Comparing H281DRAFT_05434 H281DRAFT_05434 Predicted amidohydrolase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
3klcB Crystal structure of hyperthermophilic nitrilase (see paper)
43% identity, 90% coverage: 18:285/298 of query aligns to 3:259/261 of 3klcB
Sites not aligning to the query:
3klcA Crystal structure of hyperthermophilic nitrilase (see paper)
43% identity, 90% coverage: 18:285/298 of query aligns to 3:259/261 of 3klcA
Q9UYV8 Nitrilase; PaNit; EC 3.5.5.1 from Pyrococcus abyssi (strain GE5 / Orsay) (see paper)
43% identity, 90% coverage: 18:285/298 of query aligns to 4:260/262 of Q9UYV8
6ypaB The c146a variant of an amidase from pyrococcus horikoshii with bound glutaramide
41% identity, 92% coverage: 11:285/298 of query aligns to 4:267/269 of 6ypaB
7ovgA The c146a variant of an amidase from pyrococcus horikoshii with bound acetamide (see paper)
42% identity, 90% coverage: 18:285/298 of query aligns to 5:261/263 of 7ovgA
5h8jB Crystal structure of medicago truncatula n-carbamoylputrescine amidohydrolase (mtcpa) in complex with cadaverine (see paper)
31% identity, 86% coverage: 33:289/298 of query aligns to 21:288/297 of 5h8jB
5h8iC Crystal structure of medicago truncatula n-carbamoylputrescine amidohydrolase (mtcpa) in complex with n-(dihydroxymethyl)putrescine (see paper)
31% identity, 86% coverage: 33:289/298 of query aligns to 25:292/301 of 5h8iC
5h8lB Crystal structure of medicago truncatula n-carbamoylputrescine amidohydrolase (mtcpa) c158s mutant in complex with putrescine (see paper)
31% identity, 86% coverage: 33:289/298 of query aligns to 22:289/298 of 5h8lB
Q44185 N-carbamoyl-D-amino acid hydrolase; D-N-alpha-carbamilase; EC 3.5.1.77 from Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter) (see paper)
30% identity, 81% coverage: 30:269/298 of query aligns to 21:284/304 of Q44185
Q9NQR4 Omega-amidase NIT2; Nitrilase homolog 2; EC 3.5.1.3 from Homo sapiens (Human) (see 2 papers)
31% identity, 86% coverage: 30:285/298 of query aligns to 17:269/276 of Q9NQR4
8hpcC Crystal structure of c171a mutant of n-carbamyl-d-amino acid amidohydrolase complexed with n-carbamyl-d-hydroxyphenylglycine
30% identity, 81% coverage: 30:269/298 of query aligns to 20:283/303 of 8hpcC
1uf8A Crystal structure of c171a/v236a mutant of n-carbamyl-d-amino acid amidohydrolase complexed with n-carbamyl-d-phenylalanine
30% identity, 81% coverage: 30:269/298 of query aligns to 20:283/303 of 1uf8A
1uf7A Crystal structure of c171a/v236a mutant of n-carbamyl-d-amino acid amidohydrolase complexed with n-carbamyl-d-valine
30% identity, 81% coverage: 30:269/298 of query aligns to 20:283/303 of 1uf7A
1uf5A Crystal structure of c171a/v236a mutant of n-carbamyl-d-amino acid amidohydrolase complexed with n-carbamyl-d-methionine
30% identity, 81% coverage: 30:269/298 of query aligns to 20:283/303 of 1uf5A
O25067 Aliphatic amidase; Acylamide amidohydrolase; EC 3.5.1.4 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
32% identity, 82% coverage: 29:271/298 of query aligns to 33:269/339 of O25067
4gylA The e142l mutant of the amidase from geobacillus pallidus showing the result of michael addition of acrylamide at the active site cysteine (see paper)
32% identity, 78% coverage: 48:278/298 of query aligns to 51:278/340 of 4gylA
Q9RQ17 Aliphatic amidase; Acylamide amidohydrolase; Wide spectrum amidase; EC 3.5.1.4 from Geobacillus stearothermophilus (Bacillus stearothermophilus) (see paper)
32% identity, 87% coverage: 21:278/298 of query aligns to 25:278/348 of Q9RQ17
Q03217 Aliphatic nitrilase; EC 3.5.5.7 from Rhodococcus rhodochrous (see paper)
28% identity, 88% coverage: 18:278/298 of query aligns to 10:300/366 of Q03217
4iztA The e41q mutant of the amidase from nesterenkonia sp. An1 showing covalent addition of the acetamide moiety of fluoroacetamide at the active site cysteine
33% identity, 69% coverage: 37:243/298 of query aligns to 27:231/263 of 4iztA
4izuA The e41q mutant of the amidase from nesterenkonia sp. An1 showing the result of michael addition of acrylamide at the active site cysteine
33% identity, 69% coverage: 37:243/298 of query aligns to 19:223/254 of 4izuA
Sites not aligning to the query:
>H281DRAFT_05434 H281DRAFT_05434 Predicted amidohydrolase
MEMLQRNHAERGLASPVVACVQMEPHVGEKQANVARSIKLIEEAAEHGASLVVLPELANT
GYVFSDRDEAFTLAEDVPSGETALAWADAAQRLGVHVVAGIAERDRVRLYNSALLVGPSG
IVGTYRKLHLWNNENLFFEPGNKGVPVFHTPLGRIAIAICYDGWFPEVYRLAATQGADLV
CVPTNWVPMQGQPADQPAMATTLTMAAAHSNGLMVACANRIGTERGQLFVGQSLIVGGDG
WPLAGPVSSDHEEILYAEIDLNRTRAGRNLNPFNHVLRDRRTDVYDPMLGTGWPPSPS
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory