ID I4A1A7_ORNRL Unreviewed; 348 AA.
AC I4A1A7;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|ARBA:ARBA00032744};
GN OrderedLocusNames=Ornrh_1583 {ECO:0000313|EMBL:AFL97741.1};
OS Ornithobacterium rhinotracheale (strain ATCC 51463 / DSM 15997 / CCUG 23171
OS / CIP 104009 / LMG 9086).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Ornithobacterium.
OX NCBI_TaxID=867902 {ECO:0000313|EMBL:AFL97741.1, ECO:0000313|Proteomes:UP000006051};
RN [1] {ECO:0000313|EMBL:AFL97741.1, ECO:0000313|Proteomes:UP000006051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51463 / DSM 15997 / CCUG 23171 / LMG 9086
RC {ECO:0000313|Proteomes:UP000006051};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Mikhailova N., Teshima H., Kyrpides N., Mavromatis K., Pagani I.,
RA Ivanova N., Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M.,
RA Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA Lang E., Kopitz M., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Ornithobacterium rhinotracheale DSM 15997.";
RL Submitted (JUN-2012) 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; CP003283; AFL97741.1; -; Genomic_DNA.
DR RefSeq; WP_014791292.1; NC_018016.1.
DR AlphaFoldDB; I4A1A7; -.
DR STRING; 867902.Ornrh_1583; -.
DR GeneID; 71569663; -.
DR KEGG; orh:Ornrh_1583; -.
DR PATRIC; fig|867902.3.peg.1537; -.
DR eggNOG; COG0059; Bacteria.
DR HOGENOM; CLU_033821_1_2_10; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000006051; 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:AFL97741.1};
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:UP000006051}.
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 348 AA; 38460 MW; 6B48FD2EC657A151 CRC64;
MAKINFGGVE ENVVTREEFP LEKAQEVLKD EVVAIIGYGV QGPGQALNLK DNGVNVIVGQ
RKNSKSWDKA VEDGWVTGET LFEIEEAAEK ATIIEYLLSD AGQISQWDKV KKHLTKGKAL
YFSHGFGITF NDQTGIVPPA DVDVILVAPK GSGRSLRTLF LEGKGLNSSY AIYQDATGKA
YDRVIALGIG IGSGYLFETD FKREVYSDLT GERGVLMGAI AGLFEAQYNV LRAHGHTPSE
AFNETVEELT QSLMPLVAQN GMDWMYANCS TTAQRGALDW KNKFRDVTSP VFEELYQSVA
SGNEAKKTIE ANSKEGYRDS LNQELKEIRE SEIWETGRAV RQLRPENN
//
