ID A0A0Q9JJY7_9MICO Unreviewed; 573 AA.
AC A0A0Q9JJY7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:KRE29600.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:KRE29600.1};
GN ORFNames=ASG80_19390 {ECO:0000313|EMBL:KRE29600.1};
OS Agromyces sp. Soil535.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1736390 {ECO:0000313|EMBL:KRE29600.1, ECO:0000313|Proteomes:UP000051793};
RN [1] {ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|Proteomes:UP000051793};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE29600.1, ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|EMBL:KRE29600.1,
RC ECO:0000313|Proteomes:UP000051793};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRE29600.1}.
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DR EMBL; LMRW01000006; KRE29600.1; -; Genomic_DNA.
DR RefSeq; WP_056729484.1; NZ_LMRW01000006.1.
DR AlphaFoldDB; A0A0Q9JJY7; -.
DR STRING; 1736390.ASG80_19390; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000051793; Unassembled WGS sequence.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 1.
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; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KRE29600.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
SQ SEQUENCE 573 AA; 60807 MW; 0D672191E8979C57 CRC64;
MVNHLRSADW YQGTDRNAYI HRAWMRRGLP EDAFDGTRPQ IAIANTASDL TPCNMHLNEV
AESVKQGVWA GGGVPYNLPV VSLGETQVKP TAMLWRNMAA MAMEEMFRAN PIDGLVLLGG
CDKTIPALLM AAASVDIPAV VVPGGPMLTG HFRGQALGCG TDVWRLSEEA RAGTITNGEF
LQSEQSMIRS KGHCNTMGTA STMAIVAEAL GMTIPGFAGT PAADARLLSL SHDTGRLIVD
MVAAGRKPSD IMTRESFLNA IIAVAAVGGS TNSVVHLLAI AGRLGIDLTL DDFDAAGSRV
PVLANLQPSG TFLMDDLYRA GGVLALLSQV KDLLHPEPIT VTGVPLVDYL VDRPVYDETV
IFPREAPLMD DAGIAVLRGN LAPRGAIIKP AAATPALLQH VGPAVVFDSI EDLRARIDDP
DLDVTADSVL VLRGCGPRGY PGMPEVGNMP LPRKLLEQGV RDMVRISDAR MSGTAYGTVI
LHAAPEAAAG GPLAFVRTGD IIRLDVTGRS LSFDVTDEEL QSRSRTPASD AAYAAPVRGW
ERLYVDHVMQ ADTGADLDFL VGASGDKVSR ESH
//
