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ID C8W658_DESAS Unreviewed; 331 AA.
AC C8W658;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-NOV-2009, sequence version 1.
DT 08-MAY-2019, entry version 74.
DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|HAMAP-Rule:MF_00435};
DE Short=KARI {ECO:0000256|HAMAP-Rule:MF_00435};
DE EC=1.1.1.86 {ECO:0000256|HAMAP-Rule:MF_00435};
DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|HAMAP-Rule:MF_00435};
DE Short=AHIR {ECO:0000256|HAMAP-Rule:MF_00435};
DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase {ECO:0000256|HAMAP-Rule:MF_00435};
GN Name=ilvC {ECO:0000256|HAMAP-Rule:MF_00435};
GN OrderedLocusNames=Dtox_0593 {ECO:0000313|EMBL:ACV61513.1};
OS Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS B-1644) (Desulfofarcimen acetoxidans).
OC Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC Desulfofarcimen.
OX NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61513.1, ECO:0000313|Proteomes:UP000002217};
RN [1] {ECO:0000313|EMBL:ACV61513.1, ECO:0000313|Proteomes:UP000002217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC {ECO:0000313|Proteomes:UP000002217};
RX PubMed=21304664; DOI=10.4056/sigs.39508;
RA Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT (5575).";
RL Stand. Genomic Sci. 1:242-253(2009).
CC -!- FUNCTION: Involved in the biosynthesis of branched-chain amino
CC acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-
CC acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-
CC dihydroxy-isovalerate. In the isomerase reaction, S2AL is
CC rearranged via a Mg-dependent methyl migration to produce 3-
CC hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction,
CC this 2-ketoacid undergoes a metal-dependent reduction by NADPH to
CC yield (R)-2,3-dihydroxy-isovalerate. {ECO:0000256|HAMAP-
CC Rule:MF_00435, ECO:0000256|SAAS:SAAS00992119}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00435,
CC ECO:0000256|SAAS:SAAS01120909};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-
CC 2-ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH;
CC Xref=Rhea:RHEA:13493, ChEBI:CHEBI:15378, ChEBI:CHEBI:49256,
CC ChEBI:CHEBI:49258, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.86; Evidence={ECO:0000256|HAMAP-Rule:MF_00435,
CC ECO:0000256|SAAS:SAAS01120914};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00435};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00435};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000256|HAMAP-
CC Rule:MF_00435, ECO:0000256|SAAS:SAAS00320659}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine
CC from pyruvate: step 2/4. {ECO:0000256|HAMAP-Rule:MF_00435,
CC ECO:0000256|SAAS:SAAS00320673}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
CC ProRule:PRU01198, ECO:0000256|SAAS:SAAS00556475}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}.
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DR EMBL; CP001720; ACV61513.1; -; Genomic_DNA.
DR RefSeq; WP_015756232.1; NC_013216.1.
DR STRING; 485916.Dtox_0593; -.
DR EnsemblBacteria; ACV61513; ACV61513; Dtox_0593.
DR KEGG; dae:Dtox_0593; -.
DR eggNOG; ENOG4105C6M; Bacteria.
DR eggNOG; COG0059; LUCA.
DR HOGENOM; HOG000016230; -.
DR KO; K00053; -.
DR OMA; LDWWKKF; -.
DR OrthoDB; 188901at2; -.
DR BioCyc; DACE485916:G1GFV-599-MONOMER; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000002217; Chromosome.
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: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; 2.
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 3: Inferred from homology;
DR PRODOM; C8W658.
DR SWISS-2DPAGE; C8W658.
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00435,
KW ECO:0000256|PROSITE-ProRule:PRU01198, ECO:0000256|SAAS:SAAS00320664};
KW Branched-chain amino acid biosynthesis {ECO:0000256|HAMAP-
KW Rule:MF_00435, ECO:0000256|PROSITE-ProRule:PRU01198,
KW ECO:0000256|SAAS:SAAS00320675};
KW Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW Isomerase {ECO:0000313|EMBL:ACV61513.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
KW ProRule:PRU01198, ECO:0000256|SAAS:SAAS00825999};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
KW ProRule:PRU01198, ECO:0000256|SAAS:SAAS00825953};
KW NADP {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS00993879};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
KW ProRule:PRU01198, ECO:0000256|SAAS:SAAS00320678,
KW ECO:0000313|EMBL:ACV61513.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002217}.
FT DOMAIN 2 182 KARI N-terminal Rossmann.
FT {ECO:0000259|PROSITE:PS51850}.
FT DOMAIN 183 328 KARI C-terminal knotted.
FT {ECO:0000259|PROSITE:PS51851}.
FT NP_BIND 25 28 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT ACT_SITE 108 108 {ECO:0000256|HAMAP-Rule:MF_00435}.
FT METAL 191 191 Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT MF_00435, ECO:0000256|PROSITE-ProRule:
FT PRU01198}.
FT METAL 191 191 Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT MF_00435, ECO:0000256|PROSITE-ProRule:
FT PRU01198}.
FT METAL 195 195 Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT MF_00435, ECO:0000256|PROSITE-ProRule:
FT PRU01198}.
FT METAL 227 227 Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT MF_00435, ECO:0000256|PROSITE-ProRule:
FT PRU01198}.
FT METAL 231 231 Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT MF_00435, ECO:0000256|PROSITE-ProRule:
FT PRU01198}.
FT BINDING 48 48 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT BINDING 51 51 NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT BINDING 134 134 NADP; via amide nitrogen.
FT {ECO:0000256|HAMAP-Rule:MF_00435}.
FT BINDING 252 252 Substrate. {ECO:0000256|HAMAP-Rule:
FT MF_00435, ECO:0000256|PROSITE-ProRule:
FT PRU01198}.
SQ SEQUENCE 331 AA; 36230 MW; 0DCAB8F0817CC213 CRC64;
MVQVYYDQDA DLSLLAGKKI AVMGYGSQGH AQAQNLKDSG VDVVVGLRRD SKRWAQAEAD
GLAVATVAEA ANQADIIQIL LPDETQAKVY NEEIAPNLSE GNVLMFSHGF NIHFGQIVPP
ANVDVIMVAP KSPGHMVRRM YVDGAGVPCL VAVHQDYSGK AKDIGLAYAK GLGGTKAGVF
ETSFKEETET DLFGEQAVLC GGLCELIQAG FDTLVEAGYA PEMAYFECLH EVKLIVDLIN
EGGLNFMRYS ISNTAEYGDY MTGKRIITEE TRKEMKQVLA EIQNGVFARN WMLENQVNRP
VFNAIKKAQS ESQIEVVGAG LRKMMPWLKK K
//
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