO:0000313|Proteomes:UP000007514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM102 {ECO:0000313|EMBL:EJM01709.1,
RC ECO:0000313|Proteomes:UP000007514};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJM01709.1}.
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DR EMBL; AKJB01000053; EJM01709.1; -; Genomic_DNA.
DR RefSeq; WP_007899509.1; NZ_AKJB01000053.1.
DR AlphaFoldDB; J2MUM5; -.
DR PATRIC; fig|1144321.3.peg.2405; -.
DR Proteomes; UP000007514; 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}.
FT DOMAIN 336..365
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 373..403
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 424 AA; 45939 MW; A8618558CF5A8FA9 CRC64;
MADLSIVFAG IKAPNPFWLA SAPPTDKAYN VVRAFEAGWG GVVWKTLGED PAAVNVSSRY
SAHFGANREV LGFNNIELIT DRSLEINLRE ITQVKKDWPD RALIVSLMVP CVEESWKNIL
PLVEATGADG IELNFGCPHG MPERGMGAAV GQVPEYVEQV TRWCKMYCSL PVIVKLTPNI
TDIRVAARAA HRGGADAVSL INTINSITSV NLERMVANPA VGSQSTHGGY CGSAVKPIAL
NMVAEIARDP QTQGLPISGI GGIGSWRDAA EFIALGSGSV QVCTAAMLHG FRIVEEMKDG
LSRWMDSQGY ASVSEFSGRA VGNTTDWKYL DINYQVIAKI DQQACIGCGR CHIACEDTSH
QAIASLKQAD GTHKYEVIDD ECVGCNLCQI TCPVQDCIEM VPMDTGKPFL DWNHDPRNPY
HITV
//
