(data stored in ACNUC7421 zone)

SWISSPROT: C8W658_DESAS

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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
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
//

If you have problems or comments...

PBIL Back to PBIL home page