ID A0A5B0LTQ3_PUCGR Unreviewed; 499 AA.
AC A0A5B0LTQ3;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 05-FEB-2025, entry version 16.
DE SubName: Full=Squalene epoxidase {ECO:0000313|EMBL:KAA1067439.1};
GN Name=ERG1_4 {ECO:0000313|EMBL:KAA1067439.1};
GN Synonyms=ERG1_1 {ECO:0000313|EMBL:KAA1137778.1};
GN ORFNames=PGT21_005560 {ECO:0000313|EMBL:KAA1067439.1}, PGTUg99_016480
GN {ECO:0000313|EMBL:KAA1137778.1};
OS Puccinia graminis f. sp. tritici.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=56615 {ECO:0000313|EMBL:KAA1067439.1, ECO:0000313|Proteomes:UP000324748};
RN [1] {ECO:0000313|Proteomes:UP000324748, ECO:0000313|Proteomes:UP000325313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21-0 {ECO:0000313|EMBL:KAA1067439.1}, and Ug99
RC {ECO:0000313|EMBL:KAA1137778.1, ECO:0000313|Proteomes:UP000325313};
RA Li F., Upadhyaya N.M., Sperschneider J., Matny O., Nguyen-Phuc H., Mago R.,
RA Raley C., Miller M.E., Silverstein K.A.T., Henningsen E., Hirsch C.D.,
RA Visser B., Pretorius Z.A., Steffenson B.J., Schwessinger B., Dodds P.N.,
RA Figueroa M.;
RT "Emergence of the Ug99 lineage of the wheat stem rust pathogen through
RT somatic hybridization.";
RL Submitted (MAY-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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:KAA1067439.1}.
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DR EMBL; VSWC01000184; KAA1067439.1; -; Genomic_DNA.
DR EMBL; VDEP01000005; KAA1137778.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B0LTQ3; -.
DR OrthoDB; 73846at2759; -.
DR Proteomes; UP000324748; Unassembled WGS sequence.
DR Proteomes; UP000325313; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR050838; Ketopantoate_reductase.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 2.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000324748}.
FT DOMAIN 3..169
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 252..345
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT DOMAIN 391..427
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
FT REGION 181..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 55661 MW; 87D6E2DA745B7CA2 CRC64;
MRIHCIGPGS IGSLICFHLQ SITPITLLLR SRQAQHRRSI PTLSIQLEQQ DRTRTATGFT
YEFLNKQQQQ PIESLIVTTK APHVLESLQR VRHRLSANST VLLLHNGLGV VEELIETCFQ
EPSSRPTFVL ATTSHGVYRI DKGLPGTQAG SHGRFCHAGL GDIRLGVLPN TTIRNCLERL
RGHSNQPSSN DDGQNLQDDN PLLNPHSRTK PVLEEHLPDI EPETRSLHYT LSSLLNPLMI
KELNTKWLPM GDFQTSALIK LTVNAAINPI SALLETRNEA LYRESSFESL CRQVCQEASA
VFAAQAGQPF RPHHSLSAPN LQRVVNDIVL ATRANISSMC SDIRTLATNR ISPHKTLSKA
NLNRIAASQA PIKIPNYQSL ISGQEEKSVK ETSTEIDYIN GYICRLGSQF NVDTPLNQSL
SDLVKLKSFA IKRAQVLPKL QRVNRRLKIN RPEDNPATPD QLDLFEKPEN HPGSHQLDLF
EKPENNHLAD NQASVVDKS
//