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Database: UniProt
Entry: A0A1L3JLC6_9FLAO
LinkDB: A0A1L3JLC6_9FLAO
Original site: A0A1L3JLC6_9FLAO 
ID   A0A1L3JLC6_9FLAO        Unreviewed;       492 AA.
AC   A0A1L3JLC6;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|ARBA:ARBA00032744};
GN   ORFNames=LPB136_11510 {ECO:0000313|EMBL:APG65950.1};
OS   Tenacibaculum todarodis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=1850252 {ECO:0000313|EMBL:APG65950.1, ECO:0000313|Proteomes:UP000181898};
RN   [1] {ECO:0000313|EMBL:APG65950.1, ECO:0000313|Proteomes:UP000181898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0136 {ECO:0000313|EMBL:APG65950.1,
RC   ECO:0000313|Proteomes:UP000181898};
RA   Kim E., Yi H.;
RT   "Tenacibaculum sp. LPB0136, isolated from marine environment.";
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; CP018155; APG65950.1; -; Genomic_DNA.
DR   RefSeq; WP_072556473.1; NZ_CP018155.1.
DR   AlphaFoldDB; A0A1L3JLC6; -.
DR   STRING; 1850252.LPB136_11510; -.
DR   KEGG; ten:LPB136_11510; -.
DR   OrthoDB; 9804088at2; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000181898; Chromosome.
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:APG65950.1};
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:UP000181898}.
FT   DOMAIN          14..208
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          209..341
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   DOMAIN          345..485
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   492 AA;  54334 MW;  27EBE818E169FF9B CRC64;
     MSNYFNTLTL REKLEQLGKC RFMDASEFED GVAALKGKKI VIVGCGAQGL NQGLNMRDSG
     LDISYTLRQA AISEKRQSYI NATSNNFTVG TYEELLPTAD VVINLAPDKQ HTNVVNAVMP
     LMKKGATLSY SHGFNIVEEG MQIREDLTVI MVAPKCPGSE VREEYKRGFG VPTLTAVHPE
     NDPEGKGWAQ AKAYAVATGG NRAGVLESSF VAEVKSDLMG EQTILCGLLQ TGAILSFDKM
     VEEGIEPGYA AKLIQYGWET VTEALKHGGI TNMMDRLSNP AKVEAFRLSE ELKDIMRPLF
     QKHMDDIMTG HFSKTMMEDW ANDDINLLTW RAATGETAFE KQVITSDEIP EQEYFDHGTL
     LVAFVRSGVE LAFEAMTDSG IIDASAYYES LHETPLIANT IARMKLAEMN RVISDTAEYG
     CYLFDHACKP LLTDFMKDVK TNVIGKSFSS ENGVDNQELI RINAIIRNHP VEIVGAKLRA
     SMTAMKVIKT EA
//
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