ID Q2CK19_OCEGH Unreviewed; 434 AA.
AC Q2CK19;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=OG2516_10921 {ECO:0000313|EMBL:EAR52970.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR52970.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR52970.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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:EAR52970.1}.
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DR EMBL; AAOT01000001; EAR52970.1; -; Genomic_DNA.
DR RefSeq; WP_007255704.1; NZ_CH724107.1.
DR AlphaFoldDB; Q2CK19; -.
DR STRING; 314256.OG2516_10921; -.
DR eggNOG; COG0167; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_042042_4_2_5; -.
DR OrthoDB; 9794954at2; -.
DR Proteomes; UP000003635; 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:EAR52970.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003635}.
FT DOMAIN 338..370
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 371..401
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 434 AA; 47206 MW; 2542BBC0FF7136FB CRC64;
MADLTTDFVG IKSPNPFWLA SAPPTDKEYN VRRAFEAGWG GVVWKTLGAE GPPVVNVNGP
RYGAIYGADR RLLGLNNIEL ITDRPLEVNL EEMARVKADY PDRALIASIM VPCEEAAWKA
ILPRVAETGA DGIELNFGCP HGMSERGMGS AVGQVPEYIE MVVRWCKQYY DRPVIVKLTP
NITDIRKPAT AAKNGGADAV SLINTINSIT GVDLDNFAPM PTIDGKGSHG GYCGPAVKPI
AMSMVSEIAR NPETRGLPIS GIGGITTWRD AAEFMALGCG NVQVCTAAMT YGFKIVEEMT
RDLSAWMDEK GYRSTADFVG KAVPNVTDWQ YLNLNYVTKA RIDQDLCIKC GRCYAACEDT
SHQAIAFNPG RTFEVIDEEC VACNLCVDVC PVEDCITMVE LDDGTVDPRT GKVVQKEYAN
WTTHPNNPMA KAAE
//
