(data stored in SCRATCH zone)

SWISSPROT: D7A248_STAND

ID   D7A248_STAND            Unreviewed;       339 AA.
AC   D7A248;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 64.
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=Snov_0330 {ECO:0000313|EMBL:ADH87664.1};
OS   Starkeya novella (strain ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 /
OS   NBRC 12443 / NCIB 9113).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Xanthobacteraceae; Starkeya.
OX   NCBI_TaxID=639283 {ECO:0000313|EMBL:ADH87664.1, ECO:0000313|Proteomes:UP000006633};
RN   [1] {ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Brettin T., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Beatson S., Kappler U.,
RA   Woyke T.;
RT   "Complete sequence of Starkeya novella DSM 506.";
RL   Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADH87664.1, ECO:0000313|Proteomes:UP000006633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8093 / DSM 506 / CCM 1077 / IAM 12100 / NBRC 12443 / NCIB
RC   9113 {ECO:0000313|Proteomes:UP000006633};
RX   PubMed=23450099; DOI=10.4056/sigs.3006378;
RA   Kappler U., Davenport K., Beatson S., Lucas S., Lapidus A.,
RA   Copeland A., Berry K.W., Glavina Del Rio T., Hammon N., Dalin E.,
RA   Tice H., Pitluck S., Richardson P., Bruce D., Goodwin L.A., Han C.,
RA   Tapia R., Detter J.C., Chang Y.J., Jeffries C.D., Land M., Hauser L.,
RA   Kyrpides N.C., Goker M., Ivanova N., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of the facultatively chemolithoautotrophic
RT   and methylotrophic alpha Proteobacterium Starkeya novella type strain
RT   (ATCC 8093(T)).";
RL   Stand. Genomic Sci. 7:44-58(2012).
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; CP002026; ADH87664.1; -; Genomic_DNA.
DR   RefSeq; WP_013165169.1; NC_014217.1.
DR   STRING; 639283.Snov_0330; -.
DR   EnsemblBacteria; ADH87664; ADH87664; Snov_0330.
DR   KEGG; sno:Snov_0330; -.
DR   eggNOG; ENOG4105C6M; Bacteria.
DR   eggNOG; COG0059; LUCA.
DR   HOGENOM; HOG000016230; -.
DR   KO; K00053; -.
DR   OMA; RAMFSWL; -.
DR   OrthoDB; 188901at2; -.
DR   BioCyc; SNOV639283:G1GLM-334-MONOMER; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000006633; 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; D7A248.
DR   SWISS-2DPAGE; D7A248.
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:UP000006633};
KW   Isomerase {ECO:0000313|EMBL:ADH87664.1};
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:ADH87664.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006633}.
FT   DOMAIN        1    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      24     27       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      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   339 AA;  36729 MW;  E3791636A82026E9 CRC64;
     MRVYYDRDAD LNLVKGKKVA IIGYGSQGRA HALNLKDSGV KDIAIGLKPG SATAKKVEAD
     GLKVMSVAEA AKWADLMMMA TPDELQADIY KNEIAPNIRD GAAIAFAHGL NVHFGLIEPK
     STVDVLMIAP KGPGHTVRGE YEKGGGVPCL VAVHQDASGN ALDLGLSYAS GVGGGRSGII
     ETTFKEECET DLFGEQVVLC GGLVELIRAG FETLVEAGYA PEMAYFECLH EVKLIVDLIY
     EGGIANMNYS ISNTAEWGEY VSGPRIITAE TKAEMKRVLT DIQTGKFTSE WMQEYRAGAA
     RFKGIRRIND AHQIEEVGEK LRGMMPWIGK NKLVDKTKN
//

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