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
//