(data stored in ACNUC7421 zone)

SWISSPROT: D1CDV4_THET1

ID   D1CDV4_THET1            Unreviewed;       335 AA.
AC   D1CDV4;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, 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=Tter_0188 {ECO:0000313|EMBL:ACZ41110.1};
OS   Thermobaculum terrenum (strain ATCC BAA-798 / YNP1).
OC   Bacteria; Thermobaculum.
OX   NCBI_TaxID=525904 {ECO:0000313|EMBL:ACZ41110.1, ECO:0000313|Proteomes:UP000000323};
RN   [1] {ECO:0000313|EMBL:ACZ41110.1, ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   PubMed=21304745;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Del Rio T.G., Nolan M.,
RA   Tice H., Han C., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Ovchinnikova G., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Lu M., Brettin T.,
RA   Detter J.C., Goker M., Tindall B.J., Beck B., McDermott T.R.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Cheng J.F.;
RT   "Complete genome sequence of 'Thermobaculum terrenum' type strain
RT   (YNP1).";
RL   Stand. Genomic Sci. 3:153-162(2010).
RN   [2] {ECO:0000313|Proteomes:UP000000323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-798 / YNP1 {ECO:0000313|Proteomes:UP000000323};
RX   DOI=10.4056/sigs.1153107;
RA   Kiss H., Cleland D., Lapidus A., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y., Jeffries C., Lu M.,
RA   Brettin T., Detter J., Goker M., Tindall B., Beck B., McDermott T.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA   Kyrpides N., Klenk H., Cheng J.;
RT   "Complete genome sequence of Thermobaculum terrenum type strain
RT   (YNP1T).";
RL   Stand. Genomic Sci. 3:153-162(2010).
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; CP001825; ACZ41110.1; -; Genomic_DNA.
DR   RefSeq; WP_012874145.1; NC_013525.1.
DR   STRING; 525904.Tter_0188; -.
DR   EnsemblBacteria; ACZ41110; ACZ41110; Tter_0188.
DR   KEGG; ttr:Tter_0188; -.
DR   eggNOG; ENOG4105C6M; Bacteria.
DR   eggNOG; COG0059; LUCA.
DR   HOGENOM; HOG000016230; -.
DR   KO; K00053; -.
DR   OMA; RAMFSWL; -.
DR   OrthoDB; 188901at2; -.
DR   BioCyc; TTER525904:G1GGS-192-MONOMER; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000000323; Chromosome 1.
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; D1CDV4.
DR   SWISS-2DPAGE; D1CDV4.
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:UP000000323};
KW   Isomerase {ECO:0000313|EMBL:ACZ41110.1};
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:ACZ41110.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000323}.
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      51     51       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING      53     53       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   335 AA;  36998 MW;  2F60AC6E26ABC78B CRC64;
     MAQVYYDADA DINVIKDKLI AIIGYGSQGH AHALNLHDSG CNVIVGLHEG SKSAEKARND
     GLEVRSVAEA AEAADIIMML IPDTIHKKVY EESIAPAMRA GKTLMFAHGF SIHYGQVKPP
     AEVDVVMVAP KSPGHIMRNL FTQGIGVPAL LAVYQDASGQ AEQTGLAYAK GLGCTRAGVL
     KTTFKEETET DLFGEQTVLC GGVSALIKAG FETLVEAGYQ PEIAYFECLN EMKLIVDLIY
     QGGLSYMRYS ISDTAEYGDY VAGPRIIDEH VRENMKQILK EIQDGSFARR WIEENEKGRP
     EFEKMREQDR NHLIEQVGQK LRAMMSWTQP QPANR
//

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