ID A0A2W6XSY0_9FLAO Unreviewed; 474 AA. AC A0A2W6XSY0; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 14-DEC-2022, entry version 13. DE RecName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|ARBA:ARBA00032744}; DE Flags: Fragment; GN ORFNames=DI529_17130 {ECO:0000313|EMBL:PZU79896.1}; OS Chryseobacterium sp. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; Weeksellaceae; OC Chryseobacterium group; Chryseobacterium. OX NCBI_TaxID=1871047 {ECO:0000313|EMBL:PZU79896.1, ECO:0000313|Proteomes:UP000248565}; RN [1] {ECO:0000313|EMBL:PZU79896.1, ECO:0000313|Proteomes:UP000248565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S2_003_000_R2_7 {ECO:0000313|EMBL:PZU79896.1}; RA Brooks B., Olm M.R., Firek B.A., Baker R., Thomas B.C., Morowitz M.J., RA Banfield J.F.; RT "Infants hospitalized years apart are colonized by the same room-sourced RT microbial strains."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. 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:PZU79896.1}. 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; QFQW01000119; PZU79896.1; -; Genomic_DNA. DR AlphaFoldDB; A0A2W6XSY0; -. DR EnsemblBacteria; PZU79896; PZU79896; DI529_17130. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000248565; 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; 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; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 2. 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 TIGRFAMs; TIGR00465; ilvC; 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:PZU79896.1}; KW Magnesium {ECO:0000256|PROSITE-ProRule:PRU01198}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE- KW ProRule:PRU01198}; Oxidoreductase {ECO:0000256|PROSITE-ProRule:PRU01198}. FT DOMAIN 19..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..474 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" FT NON_TER 474 FT /evidence="ECO:0000313|EMBL:PZU79896.1" SQ SEQUENCE 474 AA; 52286 MW; A2FD01B033292CA4 CRC64; MANYFNTLSL RDQLHQLGQA EFMDSSEFSD GVSALKGKKI VVVGCGAQGL NQGLNLRDSG LDVSYALRQE AIDQKRDSWK NATENNFKVG TYEELIPTAD LVINLTPDKQ HTSVINAVQP LMKQGATLSY SHGFNIVEEG MQIRKDLTVI MVAPKCPGSE VRAEYLRGFG VPTLIAVHPE NDPQGKGWAE AKAYCVGTGG HKAGVLKSSF VAEVKSDLMG EQTILCGLLQ TGSILSFDKM VEKGIDAGYA SKLVQYGVEV ITEALKHGGV SGMLDRLSNP AKLKAFELSE ELKDIMRPLF QKHQDDIISG EFSKTMMEDW ANGDANLLKW RAETGETAFE KTPAGDVKIE EQEYFDNYLL MSAFIRAGVE LAFETMVEAG IKPESAYYES LHETPLIANT IARKKLFEMN RVISDTAEYG CYLFDQACKP LLADFMKSVD TDLVGKNFNE GKKTSVDNAQ LVYVNDVLRN HPVE //