Curated BLAST for Genomes

 

Curated BLAST

Searching in Marinobacter adhaerens HP15 (Marino)

Found 65 curated entries in PaperBLAST's database that match '4.2.1.3' as complete word(s).

These curated entries have 51 distinct sequences.

Running ublast with E ≤ 0.01

Found 8 relevant proteins in Marinobacter adhaerens HP15, or try another query

HP15_3433: aconitate hydratase 1
is similar to:
PaperBLAST

HP15_3433: Aconitate hydratase (EC 4.2.1.3) from Marinobacter adhaerens

100% id,
100% cov

ACNA_ECOLI / P25516: Aconitate hydratase A; ACN; Aconitase; Iron-responsive protein-like; IRP-like; RNA-binding protein; Stationary phase enzyme; EC 4.2.1.3 from Escherichia coli
acnA: aconitate hydratase 1; EC 4.2.1.3 from Escherichia coli
P25516: aconitate hydratase (EC 4.2.1.3) from Escherichia coli

67% id,
100% cov

ACON_LEGPH / P37032: Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; IP210; Iron-responsive protein-like; IRP-like; Major iron-containing protein; MICP; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Legionella pneumophila

66% id,
100% cov

More...

HP15_1930: aconitate hydratase 1
is similar to:
PaperBLAST

ACNA_CUPNE / Q937N8: Aconitate hydratase A; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; Iron-responsive protein-like; IRP-like; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Cupriavidus necator

80% id,
100% cov

ACND_SHEON / Q8EJW3: 2-methylcitrate dehydratase (2-methyl-trans-aconitate forming); Aconitate hydratase; ACN; Aconitase; EC 4.2.1.117; EC 4.2.1.3 from Shewanella oneidensis

80% id,
99% cov

ACON_LEGPH / P37032: Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; IP210; Iron-responsive protein-like; IRP-like; Major iron-containing protein; MICP; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Legionella pneumophila

45% id,
98% cov

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HP15_2203: bifunctional aconitate hydratase 2/2-methylisocitrate dehydratase
is similar to:
PaperBLAST

ACNB_ECOLI / P36683: Aconitate hydratase B; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; 2-methyl-cis-aconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Escherichia coli
acnB / GB|AAZ86920.1: aconitate hydratas; EC 4.2.1.3 from Escherichia coli
P36683: aconitate hydratase (EC 4.2.1.3) from Escherichia coli

72% id,
99% cov

ACNB_SALTY / Q8ZRS8: Aconitate hydratase B; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; 2-methyl-cis-aconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Salmonella typhimurium

72% id,
99% cov

acnB / P56418: aconitase (EC 4.2.1.3) from Helicobacter pylori

57% id,
99% cov

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HP15_1928: 2-methylcitrate dehydratase PrpD
is similar to:
PaperBLAST

PRPD_CUPNE / Q937N6: 2-methylcitrate dehydratase; 2-MC dehydratase; Aconitate hydratase; ACN; Aconitase; EC 4.2.1.79; EC 4.2.1.3 from Cupriavidus necator

60% id,
100% cov

PRPD_SALTY / P74840: 2-methylcitrate dehydratase; 2-MC dehydratase; Aconitate hydratase; ACN; Aconitase; EC 4.2.1.79; EC 4.2.1.3 from Salmonella typhimurium

59% id,
100% cov

PRPD_ECOLI / P77243: 2-methylcitrate dehydratase; 2-MC dehydratase; (2S,3S)-2-methylcitrate dehydratase; Aconitate hydratase; ACN; Aconitase; EC 4.2.1.79; EC 4.2.1.3 from Escherichia coli

59% id,
100% cov

More...

HP15_2599: isopropylmalate isomerase large subunit
is similar to:
PaperBLAST

Q8RP87: aconitate hydratase (EC 4.2.1.3) from Bacteroides fragilis

27% id,
60% cov

ACON_BOVIN / P20004: Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus

27% id,
57% cov

ACON_HUMAN / Q99798: Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Homo sapiens
Q99798: aconitate hydratase (EC 4.2.1.3) from Homo sapiens

27% id,
57% cov

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HP15_1834: protein containing 3-isopropylmalate dehydratase, large subunit region domain
is similar to:
PaperBLAST

ACO1: aconitate hydratase; EC 4.2.1.3 from Candida albicans

26% id,
56% cov

Q9NFX3: aconitate hydratase (EC 4.2.1.3) from Drosophila melanogaster

25% id,
57% cov

Q9P7D4: aconitate hydratase (EC 4.2.1.3) from Schizosaccharomyces pombe

27% id,
48% cov

More...

HP15_2598: isopropylmalate isomerase small subunit
is similar to:
PaperBLAST

ACON_BOVIN / P20004: Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus

30% id,
15% cov

D3GQL0: aconitate hydratase (EC 4.2.1.3) from Citrus clementina

32% id,
14% cov

ACO1_ARATH / Q42560: Aconitate hydratase 1; Aconitase 1; Citrate hydro-lyase 1; EC 4.2.1.3 from Arabidopsis thaliana

32% id,
14% cov

More...

HP15_1833: isopropylmalate isomerase small subunit
is similar to:
PaperBLAST

ACNA_BACSU / P09339: Aconitate hydratase A; ACN; Aconitase; Aconitate/2-methylaconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.- from Bacillus subtilis
citB / P09339: aconitate hydratase (bifunctional aconitase) (EC 4.2.1.99; EC 4.2.1.3) from Bacillus subtilis
P09339: aconitate hydratase (EC 4.2.1.3) from Bacillus subtilis

28% id,
14% cov

ACON_ASPFU / Q4WLN1: Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; Homocitrate dehydratase; EC 4.2.1.3; EC 4.2.1.- from Aspergillus fumigatus

36% id,
11% cov

ACON_EMENI / C8VG90: Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; Homocitrate dehydratase; EC 4.2.1.3; EC 4.2.1.- from Emericella nidulans

35% id,
11% cov

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The hits are sorted by %identity * %coverage (highest first)

Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.

Found hits to 8 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory