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Database: UniProt
Entry: A0A1A9HZR4_9BACT
LinkDB: A0A1A9HZR4_9BACT
Original site: A0A1A9HZR4_9BACT 
ID   A0A1A9HZR4_9BACT        Unreviewed;       350 AA.
AC   A0A1A9HZR4;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|ARBA:ARBA00032744};
GN   ORFNames=A8C56_02010 {ECO:0000313|EMBL:ANH79912.1};
OS   Niabella ginsenosidivorans.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Niabella.
OX   NCBI_TaxID=1176587 {ECO:0000313|EMBL:ANH79912.1, ECO:0000313|Proteomes:UP000077667};
RN   [1] {ECO:0000313|EMBL:ANH79912.1, ECO:0000313|Proteomes:UP000077667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BS26 {ECO:0000313|EMBL:ANH79912.1,
RC   ECO:0000313|Proteomes:UP000077667};
RA   Im W.T., Siddiqi M.Z.;
RT   "Niabella ginsenosidivorans BS26 whole genome sequencing.";
RL   Submitted (MAY-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}.
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DR   EMBL; CP015772; ANH79912.1; -; Genomic_DNA.
DR   RefSeq; WP_067751347.1; NZ_CP015772.1.
DR   AlphaFoldDB; A0A1A9HZR4; -.
DR   STRING; 1176587.A8C56_02010; -.
DR   KEGG; nia:A8C56_02010; -.
DR   OrthoDB; 9804088at2; -.
DR   UniPathway; UPA00047; UER00056.
DR   UniPathway; UPA00049; UER00060.
DR   Proteomes; UP000077667; 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; 1.
DR   Pfam; PF07991; IlvN; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS51851; KARI_C; 1.
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:ANH79912.1};
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:UP000077667}.
FT   DOMAIN          9..199
FT                   /note="KARI N-terminal Rossmann"
FT                   /evidence="ECO:0000259|PROSITE:PS51850"
FT   DOMAIN          200..347
FT                   /note="KARI C-terminal knotted"
FT                   /evidence="ECO:0000259|PROSITE:PS51851"
FT   BINDING         208
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         208
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         212
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         244
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         248
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT   BINDING         270
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ   SEQUENCE   350 AA;  38622 MW;  05D18577EC17280E CRC64;
     MAKLNFGGVE ENVVTREEFP LSKAQEILKD ETVAVIGYGV QGPGQALNQK DNGINVIVGQ
     RKNSKSWDKA VADGFVPGET LFEIEEALQR GTIICYLLSD AAQIALWPTV QKYLTPGKAL
     YFSHGFGITF NEQTGIVPPK DVDVFLVAPK GSGTSLRRMF LQGRGLNSSY AIFQDATGKA
     KDRVIALGIA VGSGYLFETD FKKEVFSDLT GERGTLMGAI QGIFAAQYEV LRSKGHSPSE
     AFNETVEELT QSLMPLVAEN GMDWMYANCS TTAQRGALDW WKKFKDATQP VFEELYESVA
     TGKESQRSID SNSQPDYREK LNAELKELQE SEMWQAGKTV RSLRPENQAV
//
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