ID Q5KYI2_GEOKA Unreviewed; 733 AA.
AC Q5KYI2;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:BAD76254.1};
GN OrderedLocusNames=GK1969 {ECO:0000313|EMBL:BAD76254.1};
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD76254.1, ECO:0000313|Proteomes:UP000001172};
RN [1] {ECO:0000313|EMBL:BAD76254.1, ECO:0000313|Proteomes:UP000001172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD76254.1,
RC ECO:0000313|Proteomes:UP000001172};
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; BA000043; BAD76254.1; -; Genomic_DNA.
DR RefSeq; WP_011231455.1; NC_006510.1.
DR AlphaFoldDB; Q5KYI2; -.
DR STRING; 235909.GK1969; -.
DR KEGG; gka:GK1969; -.
DR PATRIC; fig|235909.7.peg.2109; -.
DR eggNOG; COG0129; Bacteria.
DR HOGENOM; CLU_384462_0_0_9; -.
DR Proteomes; UP000001172; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-RELATED; 1.
DR Pfam; PF00920; ILVD_EDD; 2.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Branched-chain amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023304};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW Reference proteome {ECO:0000313|Proteomes:UP000001172}.
SQ SEQUENCE 733 AA; 81349 MW; CFC351D22E8FFEA6 CRC64;
MPAVVYPRIE SQVNPYRDNV QGKANEPICV AGLLDRSKQI LGSELKGMQP DWTLEEIYDR
LHHNAPRIAI IGGSSDHPAH IMDYQTIARA AIRIWQNGGV PFQFSTPVMC DGTAQSNQGM
SYSLQSRNAV AQMIVNQLEA HSYHGAFVIQ GCDKQPLGVV SALAHLDRVR RERGEPPFFA
TFAPAHVLKG GTIPPKLYAE LEEVARRAEL AGEEDIAYDL RDALSYILQC SSNTAFQGVL
ERARGKGIIT KEQHEDYEKR LAVATCDSQG GVCAFNGTGN SSRHLIAGLG LIHPALELLT
APPTQEQVNA ALDSLALLMN DPVYGVANIM AANIKNAIRI HSATGGSTNI MMHIVAAMLY
GGYQFDLWEY DNIHHEVPVP DLFDYSLTEG RDIFALAIQC CSGKIRGMET VFHELLSNGV
PMDVDAPTVT GTTWRERLSV NQEQLPAENV KNNPIILSKP RRPFSGVDVL SGNFFESAVV
KISGMSTKQI DEFDKKVAFV LYYENEDEAN QGLLDVHLLE KLKHSRCFQH QSLLAALQHN
APHLFDEWKD REYDDLFDAM AKEGVLKIAV VIAGQGPEAF GMPEMFTPMQ HINANRQLKR
IATLISDGRY SGVTYGAAIG HMTPEAIRGG GILYLKTGDL LYIGLRERKI EFVNEWLFQN
GKLVFEFESV KQERAEIANQ RMANMRQRQR RIAASNRLIG HTDAAHGVVP LHIAEEAVYD
YKKDVVLPTV KKI
//
