ID A0A2W6XSY0_9FLAO Unreviewed; 474 AA. AC A0A2W6XSY0; DT 12-SEP-2018, integrated into UniProtKB/TrEMBL. DT 12-SEP-2018, sequence version 1. DT 07-NOV-2018, entry version 3. DE SubName: Full=Ketol-acid reductoisomerase {ECO:0000313|EMBL:PZU79896.1}; DE Flags: Fragment; GN ORFNames=DI529_17130 {ECO:0000313|EMBL:PZU79896.1}; OS Chryseobacterium sp. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Chryseobacterium. OX NCBI_TaxID=1871047 {ECO:0000313|EMBL:PZU79896.1}; RN [1] {ECO:0000313|EMBL:PZU79896.1} RP NUCLEOTIDE SEQUENCE. 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- RT sourced microbial strains."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC {ECO:0000256|SAAS:SAAS00365316}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. {ECO:0000256|SAAS:SAAS00365291}. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000256|PROSITE-ProRule:PRU01198, CC ECO:0000256|SAAS:SAAS00556475}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01198}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR21371; PTHR21371; 2. DR Pfam; PF01450; IlvC; 2. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 2. DR SUPFAM; SSF51735; SSF51735; 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|PROSITE-ProRule:PRU01198, KW ECO:0000256|SAAS:SAAS00442796}; KW Branched-chain amino acid biosynthesis {ECO:0000256|PROSITE- KW ProRule:PRU01198, ECO:0000256|SAAS:SAAS00442833}; KW Isomerase {ECO:0000313|EMBL:PZU79896.1}; KW Magnesium {ECO:0000256|PROSITE-ProRule:PRU01198}; KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01198}; KW Oxidoreductase {ECO:0000256|PROSITE-ProRule:PRU01198, KW ECO:0000256|SAAS:SAAS00442857}. FT DOMAIN 19 208 KARI N-terminal Rossmann. FT {ECO:0000259|PROSITE:PS51850}. FT DOMAIN 209 353 KARI C-terminal knotted. FT {ECO:0000259|PROSITE:PS51851}. FT DOMAIN 354 474 KARI C-terminal knotted. FT {ECO:0000259|PROSITE:PS51851}. FT METAL 217 217 Magnesium 1. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 217 217 Magnesium 2. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 221 221 Magnesium 1. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 389 389 Magnesium 2. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT METAL 393 393 Magnesium 2. {ECO:0000256|PROSITE- FT ProRule:PRU01198}. FT BINDING 278 278 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT BINDING 414 414 Substrate. {ECO:0000256|PROSITE-ProRule: FT PRU01198}. FT NON_TER 474 474 {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 //