ID A8NTG0_COPC7 Unreviewed; 410 AA.
AC A8NTG0;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Ketol-acid reductoisomerase, mitochondrial {ECO:0000256|PIRNR:PIRNR000119};
DE EC=1.1.1.86 {ECO:0000256|PIRNR:PIRNR000119};
DE AltName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000256|PIRNR:PIRNR000119};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|PIRNR:PIRNR000119};
GN ORFNames=CC1G_06305 {ECO:0000313|EMBL:EAU85592.1};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU85592.1, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU85592.1, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58476; EC=1.1.1.86;
CC Evidence={ECO:0000256|PIRNR:PIRNR000119};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-
CC ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
CC Evidence={ECO:0000256|PIRNR:PIRNR000119};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR000119};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR000119};
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|PIRNR:PIRNR000119}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PIRNR:PIRNR000119,
CC ECO:0000256|PROSITE-ProRule:PRU01198}.
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:EAU85592.1}.
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DR EMBL; AACS02000004; EAU85592.1; -; Genomic_DNA.
DR RefSeq; XP_001836220.1; XM_001836168.2.
DR AlphaFoldDB; A8NTG0; -.
DR STRING; 240176.A8NTG0; -.
DR GeneID; 6012761; -.
DR KEGG; cci:CC1G_06305; -.
DR VEuPathDB; FungiDB:CC1G_06305; -.
DR eggNOG; ENOG502QQBF; Eukaryota.
DR InParanoid; A8NTG0; -.
DR OMA; RAMFSWL; -.
DR OrthoDB; 1090117at2759; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IPR016207; KetolA_reductoisomerase_fun.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00465; ilvC; 1.
DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000119; Ilv5_fungal; 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; 1.
DR PROSITE; PS51850; KARI_N; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PIRNR:PIRNR000119};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|PIRNR:PIRNR000119};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000119};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000119};
KW Mitochondrion {ECO:0000256|PIRNR:PIRNR000119};
KW NADP {ECO:0000256|PIRNR:PIRNR000119};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000119};
KW Reference proteome {ECO:0000313|Proteomes:UP000001861}.
FT DOMAIN 67..257
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 258..405
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 270
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 410 AA; 44896 MW; C686BF4E9CEB76C4 CRC64;
MASIAARSAS QSLRRSLAKA AVRPATQSAK YSLLARAAVN RASAATPAGV SAVQGARGVK
TLDFAGTKET VYERSDWPLP KLQEYFKNDT LAMIGYGSQG HGQSLNARDN GLNVIVGVRE
GGESWKQAIG DGWVPGETLF PIEEAINRGT IIMNLLSDAA QSQTWPELAP LITKGKTLYF
SHGFSVVYKE DTKVVPPKDV DVILVAPKGS GRTVRTLFKE GRGINSSIAV WQDVTGKAKE
KAIALGVAVG SGYMYETTFE KEVYSDLYGE RGVLMGAIQG LFLAQYQVLR KNGHTPSEAF
NETVEEATQS LYPLIGQKGM DYMYNACSTT ARRGALDWAP IFEKANLPIF EQLYESVRNG
TETRKSLEFN GRSTYREDLA KELAVIDNQE IWRAGKVVRS LRPDYKPESE
//
