ID A0A142XAS8_9BACT Unreviewed; 651 AA.
AC A0A142XAS8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Dihydroxy-acid dehydratase {ECO:0000313|EMBL:AMV23520.1};
DE EC=4.2.1.9 {ECO:0000313|EMBL:AMV23520.1};
GN Name=ilvD_1 {ECO:0000313|EMBL:AMV23520.1};
GN ORFNames=VT84_03860 {ECO:0000313|EMBL:AMV23520.1};
OS Gemmata sp. SH-PL17.
OC Bacteria; Planctomycetota; Planctomycetia; Gemmatales; Gemmataceae;
OC Gemmata.
OX NCBI_TaxID=1630693 {ECO:0000313|EMBL:AMV23520.1, ECO:0000313|Proteomes:UP000076098};
RN [1] {ECO:0000313|EMBL:AMV23520.1, ECO:0000313|Proteomes:UP000076098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH-PL17 {ECO:0000313|EMBL:AMV23520.1,
RC ECO:0000313|Proteomes:UP000076098};
RA van der Voort M., Raaijmakers J.M.;
RT "Genome minning of novel planctomycete species.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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DR EMBL; CP011271; AMV23520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A142XAS8; -.
DR STRING; 1630693.VT84_03860; -.
DR KEGG; ges:VT84_03860; -.
DR PATRIC; fig|1630693.3.peg.826; -.
DR OrthoDB; 9807077at2; -.
DR Proteomes; UP000076098; Chromosome.
DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0050401; F:xylonate dehydratase 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; 1.
DR InterPro; IPR017798; Dehydratase_YjhG/YagF.
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 NCBIfam; TIGR03432; yjhG_yagF; 1.
DR PANTHER; PTHR43661; D-XYLONATE DEHYDRATASE; 1.
DR PANTHER; PTHR43661:SF3; D-XYLONATE DEHYDRATASE YAGF-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 Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:AMV23520.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000076098}.
SQ SEQUENCE 651 AA; 68960 MW; 1568F291D764762E CRC64;
MPSDVLDTPE SAYQIVTTGS GPKGALPLTD ELLRHSPSGN LFGWTQNVGM GWNPALLGGK
EFTILSTHGG LRAEDGTPIA LGFHSGHWEV GLLVKAAAEE FARLRCVPFA GAITDPCDGR
TQGTAGMYDS LPYRNDSSQV MRRLMRSHPT RAGVMGIATC DKGLPAMMMA LASQHDHPTI
LVPGGVMLAG EADHEDTGKV QTIGARYAHG EMTIEEAADA GCHACASPGG GCQFLGTAAT
SQVIGEALGL SLPHSALAPS GQPIWLDMAT RSARALVNMT NRGIRTPHIL TEAAFKNALA
VFAAFGGSTN LLLHTPAIAF HAGIKRPTIE DWTFYNRKVP RLVDALPNGP MNHPTMRVFL
AGGVPEVMLH LRELGLLELD ALTASGETLG SNLDWWAKSE RRTRLRELLR TRDRVDPDTV
IMSPDAARKR GLTSTVTFPT GNLAPDGCVI KSTAIDPAVV DKDGVYRKLG PAKVFIREKD
AIKAIKGEGE RKVVPGDVLV LCCRGPMGSG MEETYQVTSA LKHLKWGKQV AVITDARFSG
VSTGACIGHV SPEALVGGPI GKLRDGDLVQ IIIDRNKLEG TIDLVGDATG NHGPLWGGAE
LQARAPRPDL APDPALPADT RLWAALQHAS GGVWGGCVYD PDLIAAKLAG R
//