ID D2V5Y1_NAEGR Unreviewed; 1038 AA.
AC D2V5Y1;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=dihydropyrimidine dehydrogenase (NADP(+)) {ECO:0000256|ARBA:ARBA00013004};
DE EC=1.3.1.2 {ECO:0000256|ARBA:ARBA00013004};
DE AltName: Full=Dihydrothymine dehydrogenase {ECO:0000256|ARBA:ARBA00032722};
DE AltName: Full=Dihydrouracil dehydrogenase {ECO:0000256|ARBA:ARBA00030119};
GN ORFNames=NAEGRDRAFT_78714 {ECO:0000313|EMBL:EFC47877.1};
OS Naegleria gruberi (Amoeba).
OC Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC Vahlkampfiidae; Naegleria.
OX NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN [1] {ECO:0000313|EMBL:EFC47877.1, ECO:0000313|Proteomes:UP000006671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEG-M {ECO:0000313|EMBL:EFC47877.1,
RC ECO:0000313|Proteomes:UP000006671};
RX PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT "The genome of Naegleria gruberi illuminates early eukaryotic
RT versatility.";
RL Cell 140:631-642(2010).
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004668}.
CC -!- SIMILARITY: Belongs to the dihydropyrimidine dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00010804}.
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DR EMBL; GG738853; EFC47877.1; -; Genomic_DNA.
DR RefSeq; XP_002680621.1; XM_002680575.1.
DR AlphaFoldDB; D2V5Y1; -.
DR STRING; 5762.D2V5Y1; -.
DR EnsemblProtists; EFC47877; EFC47877; NAEGRDRAFT_78714.
DR GeneID; 8861902; -.
DR VEuPathDB; AmoebaDB:NAEGRDRAFT_78714; -.
DR eggNOG; KOG1799; Eukaryota.
DR InParanoid; D2V5Y1; -.
DR OrthoDB; 1211169at2759; -.
DR UniPathway; UPA00131; -.
DR Proteomes; UP000006671; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0017113; F:dihydropyrimidine dehydrogenase (NADP+) activity; IEA:UniProtKB-EC.
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:0019483; P:beta-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd02940; DHPD_FMN; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
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; PF14697; Fer4_21; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 3.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006671};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 69..99
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 935..967
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 969..999
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 1038 AA; 113240 MW; 4C13F9A99B7E7DDA CRC64;
MASSTNFLTL GLEDIENLNL NPKIQKYASV RPSKETEKLK QHYKRNIPIN TKQLKYDFRD
NKHSTLTEKS AIVEASRCLK CADAPCQSSC PTSLDIKSFI SCISTGNYYG AAKMIFSDNP
LGLSCGMVCP VSNLCAGSCN LAATEEGPIN INGLQAFATD VFRKMKLKQI RDPDATPLDK
LPESYKAKIA LVGAGPASIS CATFLARMGY QNVTIFEKGQ YAGGLSTQEI PQNRLPYEAV
EFEVNLMKDL GVKVEYNKEL GRDFTVESLK NDGYEAIFLG IGLPDPNKES IFDGLTPEQG
FYTSKDFLPA VMQSSKDGIC GCKASNQKLP KLYGKVVILG IGDTALDVYG SSIRCGADKA
VLVFRRGFSE MRCVEEEFEP AMKEKCDVLP NCLPKQIIMK DGRISGIELY KTEVDSNGKL
VIDEDQFIRL KCDFVVSAFG CTLKSENIIK SLSPVAVNNY GRVPINNTTM ETEVKGVFAG
GDLIGSGMTV EASNDGKTAS WYIHRYIQEE LHKADRLSDA PQLPKFFTEV DKVDISVEVC
GVKFENPYGL ASAPPCTTAD MIDRAFDAGW GFAVTKTFGL DKDLVTNVSP RIIRGSVTTN
RGPHQSAFMN IELISEKSAT YWCTAITELK KKHPTKIVIA SIMAAFKEED WKFLATKAEQ
AGADMIELNL SCPHGMGEKG LGLACGMDPY LVLNICKWVR AVTKIPFFAK LTPNVTDVLQ
IATAARDGGA DGVTATNTVS GLMTLKPDAT AWPAVGANKR TTYGGVSGNA IRPIAMKAVS
KVAKNIPGYP ILATGGCDSA DVALQFIHAG ASVVQICSSV QNQDFTVIED YITGLKALMY
INAHPAFKGW TGQTPPVVEE KKVGLPRFGP YELKRRELDV KEIEEKGVLT GRHEDNMPAE
IEQVIKVPSI NDVVAKAVPR IGSWGELDPK FDHHVIAVIN DDKCINCGKC YLTCNDSGYQ
AISFDKDTHI PKVSDDDCTG CTLCYSVCPV LDCIEMVPRK TEYKSQRGIA PGEFSQEAVL
KFASLYDSNG SLVSDMHE
//
