ILVC2_SACS2
ID ILVC2_SACS2 Reviewed; 333 AA.
AC Q97YJ9;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2001, sequence version 1.
DT 25-MAY-2022, entry version 122.
DE RecName: Full=Putative ketol-acid reductoisomerase 2;
DE EC=1.1.1.86;
DE AltName: Full=Acetohydroxy-acid isomeroreductase 2;
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase 2;
GN Name=ilvC2; Synonyms=ilvC-2; OrderedLocusNames=SSO1322;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000305}.
CC -!- CAUTION: Ser-107 is present instead of the conserved His which is
CC expected to be an active site residue. {ECO:0000305}.
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DR EMBL; AE006641; AAK41560.1; -; Genomic_DNA.
DR PIR; A99288; A99288.
DR RefSeq; WP_010923317.1; NC_002754.1.
DR PDB; 6JCV; EM; 2.92 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6JCW; EM; 3.04 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6JCZ; EM; 3.35 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6JD1; EM; 3.38 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6JD2; X-ray; 2.53 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KOU; EM; 2.43 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KPA; EM; 2.75 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KPE; EM; 2.83 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KPH; EM; 2.41 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KPI; EM; 2.43 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KPJ; EM; 2.56 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KPK; EM; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KQ4; EM; 2.30 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KQ8; EM; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KQJ; EM; 2.54 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KQK; EM; 2.17 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDB; 6KQO; EM; 2.52 A; A/B/C/D/E/F/G/H/I/J/K/L=1-333.
DR PDBsum; 6JCV; -.
DR PDBsum; 6JCW; -.
DR PDBsum; 6JCZ; -.
DR PDBsum; 6JD1; -.
DR PDBsum; 6JD2; -.
DR PDBsum; 6KOU; -.
DR PDBsum; 6KPA; -.
DR PDBsum; 6KPE; -.
DR PDBsum; 6KPH; -.
DR PDBsum; 6KPI; -.
DR PDBsum; 6KPJ; -.
DR PDBsum; 6KPK; -.
DR PDBsum; 6KQ4; -.
DR PDBsum; 6KQ8; -.
DR PDBsum; 6KQJ; -.
DR PDBsum; 6KQK; -.
DR PDBsum; 6KQO; -.
DR AlphaFoldDB; Q97YJ9; -.
DR SMR; Q97YJ9; -.
DR STRING; 273057.SSO1322; -.
DR EnsemblBacteria; AAK41560; AAK41560; SSO1322.
DR GeneID; 27427693; -.
DR KEGG; sso:SSO1322; -.
DR PATRIC; fig|273057.12.peg.1324; -.
DR eggNOG; arCOG04465; Archaea.
DR HOGENOM; CLU_033821_0_1_2; -.
DR InParanoid; Q97YJ9; -.
DR OMA; QATIMRE; -.
DR PhylomeDB; Q97YJ9; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IBA:GO_Central.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0009099; P:valine biosynthetic process; IBA:GO_Central.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
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; PTHR21371; 1.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR SUPFAM; SSF48179; SSF48179; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR00465; ilvC; 1.
DR PROSITE; PS51851; KARI_C; 1.
DR PROSITE; PS51850; KARI_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; NADP; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..333
FT /note="Putative ketol-acid reductoisomerase 2"
FT /id="PRO_0000151401"
FT DOMAIN 1..182
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 183..329
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:6KPH"
FT TURN 12..15
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:6KQK"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:6JD1"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:6KPA"
FT HELIX 64..70
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 134..140
FT /evidence="ECO:0007829|PDB:6KQK"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:6KQK"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 184..196
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 198..217
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:6KQK"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:6KPJ"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 248..252
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 255..284
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 287..298
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 301..311
FT /evidence="ECO:0007829|PDB:6KQK"
FT HELIX 314..325
FT /evidence="ECO:0007829|PDB:6KQK"
SQ SEQUENCE 333 AA; 37185 MW; D37083F704B95CA0 CRC64;
MDKTVLDANL DPLKGKTIGV IGYGNQGRVQ ATIMRENGLN VIVGNVKDKY YELAKKEGFE
VYEIDEAVRR SDVALLLIPD EVMKEVYEKK IAPVLQGKKE FVLDFASGYN VAFGLIRPPK
SVDTIMVAPR MVGEGIMDLH KQGKGYPVLL GVKQDASGKA WDYAKAIAKG IGAIPGGIAV
ISSFEEEALL DLMSEHTWVP ILFGAIKACY DIAVKEYGVS PEAALLEFYA SGELAEIARL
IAEEGIFNQM VHHSTTSQYG TLTRMFKYYD VVRRIVENEA KYIWDGSFAK EWSLEQQAGY
PVFYRLWELA TQSEMAKAEK ELYKLLGRKV KND
