ID A0A0Q0H6I5_9GAMM Unreviewed; 493 AA.
AC A0A0Q0H6I5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Ketol-acid reductoisomerase (NADP(+)) {ECO:0000256|ARBA:ARBA00015731};
DE EC=1.1.1.86 {ECO:0000256|ARBA:ARBA00013102};
DE AltName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|ARBA:ARBA00032744};
GN Name=ilvC {ECO:0000313|EMBL:KPZ68070.1};
GN ORFNames=AN944_03764 {ECO:0000313|EMBL:KPZ68070.1};
OS Shewanella sp. P1-14-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ68070.1, ECO:0000313|Proteomes:UP000050414};
RN [1] {ECO:0000313|EMBL:KPZ68070.1, ECO:0000313|Proteomes:UP000050414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ68070.1,
RC ECO:0000313|Proteomes:UP000050414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000507};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-
CC isoleucine from 2-oxobutanoate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004885}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from
CC pyruvate: step 2/4. {ECO:0000256|ARBA:ARBA00004864}.
CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family.
CC {ECO:0000256|ARBA:ARBA00010318, ECO:0000256|PROSITE-ProRule:PRU01198}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01198}.
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:KPZ68070.1}.
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; LKTL01000031; KPZ68070.1; -; Genomic_DNA.
DR RefSeq; WP_055026150.1; NZ_LKTL01000031.1.
DR AlphaFoldDB; A0A0Q0H6I5; -.
DR PATRIC; fig|1723761.3.peg.3853; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000050414; 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:0046872; F:metal 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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 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; 2.
DR Pfam; PF07991; IlvN; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51851; KARI_C; 2.
DR PROSITE; PS51850; KARI_N; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|PROSITE-ProRule:PRU01198};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304,
KW ECO:0000256|PROSITE-ProRule:PRU01198};
KW Isomerase {ECO:0000313|EMBL:KPZ68070.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PROSITE-
KW ProRule:PRU01198};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01198};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|PROSITE-
KW ProRule:PRU01198}; Reference proteome {ECO:0000313|Proteomes:UP000050414}.
FT DOMAIN 17..208
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 209..353
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT DOMAIN 354..486
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 217
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 221
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 393
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 493 AA; 54270 MW; 97E8067610868A97 CRC64;
MANYFNSLNL RQQLAQLAQC RFMDRNEFSD GCNFIKDWNI VILGCGAQGL NQGLNMRDSG
LNISFALRPQ AIAEKRASWK QATDNGFKVG TFEELIPDAD LVLNLTPDKQ HSNVVNAVMP
LMKQGSTLSY SHGFNIVEEG MQVRSDITVV MVAPKCPGTE VREEYKRGFG VPTLIAVHPE
NDPKGDGLAI AKAYASATGG DRAGVLLSSF VAEVKSDLMG EQTILCGMLQ TGAILGYEKM
VADGVEPGYA GKLIQQGWET VTEALKHGGI TNMMDRLSNP AKVKAFEVAE ELKVILKPLF
EKHMDDIISG EFSRTMMEDW ANDDANLLRW RSETNETAFE NAPASDEYID EQTYFDKGIF
LVAMIKAGVE LAFDTMVAAG IIEESAYYES LHETPLIANT IARKRLYEMN VVISDTAEYG
CYLFNHAAVP LLRDYVAGMS SELLGAGLKE GSNSVDNKRL IEVNEAIRHT DVEFIGAELR
GYMTDMKGIV EAS
//
