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Database: UniProt
Entry: G4YE49_PHYSP
LinkDB: G4YE49_PHYSP
Original site: G4YE49_PHYSP 
ID   G4YE49_PHYSP            Unreviewed;       515 AA.
AC   G4YE49;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000256|ARBA:ARBA00030593};
DE   AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|ARBA:ARBA00030209};
GN   ORFNames=PHYSODRAFT_537835 {ECO:0000313|EMBL:EGZ29630.1};
OS   Phytophthora sojae (strain P6497) (Soybean stem and root rot agent)
OS   (Phytophthora megasperma f. sp. glycines).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1094619 {ECO:0000313|EMBL:EGZ29630.1, ECO:0000313|Proteomes:UP000002640};
RN   [1] {ECO:0000313|EMBL:EGZ29630.1, ECO:0000313|Proteomes:UP000002640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P6497 {ECO:0000313|EMBL:EGZ29630.1,
RC   ECO:0000313|Proteomes:UP000002640};
RX   PubMed=16946064; DOI=10.1126/science.1128796;
RA   Tyler B.M., Tripathy S., Zhang X., Dehal P., Jiang R.H., Aerts A.,
RA   Arredondo F.D., Baxter L., Bensasson D., Beynon J.L., Chapman J.,
RA   Damasceno C.M., Dorrance A.E., Dou D., Dickerman A.W., Dubchak I.L.,
RA   Garbelotto M., Gijzen M., Gordon S.G., Govers F., Grunwald N.J., Huang W.,
RA   Ivors K.L., Jones R.W., Kamoun S., Krampis K., Lamour K.H., Lee M.K.,
RA   McDonald W.H., Medina M., Meijer H.J., Nordberg E.K., Maclean D.J.,
RA   Ospina-Giraldo M.D., Morris P.F., Phuntumart V., Putnam N.H., Rash S.,
RA   Rose J.K., Sakihama Y., Salamov A.A., Savidor A., Scheuring C.F.,
RA   Smith B.M., Sobral B.W., Terry A., Torto-Alalibo T.A., Win J., Xu Z.,
RA   Zhang H., Grigoriev I.V., Rokhsar D.S., Boore J.L.;
RT   "Phytophthora genome sequences uncover evolutionary origins and mechanisms
RT   of pathogenesis.";
RL   Science 313:1261-1266(2006).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4.
CC       {ECO:0000256|ARBA:ARBA00004885}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PROSITE-ProRule:PRU01198}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01198}.
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DR   EMBL; JH159151; EGZ29630.1; -; Genomic_DNA.
DR   RefSeq; XP_009516905.1; XM_009518610.1.
DR   AlphaFoldDB; G4YE49; -.
DR   STRING; 1094619.G4YE49; -.
DR   EnsemblProtists; EGZ29630; EGZ29630; PHYSODRAFT_537835.
DR   GeneID; 20662331; -.
DR   KEGG; psoj:PHYSODRAFT_537835; -.
DR   InParanoid; G4YE49; -.
DR   OMA; FKNTVEC; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000002640; Unassembled WGS sequence.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
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; IPR013023; KARI.
DR   InterPro; IPR000506; KARI_C.
DR   InterPro; IPR013116; KARI_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01450; IlvC; 2.
DR   Pfam; PF07991; IlvN; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51851; KARI_C; 2.
DR   PROSITE; PS51850; KARI_N; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PROSITE-ProRule:PRU01198};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|PROSITE-ProRule:PRU01198};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PROSITE-
KW   ProRule:PRU01198};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01198};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|PROSITE-
KW   ProRule:PRU01198}; Reference proteome {ECO:0000313|Proteomes:UP000002640}.
FT   DOMAIN          50..250
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          247..389
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   DOMAIN          401..515
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         255
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         259
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         424
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         428
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         450
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ   SEQUENCE   515 AA;  56446 MW;  B7DA477AFBAAC5A3 CRC64;
     MRLFLKSAMR ASSPLLKSRS FATNASELRS VVFKDHLRTV QMADAKETVL PGGRDLFPLL
     PKAFAGIKQV GVIGWGSQGP AQAQNLRESL EGSDIKVKVG LREGSSSFAK AQDAGFSEAD
     GTLGEMFDVI KESDMVVLLI SDAACVNLYS KIFPLIKPGA TLGLSHGYLL GHLESVKEEF
     PKDINVVMMA PKGMGPSVRR LYVQGKTVNG AGINSSVAIH QDVTGNAAEI ALGWSVGVGA
     PYTFYTTMSS EYKSDIFGER CILLGGVHGL VESLFRRYVQ NGMSPEDAFK NTAECITGPL
     NEKISHDGIK SVYESFKGED KIIFEKAYTA AYTPCRDIIE EVYDDVACGN EIRSVNNAVA
     RHDRFPFGKI DQTYTWKVGE KVRAARDGNF VMNPFTAGSY VAMMMAQIDV LISHGHCYSE
     VANESVIESV DSLNPYMHAR GVAYMVDNCS TTARLGSRKW APRFDYILTE QAYVAVDDNK
     IKNEAKIMSE FKNHKIHEVL EVCASMRPSV DISVE
//
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