ILVC_AZOVD
ID ILVC_AZOVD Reviewed; 338 AA.
AC C1DFH7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:25849365};
DE Short=KARI {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:25849365};
DE EC=1.1.1.86 {ECO:0000255|HAMAP-Rule:MF_00435};
DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000255|HAMAP-Rule:MF_00435};
DE Short=AHIR {ECO:0000255|HAMAP-Rule:MF_00435};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000255|HAMAP-Rule:MF_00435};
DE AltName: Full=Ketol-acid reductoisomerase type 1 {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:25849365};
DE AltName: Full=Ketol-acid reductoisomerase type I {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000303|PubMed:25849365};
GN Name=ilvC {ECO:0000255|HAMAP-Rule:MF_00435}; OrderedLocusNames=Avin_42500;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS,
RP FUNCTION, AND COFACTOR.
RX PubMed=25849365; DOI=10.1042/bj20150183;
RA Cahn J.K., Brinkmann-Chen S., Spatzal T., Wiig J.A., Buller A.R.,
RA Einsle O., Hu Y., Ribbe M.W., Arnold F.H.;
RT "Cofactor specificity motifs and the induced fit mechanism in class I
RT ketol-acid reductoisomerases.";
RL Biochem. J. 468:475-484(2015).
CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids
CC (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction
CC of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In
CC the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl
CC migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the
CC reductase reaction, this 2-ketoacid undergoes a metal-dependent
CC reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
CC {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:25849365}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00435};
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:0000255|HAMAP-Rule:MF_00435};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00435,
CC ECO:0000269|PubMed:25849365};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00435, ECO:0000269|PubMed:25849365};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-
CC Rule:MF_00435}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000255|HAMAP-Rule:MF_00435}.
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DR EMBL; CP001157; ACO80373.1; -; Genomic_DNA.
DR RefSeq; WP_012702741.1; NC_012560.1.
DR PDB; 4XIY; X-ray; 2.50 A; A/B/C/D=1-338.
DR PDBsum; 4XIY; -.
DR AlphaFoldDB; C1DFH7; -.
DR SMR; C1DFH7; -.
DR STRING; 322710.Avin_42500; -.
DR PRIDE; C1DFH7; -.
DR EnsemblBacteria; ACO80373; ACO80373; Avin_42500.
DR KEGG; avn:Avin_42500; -.
DR eggNOG; COG0059; Bacteria.
DR HOGENOM; CLU_033821_0_1_6; -.
DR OMA; RAMFSWL; -.
DR OrthoDB; 188901at2; -.
DR BRENDA; 1.1.1.383; 49.
DR BRENDA; 1.1.1.86; 49.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00435; IlvC; 1.
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; IPR014359; KARI_prok.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21371; PTHR21371; 1.
DR Pfam; PF01450; IlvC; 1.
DR Pfam; PF07991; IlvN; 1.
DR PIRSF; PIRSF000116; IlvC_gammaproteo; 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; Magnesium; Metal-binding; NADP;
KW Oxidoreductase.
FT CHAIN 1..338
FT /note="Ketol-acid reductoisomerase (NADP(+))"
FT /id="PRO_1000206075"
FT DOMAIN 1..181
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT DOMAIN 182..327
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT ACT_SITE 107
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 24..27
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 50
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 82..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435,
FT ECO:0000305|PubMed:25849365"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435,
FT ECO:0000269|PubMed:25849365"
FT BINDING 194
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435,
FT ECO:0000305|PubMed:25849365"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435,
FT ECO:0000269|PubMed:25849365"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435,
FT ECO:0000269|PubMed:25849365"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00435"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 26..37
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 109..112
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4XIY"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 183..196
FT /evidence="ECO:0007829|PDB:4XIY"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 200..215
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:4XIY"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 231..249
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 252..265
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 268..282
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:4XIY"
FT HELIX 312..322
FT /evidence="ECO:0007829|PDB:4XIY"
SQ SEQUENCE 338 AA; 36635 MW; A8336C391F9DE86D CRC64;
MKVYYDKDCD LSIIQSKKVA IIGYGSQGHA HACNLKDSGV DVYVGLRAGS ASVAKAEAHG
LTVKSVKDAV AAADVVMILT PDEFQGRLYK DEIEPNLKKG ATLAFAHGFS IHYNQVVPRA
DLDVIMIAPK APGHTVRSEF VRGGGIPDLI AVYQDASGNA KNLALSYACG VGGGRTGIIE
TTFKDETETD LFGEQAVLCG GCVELVKAGF ETLVEAGYAP EMAYFECLHE LKLIVDLMFE
GGIANMNYSI SNNAEYGEYV TGPEVINEQS RQAMRNALKR IQDGEYAKMF ITEGAANYPS
MTAYRRNNAA HQIEVVGEKL RTMMPWIAAN KIVDKTKN
