Curated BLAST

Curated BLAST for Genomes

Curated BLAST

Searching in Pseudomonas stutzeri RCH2 (psRCH2)

Found 110 curated entries in PaperBLAST's database that match '4.3.1.1'.

These curated entries have 73 distinct sequences.

Running ublast with E ≤ 0.01

Found 7 relevant proteins in Pseudomonas stutzeri RCH2, or try another query

Psest_4074: Aspartate ammonia-lyase is similar to:	PaperBLAST
Q9HTD7: aspartate ammonia-lyase (EC 4.3.1.1) from Pseudomonas aeruginosa	86% id, 100% cov
Q0PC50: aspartate ammonia-lyase (EC 4.3.1.1) from Campylobacter jejuni	57% id, 99% cov
ASPA_ECOLI / P0AC38: Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Escherichia coli AspA / b4139: aspartate ammonia-lyase (EC 4.3.1.1) from Escherichia coli aspA / P0AC38: aspartate ammonia-lyase (EC 4.3.1.1) from Escherichia coli P0AC38: aspartate ammonia-lyase (EC 4.3.1.1) from Escherichia coli	55% id, 96% cov
Q9LCC6: aspartate ammonia-lyase (EC 4.3.1.1) from Bacillus sp.	50% id, 98% cov
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Psest_0784: L-serine dehydratase, iron-sulfur-dependent, single chain form is similar to:	PaperBLAST
Pf6N2E2_5557: L-serine ammonia-lyase (EC 4.3.1.17) from Pseudomonas fluorescens	81% id, 100% cov
RR42_RS20080: L-serine ammonia-lyase (EC 4.3.1.17) from Cupriavidus basilensis	66% id, 100% cov
BPHYT_RS19340: L-serine ammonia-lyase (EC 4.3.1.17) from Burkholderia phytofirmans	65% id, 100% cov
Ac3H11_929: L-serine ammonia-lyase (EC 4.3.1.17) from Acidovorax sp.	65% id, 100% cov
PfGW456L13_4954: L-serine ammonia-lyase (EC 4.3.1.17) from Pseudomonas fluorescens	61% id, 100% cov
AO353_15500: L-serine ammonia-lyase (EC 4.3.1.17) from Pseudomonas fluorescens	61% id, 100% cov
Pf1N1B4_1013: L-serine ammonia-lyase (EC 4.3.1.17) from Pseudomonas fluorescens	61% id, 100% cov
Q5ZXE1: L-serine ammonia-lyase (EC 4.3.1.17) from Legionella pneumophila	58% id, 100% cov
YhaQ / b4471: L-serine deaminase III (EC 4.3.1.17) from Escherichia coli tdcG / P42630: L-serine deaminase III (EC 4.3.1.17) from Escherichia coli P42630: L-serine ammonia-lyase (EC 4.3.1.17) from Escherichia coli	55% id, 99% cov
SDHM_ECOLI / P30744: L-serine dehydratase 2; SDH 2; L-serine deaminase 2; L-SD2; EC 4.3.1.17 from Escherichia coli SdaB / b2797: L-serine deaminase II (EC 4.3.1.17) from Escherichia coli sdaB / GB\|AAC75839.1: L-serine dehydratase 2; EC 4.3.1.17 from Escherichia coli sdaB / P30744: L-serine deaminase II (EC 4.3.1.17) from Escherichia coli P30744: L-serine ammonia-lyase (EC 4.3.1.17) from Escherichia coli	53% id, 100% cov
SdaA / b1814: L-serine deaminase I (EC 4.3.1.17) from Escherichia coli sdaA / P16095: L-serine deaminase I (EC 4.3.1.17) from Escherichia coli P16095: L-serine ammonia-lyase (EC 4.3.1.17) from Escherichia coli	53% id, 100% cov
sdaA / RF\|YP_225930.1: L-serine ammonia-lyase; EC 4.3.1.17 from Corynebacterium glutamicum sdaA / Q8NQ09: L-serine dehydratase (EC 4.3.1.17) from Corynebacterium glutamicum	51% id, 100% cov
DvMF_0011: L-serine ammonia-lyase (EC 4.3.1.17) from Desulfovibrio vulgaris	44% id, 98% cov
sdhA / P33073: L-serine dehydratase α subunit (EC 4.3.1.17) from Peptoniphilus asaccharolyticus	32% id, 94% cov
sdhB / P33074: L-serine dehydratase β subunit (EC 4.3.1.17) from Peptoniphilus asaccharolyticus	26% id, 61% cov
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Psest_3866: threonine ammonia-lyase, biosynthetic, long form is similar to:	PaperBLAST
ILVA_ECOLI / P04968: L-threonine dehydratase biosynthetic IlvA; Threonine deaminase; EC 4.3.1.19 from Escherichia coli Ile / b3772: threonine deaminase (EC 4.3.1.19) from Escherichia coli ilvA / P04968: threonine deaminase (EC 4.3.1.19) from Escherichia coli P04968: threonine ammonia-lyase (EC 4.3.1.19) from Escherichia coli	52% id, 97% cov
THDH_YEAST / P00927: Threonine dehydratase, mitochondrial; Threonine deaminase; EC 4.3.1.19 from Saccharomyces cerevisiae	51% id, 89% cov
V6QU65: threonine ammonia-lyase (EC 4.3.1.19) from Fusarium graminearum	51% id, 87% cov
TD1_SOLLC / A0FKE6: Threonine dehydratase 1 biosynthetic, chloroplastic; SlTD1; Threonine deaminase 1; EC 4.3.1.19 from Solanum lycopersicum	53% id, 82% cov
TD_SOLTU / P31212: Threonine dehydratase biosynthetic, chloroplastic; Threonine deaminase; EC 4.3.1.19 from Solanum tuberosum	42% id, 100% cov
TD_NICAT / Q9AXU4: Threonine dehydratase; Threonine deaminase; EC 4.3.1.19 from Nicotiana attenuata Q9AXU4: threonine ammonia-lyase (EC 4.3.1.19) from Nicotiana attenuata	50% id, 83% cov
THDH_SCHPO / O94634: Threonine dehydratase, mitochondrial; Threonine deaminase; EC 4.3.1.19 from Schizosaccharomyces pombe	48% id, 84% cov
TD2_SOLLC / P25306: Threonine dehydratase 2 biosynthetic, chloroplastic; SlTD2; Threonine deaminase 2; EC 4.3.1.17; EC 4.3.1.19 from Solanum lycopersicum	46% id, 84% cov
TDCB_SALTY / P11954: L-threonine dehydratase catabolic TdcB; L-serine dehydratase; Threonine deaminase; EC 4.3.1.19; EC 4.3.1.17 from Salmonella typhimurium	40% id, 94% cov
CA265_RS15860: threonine deaminase (EC 4.3.1.19) from Pedobacter sp.	39% id, 95% cov
A0QY48: L-serine ammonia-lyase (EC 4.3.1.17) from Mycolicibacterium smegmatis	40% id, 93% cov
TDCB_ECOLI / P0AGF6: L-threonine dehydratase catabolic TdcB; L-serine dehydratase; Threonine deaminase; EC 4.3.1.19; EC 4.3.1.17 from Escherichia coli Tdc / b3117: catabolic threonine dehydratase (EC 4.3.1.17; EC 4.3.1.19) from Escherichia coli tdcB / RF\|NP_417587: threonine ammonia-lyase; EC 4.3.1.19 from Escherichia coli tdcB / P0AGF6: catabolic threonine dehydratase (EC 4.3.1.17; EC 4.3.1.19) from Escherichia coli	39% id, 94% cov
A0QX60: threonine ammonia-lyase (EC 4.3.1.19) from Mycolicibacterium smegmatis	41% id, 88% cov
LTHAD_YEAST / P36007: L-threo-3-hydroxyaspartate ammonia-lyase; L-threo-3-hydroxyaspartate dehydratase; EC 4.3.1.16 from Saccharomyces cerevisiae	38% id, 95% cov
SRR_ARATH / Q2PGG3: Serine racemase; AtSR; D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase; EC 4.3.1.17; EC 4.3.1.18; EC 5.1.1.18 from Arabidopsis thaliana	37% id, 96% cov
LTHAD_PSESP / A4F2N8: L-threo-3-hydroxyaspartate ammonia-lyase; L-threo-3-hydroxyaspartate dehydratase; L-THA DH; EC 4.3.1.16 from Pseudomonas sp. thadh / A4F2N8: L-threo-3-hydroxy aspartate ammonia-lyase (EC 4.3.1.16) from Pseudomonas sp. A4F2N8: threo-3-hydroxy-L-aspartate ammonia-lyase (EC 4.3.1.16) from Pseudomonas sp.	37% id, 96% cov
L0N5C4: threo-3-hydroxy-L-aspartate ammonia-lyase (EC 4.3.1.16) from Pseudomonas sp.	36% id, 95% cov
Q04513: threonine ammonia-lyase (EC 4.3.1.19) from Corynebacterium glutamicum	40% id, 85% cov
TSAL_THEMA / Q9WYJ1: L-threonine ammonia-lyase; L-serine ammonia-lyase; Threonine dehydratase; EC 4.3.1.19; EC 4.3.1.17 from Thermotoga maritima	39% id, 86% cov
SRR_RAT / Q76EQ0: Serine racemase; D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase; EC 5.1.1.18; EC 4.3.1.18; EC 4.3.1.17 from Rattus norvegicus	36% id, 94% cov
SRR_SCHPO / O59791: Serine racemase; D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase; EC 4.3.1.17; EC 4.3.1.18; EC 5.1.1.18 from Schizosaccharomyces pombe	36% id, 94% cov
CCNA_03750: threonine deaminase (EC 4.3.1.19) from Caulobacter crescentus	35% id, 94% cov
SRR_MOUSE / Q9QZX7: Serine racemase; D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase; EC 5.1.1.18; EC 4.3.1.18; EC 4.3.1.17 from Mus musculus	37% id, 90% cov
TSAL_GEOSL / Q74FW6: L-threonine ammonia-lyase; L-serine ammonia-lyase; Threonine/serine ammonia-lyase; EC 4.3.1.19; EC 4.3.1.17 from Geobacter sulfurreducens Q74FW6: threonine ammonia-lyase (EC 4.3.1.19) from Geobacter sulfurreducens	37% id, 87% cov
B1N2N4: L-serine ammonia-lyase (EC 4.3.1.17) from Entamoeba histolytica	38% id, 85% cov
SRR_HUMAN / Q9GZT4: Serine racemase; D-serine ammonia-lyase; D-serine dehydratase; L-serine ammonia-lyase; L-serine dehydratase; EC 5.1.1.18; EC 4.3.1.18; EC 4.3.1.17 from Homo sapiens	37% id, 86% cov
Q54HH2: D-Serine ammonia-lyase (EC 4.3.1.18) from Dictyostelium discoideum	33% id, 94% cov
SRR_ORYSJ / Q7XSN8: Serine racemase; D-serine dehydratase; D-serine ammonia-lyase; L-serine dehydratase; L-serine ammonia-lyase; EC 5.1.1.18; EC 4.3.1.18; EC 4.3.1.17 from Oryza sativa	33% id, 92% cov
Ga0059261_3694: threonine deaminase (EC 4.3.1.19) from Sphingomonas koreensis	33% id, 92% cov
SDSL_HUMAN / Q96GA7: Serine dehydratase-like; L-serine deaminase; L-serine dehydratase/L-threonine deaminase; L-threonine dehydratase; TDH; Serine dehydratase 2; SDH 2; EC 4.3.1.19; EC 4.3.1.17 from Homo sapiens SDSL / Q96GA7: Serine dehydratase-like (EC 4.3.1.19; EC 4.3.1.17) from Homo sapiens Q96GA7: L-serine ammonia-lyase (EC 4.3.1.17) from Homo sapiens	30% id, 95% cov
SDHL_HUMAN / P20132: L-serine dehydratase/L-threonine deaminase; SDH; L-serine deaminase; L-threonine dehydratase; TDH; EC 4.3.1.17; EC 4.3.1.19 from Homo sapiens SDS / P20132: L-serine dehydratase (EC 4.3.1.19; EC 4.3.1.17) from Homo sapiens P20132: L-serine ammonia-lyase (EC 4.3.1.17) from Homo sapiens	29% id, 95% cov
SDSL_MOUSE / Q8R238: Serine dehydratase-like; L-serine deaminase; L-serine dehydratase/L-threonine deaminase; L-threonine dehydratase; TDH; SDH; EC 4.3.1.17; EC 4.3.1.19 from Mus musculus	29% id, 94% cov
P09367: L-serine ammonia-lyase (EC 4.3.1.17) from Rattus norvegicus	29% id, 71% cov
DPAL_SALTY / P40817: Diaminopropionate ammonia-lyase; DAPAL; 2,3-diaminopropionate ammonia-lyase; Alpha,beta-diaminopropionate ammonia-lyase; Diaminopropionatase; EC 4.3.1.15 from Salmonella typhimurium P40817: Diaminopropionate ammonia-lyase (EC 4.3.1.15) from Salmonella enterica	26% id, 76% cov
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Psest_2682: fumarate hydratase, class II is similar to:	PaperBLAST
Q9LCC6: aspartate ammonia-lyase (EC 4.3.1.1) from Bacillus sp.	42% id, 98% cov
Q9HTD7: aspartate ammonia-lyase (EC 4.3.1.1) from Pseudomonas aeruginosa	41% id, 97% cov
ASPA_ECOLI / P0AC38: Aspartate ammonia-lyase; Aspartase; EC 4.3.1.1 from Escherichia coli AspA / b4139: aspartate ammonia-lyase (EC 4.3.1.1) from Escherichia coli aspA / P0AC38: aspartate ammonia-lyase (EC 4.3.1.1) from Escherichia coli P0AC38: aspartate ammonia-lyase (EC 4.3.1.1) from Escherichia coli	40% id, 94% cov
Q0PC50: aspartate ammonia-lyase (EC 4.3.1.1) from Campylobacter jejuni	38% id, 98% cov
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Psest_2636: tryptophan synthase, beta subunit is similar to:	PaperBLAST
TDCB_SALTY / P11954: L-threonine dehydratase catabolic TdcB; L-serine dehydratase; Threonine deaminase; EC 4.3.1.19; EC 4.3.1.17 from Salmonella typhimurium	22% id, 98% cov
Q04513: threonine ammonia-lyase (EC 4.3.1.19) from Corynebacterium glutamicum	27% id, 73% cov
TSAL_THEMA / Q9WYJ1: L-threonine ammonia-lyase; L-serine ammonia-lyase; Threonine dehydratase; EC 4.3.1.19; EC 4.3.1.17 from Thermotoga maritima	32% id, 51% cov
TDCB_ECOLI / P0AGF6: L-threonine dehydratase catabolic TdcB; L-serine dehydratase; Threonine deaminase; EC 4.3.1.19; EC 4.3.1.17 from Escherichia coli Tdc / b3117: catabolic threonine dehydratase (EC 4.3.1.17; EC 4.3.1.19) from Escherichia coli tdcB / RF\|NP_417587: threonine ammonia-lyase; EC 4.3.1.19 from Escherichia coli tdcB / P0AGF6: catabolic threonine dehydratase (EC 4.3.1.17; EC 4.3.1.19) from Escherichia coli	23% id, 62% cov
CCNA_03750: threonine deaminase (EC 4.3.1.19) from Caulobacter crescentus	27% id, 46% cov
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Psest_0063: tryptophan synthase, beta subunit is similar to:	PaperBLAST
Q04513: threonine ammonia-lyase (EC 4.3.1.19) from Corynebacterium glutamicum	27% id, 68% cov
B1N2N4: L-serine ammonia-lyase (EC 4.3.1.17) from Entamoeba histolytica	28% id, 54% cov
TD1_SOLLC / A0FKE6: Threonine dehydratase 1 biosynthetic, chloroplastic; SlTD1; Threonine deaminase 1; EC 4.3.1.19 from Solanum lycopersicum	24% id, 50% cov
TSAL_GEOSL / Q74FW6: L-threonine ammonia-lyase; L-serine ammonia-lyase; Threonine/serine ammonia-lyase; EC 4.3.1.19; EC 4.3.1.17 from Geobacter sulfurreducens Q74FW6: threonine ammonia-lyase (EC 4.3.1.19) from Geobacter sulfurreducens	29% id, 23% cov
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Psest_2551: 1-aminocyclopropane-1-carboxylate deaminase is similar to:	PaperBLAST
O57809: L-serine ammonia-lyase (EC 4.3.1.17); D-Serine ammonia-lyase (EC 4.3.1.18) from Pyrococcus horikoshii	33% id, 51% cov

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 7 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory