Family Search for TIGR00110

TIGR00110 hits 142 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

IlvD / b3771 dihydroxy-acid dehydratase (EC 4.2.1.9) from Escherichia coli K-12 substr. MG1655 (see paper)
ilvD / P05791 dihydroxy-acid dehydratase (EC 4.2.1.9) from Escherichia coli (strain K12) (see 14 papers)
ILVD_ECOLI / P05791 Dihydroxy-acid dehydratase; DAD; EC 4.2.1.9 from Escherichia coli (strain K12) (see 4 papers)
Aligns to 17:611 / 616 (96.6%), covers 99.6% of TIGR00110, 908.4 bits

• function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
  catalytic activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (RHEA:24809)
  catalytic activity: (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2- oxopentanoate + H2O (RHEA:27694)
  cofactor: [2Fe-2S] cluster (Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.)
  cofactor: Mg(2+)
  subunit: Homodimer.

ilvDD / O27498 dihydroxy-acid dehydratase subunit (EC 4.2.1.9) from Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (see 4 papers)
Aligns to 14:549 / 549 (97.6%), covers 99.8% of TIGR00110, 882.3 bits

ILVD_RHIJ3 / Q1MIB2 Dihydroxy-acid dehydratase; DAD; EC 4.2.1.9 from Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841) (Rhizobium leguminosarum bv. viciae) (see paper)
Aligns to 17:609 / 612 (96.9%), covers 99.6% of TIGR00110, 845.0 bits

• function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
  catalytic activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (RHEA:24809)
  catalytic activity: (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2- oxopentanoate + H2O (RHEA:27694)
  cofactor: [2Fe-2S] cluster (Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.)
  cofactor: Mg(2+)
  subunit: Homodimer.
  disruption phenotype: Does not nodulate the roots of pea plants.

ILV3_YEAST / P39522 Dihydroxy-acid dehydratase, mitochondrial; DAD; EC 4.2.1.9 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 13 papers)
Aligns to 38:585 / 585 (93.7%), covers 99.6% of TIGR00110, 838.2 bits

• function: Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids (PubMed:20008079, PubMed:21798060, PubMed:21987576, PubMed:22954227, PubMed:25280745, PubMed:26543501, PubMed:27532773, PubMed:28505306, PubMed:30850698, PubMed:31303893, PubMed:33620449, PubMed:8299945). Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3- methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3- methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3- methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L- valine, respectively (PubMed:20008079, PubMed:27532773). Required for the synthesis of alpha-isopropylmalate which modulates the activity of LEU3 and subsequently regulates the expression of LEU1 (PubMed:20008079).
  catalytic activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (RHEA:24809)
  catalytic activity: (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2- oxopentanoate + H2O (RHEA:27694)
  cofactor: [2Fe-2S] cluster (Binds 1 [2Fe-2S] cluster per subunit.)
  cofactor: Mg(2+)
  disruption phenotype: Strongly reduces the iron responsiveness of expression of LEU1 by affecting the synthesis of alpha-isopropylmalate.

ILVD_CAUVC / P55186 Dihydroxy-acid dehydratase; DAD; EC 4.2.1.9 from Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus) (see paper)
Aligns to 17:611 / 617 (96.4%), covers 99.6% of TIGR00110, 811.0 bits

• function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
  catalytic activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (RHEA:24809)
  catalytic activity: (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2- oxopentanoate + H2O (RHEA:27694)
  cofactor: [2Fe-2S] cluster (Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.)
  cofactor: Mg(2+)
  subunit: Homodimer.

Q8NQZ9 dihydroxy-acid dehydratase (EC 4.2.1.9) from Corynebacterium glutamicum (see 2 papers)
Aligns to 17:612 / 613 (97.2%), covers 99.6% of TIGR00110, 784.3 bits

ilvD / Q0K7F8 dihydroxyacid dehydratase (EC 4.2.1.9) from Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (see paper)
Q0K7F8 dihydroxy-acid dehydratase (EC 4.2.1.9) from Cupriavidus necator (see paper)
Aligns to 18:557 / 557 (96.9%), covers 99.8% of TIGR00110, 748.2 bits

A0A481UJA7 dihydroxy-acid dehydratase (EC 4.2.1.9) from Hevea brasiliensis (see paper)
Aligns to 74:614 / 614 (88.1%), covers 99.6% of TIGR00110, 742.6 bits

ILVD_ARATH / Q9LIR4 Dihydroxy-acid dehydratase, chloroplastic; AthDHAD; DAD; EC 4.2.1.9 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
Q9LIR4 dihydroxy-acid dehydratase (EC 4.2.1.9) from Arabidopsis thaliana (see 2 papers)
Aligns to 68:608 / 608 (89.0%), covers 99.6% of TIGR00110, 734.0 bits

• function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively.
  catalytic activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (RHEA:24809)
  catalytic activity: (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2- oxopentanoate + H2O (RHEA:27694)
  cofactor: [2Fe-2S] cluster (Binds 1 [2Fe-2S] cluster per subunit.)
  cofactor: Mg(2+)

ILVC_ASPFU / Q4X099 Dihydroxy-acid dehydratase ilvC, mitochondrial; DHAD ilvC; EC 4.2.1.9 from Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata) (see paper)
Aligns to 52:604 / 606 (91.3%), covers 99.6% of TIGR00110, 728.9 bits

• function: Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to biosynthesis of branched-chain amino acids (PubMed:23028460). Catalyzes the dehydration of (2R,3R)-2,3- dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2- oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3- dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3- methylbutanoate (2-oxoisovalerate), the penultimate precursor to L- isoleucine and L-valine, respectively (By similarity). IlvC and the branched-chain amino acid biosynthesis are crucial for virulence and may be a potential target to develop antifungal agents (PubMed:23028460).
  catalytic activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (RHEA:24809)
  catalytic activity: (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2- oxopentanoate + H2O (RHEA:27694)
  cofactor: [2Fe-2S] cluster (Binds 1 [2Fe-2S] cluster per subunit.)
  cofactor: Mg(2+)
  disruption phenotype: Requires supplementation with isoleucine and valine for growth (PubMed:23028460). Results in considerably lower kidney tissue burden in murine infection models (PubMed:23028460).

Q97UB2 dihydroxy-acid dehydratase (EC 4.2.1.9) from Saccharolobus solfataricus (see 2 papers)
Aligns to 18:557 / 558 (96.8%), covers 99.8% of TIGR00110, 716.3 bits

ILVD_MYCTU / P9WKJ5 Dihydroxy-acid dehydratase; DAD; EC 4.2.1.9 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
Aligns to 32:575 / 575 (94.6%), covers 99.3% of TIGR00110, 711.4 bits

• function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo- 3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3- dihydroxyisovalerate) into 2-oxo-3-methylbutanoate (2-oxoisovalerate), the penultimate precursor to L-isoleucine and L-valine, respectively. Is specific for the (R) isomer of 2,3-dihydroxy-3-methylbutanoate, with no catalytic activity against the (S) isomer.
  catalytic activity: (2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O (RHEA:24809)
  catalytic activity: (2R,3R)-2,3-dihydroxy-3-methylpentanoate = (S)-3-methyl-2- oxopentanoate + H2O (RHEA:27694)
  cofactor: [2Fe-2S] cluster (Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.)
  cofactor: Mg(2+)
  subunit: Homodimer.
  disruption phenotype: Cells lacking this gene display impaired growth.

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