ID A0A0J8RQA4_COCIT Unreviewed; 262 AA.
AC A0A0J8RQA4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Ketol-acid reductoisomerase {ECO:0000313|EMBL:KMU87022.1};
GN ORFNames=CIHG_04962 {ECO:0000313|EMBL:KMU87022.1};
OS Coccidioides immitis H538.4.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=396776 {ECO:0000313|EMBL:KMU87022.1, ECO:0000313|Proteomes:UP000054563};
RN [1] {ECO:0000313|Proteomes:UP000054563}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H538.4 {ECO:0000313|Proteomes:UP000054563};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
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DR EMBL; DS016995; KMU87022.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J8RQA4; -.
DR STRING; 396776.A0A0J8RQA4; -.
DR VEuPathDB; FungiDB:CIHG_04962; -.
DR Proteomes; UP000054563; Unassembled WGS sequence.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR013023; KARI.
DR InterPro; IPR013116; KARI_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21371; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR21371:SF1; KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL; 1.
DR Pfam; PF07991; IlvN; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS51850; KARI_N; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KMU87022.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000054563}.
FT DOMAIN 66..262
FT /note="KARI N-terminal Rossmann"
FT /evidence="ECO:0000259|PROSITE:PS51850"
FT REGION 175..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 262 AA; 28264 MW; 5BB6651E1A1D1B5C CRC64;
MASRPAARAL RSSFSRNLAA SASKASRRTF ISATNARPAL AAKAAPIAAP FAQQARGIKT
IDFAGTKETV YEREDWPREK LLDYFKNDTL ALIGYGSQGH GQGLNLRDNG LNVIVGVRKD
GASWRGAVQD GWVPGKNLFD VNEAINRGTI VMNLLSDAAQ SETWPAIKPL LTKGKTPQLL
PPGFTPPPSE DPPQGWWSQR RAGGVIDVSK GSGRDCRSPL HGRTETSNPT YSDDEGGRTG
NAKRREAHPL FVFRRSEGGV AS
//
