(data stored in SCRATCH zone)

SWISSPROT: D3VHW4_XENNA

ID   D3VHW4_XENNA            Unreviewed;       492 AA.
AC   D3VHW4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 70.
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   ECO:0000313|EMBL:CBJ88453.1};
GN   OrderedLocusNames=XNC1_0376 {ECO:0000313|EMBL:CBJ88453.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88453.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88453.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:SAAS01086624}.
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:SAAS01121798};
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:SAAS01121803};
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|PROSITE-ProRule:PRU01198}.
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; FN667742; CBJ88453.1; -; Genomic_DNA.
DR   RefSeq; WP_013183245.1; NC_014228.1.
DR   STRING; 406817.XNC1_0376; -.
DR   EnsemblBacteria; CBJ88453; CBJ88453; XNC1_0376.
DR   KEGG; xne:XNC1_0376; -.
DR   eggNOG; ENOG4105C6M; Bacteria.
DR   eggNOG; COG0059; LUCA.
DR   HOGENOM; HOG000286135; -.
DR   KO; K00053; -.
DR   OMA; KLFEMNR; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000008075; 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:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1040.10; -; 1.
DR   HAMAP; MF_00435; IlvC; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
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; 2.
DR   Pfam; PF01450; IlvC; 2.
DR   Pfam; PF07991; IlvN; 1.
DR   SUPFAM; SSF48179; SSF48179; 2.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00465; ilvC; 1.
DR   PROSITE; PS51851; KARI_C; 2.
DR   PROSITE; PS51850; KARI_N; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VHW4.
DR   SWISS-2DPAGE; D3VHW4.
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:UP000008075};
KW   Isomerase {ECO:0000313|EMBL:CBJ88453.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
KW   ProRule:PRU01198, ECO:0000256|SAAS:SAAS01086597};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
KW   ProRule:PRU01198, ECO:0000256|SAAS:SAAS01086598};
KW   NADP {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|SAAS:SAAS01086686};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00435, ECO:0000256|PROSITE-
KW   ProRule:PRU01198, ECO:0000256|SAAS:SAAS00320678,
KW   ECO:0000313|EMBL:CBJ88453.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Repeat {ECO:0000256|SAAS:SAAS01086595}.
FT   DOMAIN       15    208       KARI N-terminal Rossmann.
FT                                {ECO:0000259|PROSITE:PS51850}.
FT   DOMAIN      209    340       KARI C-terminal knotted.
FT                                {ECO:0000259|PROSITE:PS51851}.
FT   DOMAIN      345    485       KARI C-terminal knotted.
FT                                {ECO:0000259|PROSITE:PS51851}.
FT   NP_BIND      45     48       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   NP_BIND     108    110       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   ACT_SITE    132    132       {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   METAL       217    217       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435, ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
FT   METAL       217    217       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435, ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
FT   METAL       221    221       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435, ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
FT   METAL       389    389       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435, ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
FT   METAL       393    393       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435, ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
FT   BINDING      68     68       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING      76     76       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING      78     78       NADP. {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING     158    158       NADP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00435}.
FT   BINDING     278    278       Substrate. {ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
FT   BINDING     414    414       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00435, ECO:0000256|PROSITE-ProRule:
FT                                PRU01198}.
SQ   SEQUENCE   492 AA;  54222 MW;  4AFF68BCA7987172 CRC64;
     MANYFDTLNL RQQLAQLGKC RFMAREEFAD EAGYLKGKKV VIVGCGAQGL NQGLNMRDSG
     LDIAYALRKE AIEEKRASWR KATENGFRVG TYEELIPQAD LVINLTPDKQ HSSVVRAVQP
     LMKEGAALGY SHGFNIVEVG EQIRKDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
     NDVKGEGMAI AKAWVAATGG HRAGVLESSF VAEVKSDLMG EQTILCGMLQ AGSLLCYDKL
     VADGAEPSYA GKLIQFGWET ITEALKQGGI TLMMDRLSNS AKLRAYALAE QLKTLLAPLF
     QKHMDDIISG AFSSTMMADW ANDDKNLLTW REETGKTPFE NYPDYSGNIS EQEYFDHGVL
     MIAMVKAGVE LAFDTMIDAG IIEESAYYES LHELPLIANT IARKRLYEMN VVISDTAEYG
     NYLFSHIAVP LLKEKFMATL QAGDLGKEVA DSGIDNAQLR DVNEAIRHHP IETIGHTLRG
     YMTDMKRIAV GG
//

If you have problems or comments...

PBIL Back to PBIL home page