UniProt: A0A099W7D4

Database: UniProt
Entry: A0A099W7D4_9LIST

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Original site:  A0A099W7D4_9LIST

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (39)   
   EMBL (39)   
Protein domain (10)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (2)   
All databases (58)   

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ID   A0A099W7D4_9LIST        Unreviewed;       331 AA.
AC   A0A099W7D4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 53.
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:MBC1226059.1};
GN   ORFNames=EP57_09015 {ECO:0000313|EMBL:KGL40686.1}, HB759_02350
GN   {ECO:0000313|EMBL:MBC1330782.1}, HB809_02355
GN   {ECO:0000313|EMBL:MBC1306539.1}, HB810_03865
GN   {ECO:0000313|EMBL:MBC1245722.1}, HB811_02495
GN   {ECO:0000313|EMBL:MBC1315632.1}, HB816_01505
GN   {ECO:0000313|EMBL:MBC1229128.1}, HB817_03000
GN   {ECO:0000313|EMBL:MBC1226059.1}, HB818_03150
GN   {ECO:0000313|EMBL:MBC1284758.1}, HB847_04330
GN   {ECO:0000313|EMBL:MBC1371588.1}, HB856_03085
GN   {ECO:0000313|EMBL:MBC1357185.1}, HB900_03940
GN   {ECO:0000313|EMBL:MBC1573596.1}, HB902_01090
GN   {ECO:0000313|EMBL:MBC1560646.1}, HB907_03320
GN   {ECO:0000313|EMBL:MBC1564419.1}, HBP98_11060
GN   {ECO:0000313|EMBL:MBC2372539.1}, HCA46_03405
GN   {ECO:0000313|EMBL:MBC1777873.1}, HCA52_01095
GN   {ECO:0000313|EMBL:MBC1791996.1}, HCA55_00860
GN   {ECO:0000313|EMBL:MBC1795247.1}, HCA67_01055
GN   {ECO:0000313|EMBL:MBC2066339.1}, HCA68_05795
GN   {ECO:0000313|EMBL:MBC1897186.1}, HCA72_03855
GN   {ECO:0000313|EMBL:MBC2046994.1}, HCA73_00515
GN   {ECO:0000313|EMBL:MBC1911112.1}, HCA78_09805
GN   {ECO:0000313|EMBL:MBC2004063.1}, HCA80_09845
GN   {ECO:0000313|EMBL:MBC2036525.1}, HCA81_02880
GN   {ECO:0000313|EMBL:MBC2019974.1}, HCB02_09225
GN   {ECO:0000313|EMBL:MBC2105133.1}, HCB06_05150
GN   {ECO:0000313|EMBL:MBC2116000.1}, HCB08_07140
GN   {ECO:0000313|EMBL:MBC2206599.1}, HCB25_01115
GN   {ECO:0000313|EMBL:MBC2242643.1}, HCB26_02370
GN   {ECO:0000313|EMBL:MBC2165421.1}, HCB27_09755
GN   {ECO:0000313|EMBL:MBC2176901.1}, HCB29_07385
GN   {ECO:0000313|EMBL:MBC2162902.1}, HCB35_01095
GN   {ECO:0000313|EMBL:MBC2239054.1}, HCB69_00955
GN   {ECO:0000313|EMBL:MBC2282942.1}, HCB83_02335
GN   {ECO:0000313|EMBL:MBC2303690.1}, HCC18_01070
GN   {ECO:0000313|EMBL:MBC2315420.1}, HCC36_02190
GN   {ECO:0000313|EMBL:MBC2292029.1}, HCJ43_12815
GN   {ECO:0000313|EMBL:MBC1976156.1}, HCJ81_03155
GN   {ECO:0000313|EMBL:MBC2309867.1}, HCX63_06790
GN   {ECO:0000313|EMBL:MBC2322991.1};
OS   Listeria booriae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1552123 {ECO:0000313|EMBL:KGL40686.1, ECO:0000313|Proteomes:UP000029844};
RN   [1] {ECO:0000313|EMBL:KGL40686.1, ECO:0000313|Proteomes:UP000029844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL A5-0281 {ECO:0000313|EMBL:KGL40686.1,
RC   ECO:0000313|Proteomes:UP000029844};
RA   den Bakker H.C.;
RT   "Novel Listeriaceae from food processing environments.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000519573, ECO:0000313|Proteomes:UP000525521}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL L7-0025 {ECO:0000313|EMBL:MBC2322991.1,
RC   ECO:0000313|Proteomes:UP000585036}, FSL L7-0029
RC   {ECO:0000313|EMBL:MBC2315420.1, ECO:0000313|Proteomes:UP000576477},
RC   FSL L7-0035 {ECO:0000313|EMBL:MBC2303690.1,
RC   ECO:0000313|Proteomes:UP000526161}, FSL L7-0039
RC   {ECO:0000313|EMBL:MBC2309867.1, ECO:0000313|Proteomes:UP000565628},
RC   FSL L7-0051 {ECO:0000313|EMBL:MBC2292029.1,
RC   ECO:0000313|Proteomes:UP000543005}, FSL L7-0054
RC   {ECO:0000313|EMBL:MBC2282942.1, ECO:0000313|Proteomes:UP000585696},
RC   FSL L7-0149 {ECO:0000313|EMBL:MBC2239054.1,
RC   ECO:0000313|Proteomes:UP000553016}, FSL L7-0153
RC   {ECO:0000313|EMBL:MBC2242643.1, ECO:0000313|Proteomes:UP000550367},
RC   FSL L7-0217 {ECO:0000313|EMBL:MBC2206599.1,
RC   ECO:0000313|Proteomes:UP000572892}, FSL L7-0245
RC   {ECO:0000313|EMBL:MBC2165421.1, ECO:0000313|Proteomes:UP000519573},
RC   FSL L7-0256 {ECO:0000313|EMBL:MBC2162902.1,
RC   ECO:0000313|Proteomes:UP000528739}, FSL L7-0259
RC   {ECO:0000313|EMBL:MBC2176901.1, ECO:0000313|Proteomes:UP000541735},
RC   FSL L7-0335 {ECO:0000313|EMBL:MBC2105133.1,
RC   ECO:0000313|Proteomes:UP000565263}, FSL L7-0360
RC   {ECO:0000313|EMBL:MBC2116000.1, ECO:0000313|Proteomes:UP000529446},
RC   FSL L7-0385 {ECO:0000313|EMBL:MBC2019974.1,
RC   ECO:0000313|Proteomes:UP000587422}, FSL L7-0435
RC   {ECO:0000313|EMBL:MBC2004063.1, ECO:0000313|Proteomes:UP000546806},
RC   FSL L7-0459 {ECO:0000313|EMBL:MBC2036525.1,
RC   ECO:0000313|Proteomes:UP000591514}, FSL L7-0514
RC   {ECO:0000313|EMBL:MBC2046994.1, ECO:0000313|Proteomes:UP000588249},
RC   FSL L7-0520 {ECO:0000313|EMBL:MBC1976156.1,
RC   ECO:0000313|Proteomes:UP000587214}, FSL L7-0587
RC   {ECO:0000313|EMBL:MBC2066339.1, ECO:0000313|Proteomes:UP000573524},
RC   FSL L7-0811 {ECO:0000313|EMBL:MBC1911112.1,
RC   ECO:0000313|Proteomes:UP000574808}, FSL L7-0818
RC   {ECO:0000313|EMBL:MBC1897186.1, ECO:0000313|Proteomes:UP000578190},
RC   FSL L7-0978 {ECO:0000313|EMBL:MBC1791996.1,
RC   ECO:0000313|Proteomes:UP000539064}, FSL L7-0990
RC   {ECO:0000313|EMBL:MBC1795247.1, ECO:0000313|Proteomes:UP000548082},
RC   FSL L7-1017 {ECO:0000313|EMBL:MBC1777873.1,
RC   ECO:0000313|Proteomes:UP000547643}, FSL L7-1385
RC   {ECO:0000313|EMBL:MBC1573596.1, ECO:0000313|Proteomes:UP000571880},
RC   FSL L7-1387 {ECO:0000313|EMBL:MBC1560646.1,
RC   ECO:0000313|Proteomes:UP000541955}, FSL L7-1427
RC   {ECO:0000313|EMBL:MBC1564419.1, ECO:0000313|Proteomes:UP000586951},
RC   FSL L7-1681 {ECO:0000313|EMBL:MBC1371588.1,
RC   ECO:0000313|Proteomes:UP000591929}, FSL L7-1698
RC   {ECO:0000313|EMBL:MBC1357185.1, ECO:0000313|Proteomes:UP000525521},
RC   FSL L7-1816 {ECO:0000313|EMBL:MBC1315632.1,
RC   ECO:0000313|Proteomes:UP000543379}, FSL L7-1825
RC   {ECO:0000313|EMBL:MBC1306539.1, ECO:0000313|Proteomes:UP000571424},
RC   FSL L7-1827 {ECO:0000313|EMBL:MBC1245722.1,
RC   ECO:0000313|Proteomes:UP000574869}, FSL L7-1831
RC   {ECO:0000313|EMBL:MBC1229128.1, ECO:0000313|Proteomes:UP000585770},
RC   FSL L7-1833 {ECO:0000313|EMBL:MBC1330782.1,
RC   ECO:0000313|Proteomes:UP000532866}, FSL L7-1834
RC   {ECO:0000313|EMBL:MBC1226059.1, ECO:0000313|Proteomes:UP000588567},
RC   FSL L7-1836 {ECO:0000313|EMBL:MBC1284758.1,
RC   ECO:0000313|Proteomes:UP000588455}, and FSL L7-1850
RC   {ECO:0000313|EMBL:MBC2372539.1, ECO:0000313|Proteomes:UP000546244};
RA   Liao J., Wiedmann M.;
RT   "Soil Listeria distribution.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of branched-chain amino acids
CC       (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction
CC       of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In
CC       the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl
CC       migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the
CC       reductase reaction, this 2-ketoacid undergoes a metal-dependent
CC       reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
CC       {ECO:0000256|HAMAP-Rule:MF_00435}.
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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00435};
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         Evidence={ECO:0000256|HAMAP-Rule:MF_00435};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-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.
CC       {ECO:0000256|ARBA:ARBA00004885, ECO:0000256|HAMAP-Rule:MF_00435}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC       pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864, ECO:0000256|HAMAP-
CC       Rule:MF_00435}.
CC   -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|HAMAP-Rule:MF_00435,
CC       ECO:0000256|PROSITE-ProRule:PRU01198}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00435}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGL40686.1}.
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DR   EMBL; JNFA01000023; KGL40686.1; -; Genomic_DNA.
DR   EMBL; JAAROK010000001; MBC1226059.1; -; Genomic_DNA.
DR   EMBL; JAARON010000001; MBC1229128.1; -; Genomic_DNA.
DR   EMBL; JAAROQ010000001; MBC1245722.1; -; Genomic_DNA.
DR   EMBL; JAAROI010000001; MBC1284758.1; -; Genomic_DNA.
DR   EMBL; JAAROS010000001; MBC1306539.1; -; Genomic_DNA.
DR   EMBL; JAAROV010000001; MBC1315632.1; -; Genomic_DNA.
DR   EMBL; JAAROL010000001; MBC1330782.1; -; Genomic_DNA.
DR   EMBL; JAARPI010000001; MBC1357185.1; -; Genomic_DNA.
DR   EMBL; JAARPL010000003; MBC1371588.1; -; Genomic_DNA.
DR   EMBL; JAARRW010000001; MBC1560646.1; -; Genomic_DNA.
DR   EMBL; JAARRU010000001; MBC1564419.1; -; Genomic_DNA.
DR   EMBL; JAARRX010000002; MBC1573596.1; -; Genomic_DNA.
DR   EMBL; JAARUV010000001; MBC1777873.1; -; Genomic_DNA.
DR   EMBL; JAARVG010000001; MBC1791996.1; -; Genomic_DNA.
DR   EMBL; JAARVD010000001; MBC1795247.1; -; Genomic_DNA.
DR   EMBL; JAARWF010000002; MBC1897186.1; -; Genomic_DNA.
DR   EMBL; JAARWI010000001; MBC1911112.1; -; Genomic_DNA.
DR   EMBL; JAASWF010000008; MBC1976156.1; -; Genomic_DNA.
DR   EMBL; JAARWW010000004; MBC2004063.1; -; Genomic_DNA.
DR   EMBL; JAARWY010000001; MBC2019974.1; -; Genomic_DNA.
DR   EMBL; JAARWV010000004; MBC2036525.1; -; Genomic_DNA.
DR   EMBL; JAARWT010000001; MBC2046994.1; -; Genomic_DNA.
DR   EMBL; JAARWQ010000001; MBC2066339.1; -; Genomic_DNA.
DR   EMBL; JAARXL010000004; MBC2105133.1; -; Genomic_DNA.
DR   EMBL; JAARXI010000002; MBC2116000.1; -; Genomic_DNA.
DR   EMBL; JAARYE010000002; MBC2162902.1; -; Genomic_DNA.
DR   EMBL; JAARYH010000001; MBC2165421.1; -; Genomic_DNA.
DR   EMBL; JAARYD010000004; MBC2176901.1; -; Genomic_DNA.
DR   EMBL; JAARYN010000002; MBC2206599.1; -; Genomic_DNA.
DR   EMBL; JAARZA010000001; MBC2239054.1; -; Genomic_DNA.
DR   EMBL; JAARYY010000001; MBC2242643.1; -; Genomic_DNA.
DR   EMBL; JAARZS010000002; MBC2282942.1; -; Genomic_DNA.
DR   EMBL; JAARZT010000003; MBC2292029.1; -; Genomic_DNA.
DR   EMBL; JAARZW010000002; MBC2303690.1; -; Genomic_DNA.
DR   EMBL; JAASWV010000003; MBC2309867.1; -; Genomic_DNA.
DR   EMBL; JAARZZ010000001; MBC2315420.1; -; Genomic_DNA.
DR   EMBL; JAATOC010000002; MBC2322991.1; -; Genomic_DNA.
DR   EMBL; JAARMV010000002; MBC2372539.1; -; Genomic_DNA.
DR   RefSeq; WP_036085892.1; NZ_UGPF01000002.1.
DR   STRING; 1552123.EP57_09015; -.
DR   GeneID; 58717512; -.
DR   eggNOG; COG0059; Bacteria.
DR   OrthoDB; 9804088at2; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000029844; Unassembled WGS sequence.
DR   Proteomes; UP000519573; Unassembled WGS sequence.
DR   Proteomes; UP000525521; Unassembled WGS sequence.
DR   Proteomes; UP000526161; Unassembled WGS sequence.
DR   Proteomes; UP000528739; Unassembled WGS sequence.
DR   Proteomes; UP000529446; Unassembled WGS sequence.
DR   Proteomes; UP000532866; Unassembled WGS sequence.
DR   Proteomes; UP000539064; Unassembled WGS sequence.
DR   Proteomes; UP000541735; Unassembled WGS sequence.
DR   Proteomes; UP000541955; Unassembled WGS sequence.
DR   Proteomes; UP000543005; Unassembled WGS sequence.
DR   Proteomes; UP000543379; Unassembled WGS sequence.
DR   Proteomes; UP000546244; Unassembled WGS sequence.
DR   Proteomes; UP000546806; Unassembled WGS sequence.
DR   Proteomes; UP000547643; Unassembled WGS sequence.
DR   Proteomes; UP000548082; Unassembled WGS sequence.
DR   Proteomes; UP000550367; Unassembled WGS sequence.
DR   Proteomes; UP000553016; Unassembled WGS sequence.
DR   Proteomes; UP000565263; Unassembled WGS sequence.
DR   Proteomes; UP000565628; Unassembled WGS sequence.
DR   Proteomes; UP000571424; Unassembled WGS sequence.
DR   Proteomes; UP000571880; Unassembled WGS sequence.
DR   Proteomes; UP000572892; Unassembled WGS sequence.
DR   Proteomes; UP000573524; Unassembled WGS sequence.
DR   Proteomes; UP000574808; Unassembled WGS sequence.
DR   Proteomes; UP000574869; Unassembled WGS sequence.
DR   Proteomes; UP000576477; Unassembled WGS sequence.
DR   Proteomes; UP000578190; Unassembled WGS sequence.
DR   Proteomes; UP000585036; Unassembled WGS sequence.
DR   Proteomes; UP000585696; Unassembled WGS sequence.
DR   Proteomes; UP000585770; Unassembled WGS sequence.
DR   Proteomes; UP000586951; Unassembled WGS sequence.
DR   Proteomes; UP000587214; Unassembled WGS sequence.
DR   Proteomes; UP000587422; Unassembled WGS sequence.
DR   Proteomes; UP000588249; Unassembled WGS sequence.
DR   Proteomes; UP000588455; Unassembled WGS sequence.
DR   Proteomes; UP000588567; Unassembled WGS sequence.
DR   Proteomes; UP000591514; Unassembled WGS sequence.
DR   Proteomes; UP000591929; Unassembled WGS sequence.
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   Gene3D; 6.10.240.10; -; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR00465; ilvC; 1.
DR   PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF01450; IlvC; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   PIRSF; PIRSF000116; IlvC_gammaproteo; 2.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51851; KARI_C; 1.
DR   PROSITE; PS51850; KARI_N; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_00435};
KW   Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW   ECO:0000256|HAMAP-Rule:MF_00435}; Isomerase {ECO:0000313|EMBL:KGL40686.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00435}; NADP {ECO:0000256|HAMAP-Rule:MF_00435};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00435}; Reference proteome {ECO:0000313|Proteomes:UP000029844}.
FT   DOMAIN          2..181
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          182..327
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         25..28
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         48
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         52
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         133
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         190
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         194
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         226
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         230
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         251
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00435,
FT                   ECO:0000256|PROSITE-ProRule:PRU01198"
SQ   SEQUENCE   331 AA;  35915 MW;  A47ED11B50E36C36 CRC64;
     MTKVYYEDAV QKSALEGKKV AVIGYGSQGH AHSQNLRDNG NNVIIGIREG KSAEAARNDG
     FEVLSVADAT KAADVVMILL PDETQGDTYE AEIKPNLEAG NALAFAHGFN IHFDVIKPPA
     DVDVFLVAPK GPGHLVRRTF VEGGAVPGLF AVYQDATGNA TDVALSYAKG IGATRAGVIE
     TTFKEETETD LFGEQAVLCG GTTHLVQAGF ETLVEAGYQP ELAYFEVLHE LKLIVDLMYE
     GGMEKMRHSI SNTAEYGDYV SGPRVVTSDT KKAMKEVLTD IQDGTFAKAF IDDNKNGFKE
     FHRLRAEQKG HQIEQVGAAL REMMPFVKPQ N
//

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