ID A0A0M0JUG2_9EUKA Unreviewed; 499 AA.
AC A0A0M0JUG2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Acetohydroxy-acid reductoisomerase {ECO:0000256|ARBA:ARBA00030593};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|ARBA:ARBA00030209};
GN ORFNames=Ctob_006115 {ECO:0000313|EMBL:KOO30155.1};
OS Chrysochromulina tobinii.
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Prymnesiales;
OC Chrysochromulinaceae; Chrysochromulina.
OX NCBI_TaxID=1460289 {ECO:0000313|EMBL:KOO30155.1, ECO:0000313|Proteomes:UP000037460};
RN [1] {ECO:0000313|Proteomes:UP000037460}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP291 {ECO:0000313|Proteomes:UP000037460};
RX PubMed=26397803; DOI=10.1371/journal.pgen.1005469;
RA Hovde B.T., Deodato C.R., Hunsperger H.M., Ryken S.A., Yost W., Jha R.K.,
RA Patterson J., Monnat R.J. Jr., Barlow S.B., Starkenburg S.R.,
RA Cattolico R.A.;
RT "Genome Sequence and Transcriptome Analyses of Chrysochromulina tobin:
RT Metabolic Tools for Enhanced Algal Fitness in the Prominent Order
RT Prymnesiales (Haptophyceae).";
RL PLoS Genet. 11:e1005469-e1005469(2015).
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}.
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:KOO30155.1}.
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DR EMBL; JWZX01002279; KOO30155.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M0JUG2; -.
DR OrthoDB; 1329473at2759; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000037460; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
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 HAMAP; MF_00435; IlvC; 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 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; 2.
DR Pfam; PF07991; IlvN; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
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 Isomerase {ECO:0000313|EMBL:KOO30155.1};
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:UP000037460}.
FT DOMAIN 22..212
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 213..357
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT DOMAIN 358..491
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 393
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 397
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 418
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 499 AA; 54938 MW; 19FE77CC1A8A2000 CRC64;
MPPKRVNYFN TLSMAGKLDQ LARCRFMGRD EFANGMAAIA GKKIVIVGCG AQGLNQGLNM
RDSGCDISYT LRKEAIESKR ASYVNASSNG FTVGTYEQLI PSADLVLNLT PDKQHSSVVS
AIMPMMKKGA TLAYSHGFNI VEEGMQIRPD LTVIMVAPKC PGTEVREEYK RGFGVPTLIA
VHPPNDPRGE GLELAKAYAA ATGGHRAGVL ESSFVAEVKS DLMGEQTILC GMLQSGGLLC
FDKMVSQGID PGYAAKFIQY GWETITEALK HGGVTGMMDR LDNPSKLKAF EIADELKVIM
KPLYDKHQDD IITGHFSKTM MEDWDNDDKN LHKWRAETAE TTFEKTAAGS MIISEQEYFD
HGVLMVAMVK AGVELAFDAM VNVGMRPESA YYESLHETPL IANTIARKKF YEMNRVISDT
AEYGCYLFDQ QCRPLLKDFM AKQKIDVIGT KFNKSGNNSV DNRTMIAVND AIRSHPVEAI
GKELRGYMTG MQKIAVASS
//
