ID R6DHD5_9BACE Unreviewed; 347 AA.
AC R6DHD5;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Acetohydroxy-acid isomeroreductase {ECO:0000256|ARBA:ARBA00032744};
GN ORFNames=BN772_02141 {ECO:0000313|EMBL:CDA83671.1};
OS Bacteroides sp. CAG:754.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1262750 {ECO:0000313|EMBL:CDA83671.1, ECO:0000313|Proteomes:UP000017906};
RN [1] {ECO:0000313|EMBL:CDA83671.1, ECO:0000313|Proteomes:UP000017906}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:754 {ECO:0000313|Proteomes:UP000017906};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDA83671.1}.
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DR EMBL; CBCP010000096; CDA83671.1; -; Genomic_DNA.
DR AlphaFoldDB; R6DHD5; -.
DR UniPathway; UPA00047; UER00056.
DR UniPathway; UPA00049; UER00060.
DR Proteomes; UP000017906; Unassembled WGS sequence.
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:CDA83671.1};
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:UP000017906}.
FT DOMAIN 10..198
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT DOMAIN 199..346
FT /note="KARI C-terminal knotted"
FT /evidence="ECO:0000259|PROSITE:PS51851"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 211
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01198"
SQ SEQUENCE 347 AA; 38100 MW; C42479FCE6EE9F39 CRC64;
MAQLNFGGTV ETVVIRDEFP LEKAREVLKN ETIAVIGYGV QGPGQALNLR DNGFNVIVGQ
REGKTYDKAV ADGWVPGETL FGIEEACEKG TIVMCLLSDA AVMSVWPTIK PYLTAGKALY
FSHGFAITWN DRTGVVPPAD IDVIMVAPKG SGTSLRTMFL EGRGLNSSYA IYQDATGKAY
EKTIALGIGI GSGYLFETTF QREATSDLTG ERGSLMGAIQ GLLLAQYEVL RENGHTPSEA
FNETVEELTQ SLMPLFAKNG MDWMYANCST TAQRGALDWM GPFHDAIKPV VEKLYHSVKT
GNEAQISIDS NSKVDYREKL EEELKALRES EMWQTAVTVR KLRPENN
//
