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ILV5_SPIOL
ID   ILV5_SPIOL              Reviewed;         595 AA.
AC   Q01292;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Ketol-acid reductoisomerase, chloroplastic;
DE            EC=1.1.1.86;
DE   AltName: Full=Acetohydroxy-acid reductoisomerase;
DE   AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase;
DE   Flags: Precursor;
GN   Name=AHRI;
OS   Spinacia oleracea (Spinach).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX   NCBI_TaxID=3562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-88, AND SUBCELLULAR
RP   LOCATION.
RC   TISSUE=Leaf;
RX   PubMed=1713446; DOI=10.1042/bj2770469;
RA   Dumas R., Lebrun M., Douce R.;
RT   "Isolation, characterization and sequence analysis of a full-length cDNA
RT   clone encoding acetohydroxy acid reductoisomerase from spinach
RT   chloroplasts.";
RL   Biochem. J. 277:469-475(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 72-595 IN COMPLEX WITH NADPH AND
RP   MAGNESIUM IONS, AND SUBUNIT.
RX   PubMed=9218783; DOI=10.1093/emboj/16.12.3405;
RA   Biou V., Dumas R., Cohen-Addad C., Douce R., Job D., Pebay-Peyroula E.;
RT   "The crystal structure of plant acetohydroxy acid isomeroreductase
RT   complexed with NADPH, two magnesium ions and a herbicidal transition state
RT   analog determined at 1.65-A resolution.";
RL   EMBO J. 16:3405-3415(1997).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 72-595 IN COMPLEX WITH NADPH AND
RP   MAGNESIUM IONS, AND SUBUNIT.
RX   PubMed=10739911; DOI=10.1107/s0907444900001694;
RA   Thomazeau K., Dumas R., Halgand F., Forest E., Douce R., Biou V.;
RT   "Structure of spinach acetohydroxyacid isomeroreductase complexed with its
RT   reaction product dihydroxymethylvalerate, manganese and (phospho)-ADP-
RT   ribose.";
RL   Acta Crystallogr. D 56:389-397(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-
CC         acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:58476; EC=1.1.1.86;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-
CC         ethyl-2-hydroxy-3-oxobutanoate + H(+) + NADPH; Xref=Rhea:RHEA:13493,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:49256, ChEBI:CHEBI:49258,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.86;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds 2 magnesium ions per subunit.;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC       isoleucine from 2-oxobutanoate: step 2/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 2/4.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10739911,
CC       ECO:0000269|PubMed:9218783}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000269|PubMed:1713446}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000305}.
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DR   EMBL; X57073; CAA40356.1; -; mRNA.
DR   PIR; S17180; S17180.
DR   PDB; 1QMG; X-ray; 1.60 A; A/B/C/D=72-595.
DR   PDB; 1YVE; X-ray; 1.65 A; I/J/K/L=72-595.
DR   PDBsum; 1QMG; -.
DR   PDBsum; 1YVE; -.
DR   AlphaFoldDB; Q01292; -.
DR   SMR; Q01292; -.
DR   BRENDA; 1.1.1.86; 5812.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   EvolutionaryTrace; Q01292; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 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; IPR016206; KetolA_reductoisomerase_plant.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR21371; PTHR21371; 1.
DR   Pfam; PF01450; IlvC; 2.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000118; Ilv5_plant; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS51851; KARI_C; 2.
DR   PROSITE; PS51850; KARI_N; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis;
KW   Branched-chain amino acid biosynthesis; Chloroplast;
KW   Direct protein sequencing; Magnesium; Metal-binding; NADP; Oxidoreductase;
KW   Plastid; Transit peptide.
FT   TRANSIT         1..72
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000269|PubMed:1713446"
FT   CHAIN           73..595
FT                   /note="Ketol-acid reductoisomerase, chloroplastic"
FT                   /id="PRO_0000015631"
FT   DOMAIN          108..306
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01197"
FT   DOMAIN          307..455
FT                   /note="KARI C-terminal knotted 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   DOMAIN          456..592
FT                   /note="KARI C-terminal knotted 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   ACT_SITE        226
FT                   /evidence="ECO:0000255"
FT   BINDING         129..136
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10739911,
FT                   ECO:0000269|PubMed:9218783"
FT   BINDING         162..167
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10739911,
FT                   ECO:0000269|PubMed:9218783"
FT   BINDING         201..205
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000269|PubMed:10739911,
FT                   ECO:0000269|PubMed:9218783"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         315
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         492
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         496
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   BINDING         518
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01198"
FT   STRAND          91..93
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           112..117
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           118..121
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   TURN            122..124
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           136..150
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          156..161
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           168..173
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           178..180
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           186..191
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           202..215
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          221..227
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           228..235
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          244..253
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           255..265
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   TURN            266..269
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          275..281
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          283..285
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           287..297
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          301..305
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           308..320
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   TURN            321..324
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           325..340
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           345..350
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           353..357
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           359..366
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           369..374
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           378..408
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           410..420
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           440..450
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           462..482
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           486..493
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           495..499
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           502..514
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           519..538
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           540..545
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           552..560
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           563..571
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   STRAND          586..588
FT                   /evidence="ECO:0007829|PDB:1QMG"
FT   HELIX           590..592
FT                   /evidence="ECO:0007829|PDB:1QMG"
SQ   SEQUENCE   595 AA;  63754 MW;  B0EE9055097CFBA5 CRC64;
     MAATAATTFS LSSSSSTSAA ASKALKQSPK PSALNLGFLG SSSTIKACRS LKAARVLPSG
     ANGGGSALSA QMVSAPSINT PSATTFDFDS SVFKKEKVTL SGHDEYIVRG GRNLFPLLPD
     AFKGIKQIGV IGWGSQAPAQ AQNLKDSLTE AKSDVVVKIG LRKGSNSFAE ARAAGFSEEN
     GTLGDMWETI SGSDLVLLLI SDSAQADNYE KVFSHMKPNS ILGLSHGFLL GHLQSLGQDF
     PKNISVIAVC PKGMGPSVRR LYVQGKEVNG AGINSSFAVH QDVDGRATDV ALGWSIALGS
     PFTFATTLEQ EYKSDIFGER GILLGAVHGI VECLFRRYTE SGMSEDLAYK NTVECITGVI
     SKTISTKGML ALYNSLSEEG KKDFQAAYSA SYYPSMDILY ECYEDVASGS EIRSVVLAGR
     RFYEKEGLPA FPMGKIDQTR MWKVGEKVRS VRPAGDLGPL YPFTAGVYVA LMMAQIEILR
     KKGHSYSEII NESVIEAVDS LNPFMHARGV SFMVDNCSTT ARLGSRKWAP RFDYILSQQA
     LVAVDNGAPI NQDLISNFLS DPVHEAIGVC AQLRPSVDIS VTADADFVRP ELRQA
 
 
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