ID A0A444ZCI6_ARAHY Unreviewed; 572 AA.
AC A0A444ZCI6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 15.
DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Ahy_B04g069398 {ECO:0000313|EMBL:RYR11879.1};
OS Arachis hypogaea (Peanut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC dalbergioids sensu lato; Dalbergieae; Pterocarpus clade; Arachis.
OX NCBI_TaxID=3818 {ECO:0000313|EMBL:RYR11879.1, ECO:0000313|Proteomes:UP000289738};
RN [1] {ECO:0000313|EMBL:RYR11879.1, ECO:0000313|Proteomes:UP000289738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Fuhuasheng {ECO:0000313|Proteomes:UP000289738};
RC TISSUE=Leaves {ECO:0000313|EMBL:RYR11879.1};
RA Chen X.;
RT "Sequencing of cultivated peanut Arachis hypogaea provides insights into
RT genome evolution and oil improvement.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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:RYR11879.1}.
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DR EMBL; SDMP01000014; RYR11879.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A444ZCI6; -.
DR STRING; 3818.A0A444ZCI6; -.
DR Proteomes; UP000289738; Chromosome b04.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 2.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR PANTHER; PTHR21000; DIHYDROXY-ACID DEHYDRATASE DAD; 1.
DR PANTHER; PTHR21000:SF5; DIHYDROXY-ACID DEHYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00920; ILVD_EDD; 2.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00887; ILVD_EDD_2; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000289738}.
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 61727 MW; 1BA698DB03C9973D CRC64;
MQSTLFLPTS LPTLHRRTLP FFSIRASQSS PSVTVDSPPE SSSAAAATQK LNKYSSRITQ
PKSQGASQAV LYGVGLSEDD MDKPQIGVSS VWYEGNTCNM HLLELSEAVK EGVREAGMIP
FRFNTIGVSD AISMGTRGMC YSLQSRDLIA DSIETVMSAQ WYDGNISIPG CDKNMPGTIM
AMGRLNRPSI MVYGGTIKPG HFQGNTFDIV SAFQIYGEYV SGSIDDQYRQ NVLRNSCPGA
GACGGMYTAN TMASAIEAMG MSLPYSSSTP AEDPLKLDEC RLAGKYLLEL LKMDLKPRDI
ITRKSLRNAM VIVMALGGST NAVLHLIAIA KSVGIELSLD DFQKVSDEVP FLADLKPSGK
YVMEDVHKIG GTPAVIRYLL EQGFLEGDCL TVTGRTLAEN SELVPPLSPG QEIIRPIENP
IKKTAHIQIL YGNLAPQGSV AKITGKEGLY FSGPALVFEG EESMIAAISE DPSSFKEVAL
LTDGRFSGGS HGFVVGHICP EAQEGGPIGL IQNGDVINID VQKRRIDTLV SDEEMEARKK
KWSAPPYKAN QGVLYKYIKN VKSASSGCVT DE
//