ID A0A1R3JVQ7_COCAP Unreviewed; 590 AA.
AC A0A1R3JVQ7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Ketol-acid reductoisomerase {ECO:0000256|PIRNR:PIRNR000118};
DE EC=1.1.1.86 {ECO:0000256|PIRNR:PIRNR000118};
DE AltName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000256|PIRNR:PIRNR000118};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|PIRNR:PIRNR000118};
GN ORFNames=CCACVL1_04016 {ECO:0000313|EMBL:OMO98861.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO98861.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO98861.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO98861.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:PIRNR000118};
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:PIRNR000118};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRNR:PIRNR000118};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR000118};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004885, ECO:0000256|PIRNR:PIRNR000118}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864,
CC ECO:0000256|PIRNR:PIRNR000118}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|PIRNR:PIRNR000118}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PIRNR:PIRNR000118,
CC ECO:0000256|PROSITE-ProRule:PRU01198}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {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:OMO98861.1}.
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DR EMBL; AWWV01006979; OMO98861.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JVQ7; -.
DR STRING; 210143.A0A1R3JVQ7; -.
DR EnsemblPlants; OMO98861; OMO98861; CCACVL1_04016.
DR Gramene; OMO98861; OMO98861; CCACVL1_04016.
DR OMA; FKNTVEC; -.
DR OrthoDB; 1090117at2759; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000188268; 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; IPR016206; KetolA_reductoisomerase_plant.
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 PIRSF; PIRSF000118; Ilv5_plant; 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|PIRNR:PIRNR000118};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|PIRNR:PIRNR000118};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRNR:PIRNR000118};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR000118}; NADP {ECO:0000256|PIRNR:PIRNR000118};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000118};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268}.
FT DOMAIN 101..299
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 300..448
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT DOMAIN 449..585
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-1"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-2,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-2,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR000118-2,
FT ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 370
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 511
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 590 AA; 63742 MW; 7B05AEBFD96612A1 CRC64;
MAAATSFSAS ISTSTPSLNP PSKTHKALAT SSSLGFLASA SRSLRSLKSS RLSTGNGCGS
AMAARMVSSA PAVKAPTSLD FETSVFKKEK VSLAGHEEYI VRGGRDLFKL LPDAFKGIKQ
IGVIGWGSQG PAQAQNLRDS LAEAKSDIVV KVGLRKGSRS FAEARAAGFS EENGTLGDIW
ETISGSDLVL LLISDAAQAD NYEKIFSHMK PNSILGLSHG FLLGHLQSMG LDFPKNFSVI
AVCPKGMGPS VRRLYVQGKE INGAGINSSF GVHQDVDGRA TDVALGWSVA LGSPFTFATT
LEQEYKSDIF GERGILLGAV HGLVECLFRR YTENGMSEED AYKNTVECVT GIISKTISTQ
GMLSVYNSFS EEDKKEFEAA YSASYYPCMD ILYECYEDVA SGSEVRSVVL AGQRFYEKEG
LPAFPMGKID QTRMWKVGER VRKTRPAGDL GPLYPFTAGV YVALMMAQIE ILRKKGHSYS
EIINESVIEA VDSLNPFMHA RGVSFMVDNC STTARLGSRK WAPRFDYILT QQALVAVDNG
APINQDLISN FLSDPVHGAI EVCAQLRPTV DISVPPDADF VRPELRQSGN
//
