SitesBLAST
Comparing WP_092350282.1 NCBI__GCF_900107645.1:WP_092350282.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
31% identity, 91% coverage: 32:451/463 of query aligns to 12:442/448 of 4ysnC
- active site: A29 (≠ S49), Y149 (≠ F166), E224 (= E234), D257 (= D266), N260 (≠ P269), K287 (= K295), T316 (= T325), R415 (≠ T424)
- binding pyridoxal-5'-phosphate: S121 (≠ G138), G122 (= G139), S123 (≠ T140), Y149 (≠ F166), H150 (= H167), E224 (= E234), D257 (= D266), V259 (≠ I268), K287 (= K295), F315 (≠ Y324), T316 (= T325)
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
31% identity, 91% coverage: 32:451/463 of query aligns to 3:433/439 of 5wyaA
- active site: A20 (≠ S49), Y140 (≠ F166), E215 (= E234), D248 (= D266), N251 (≠ P269), K278 (= K295), T307 (= T325), R406 (≠ T424)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ S81), Y82 (≠ R109), S112 (≠ G138), G113 (= G139), S114 (≠ T140), Y140 (≠ F166), H141 (= H167), E215 (= E234), D248 (= D266), V250 (≠ I268), N251 (≠ P269), K278 (= K295), F306 (≠ Y324), T307 (= T325), R406 (≠ T424)
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
31% identity, 91% coverage: 32:451/463 of query aligns to 5:435/446 of 5wyfA
- active site: A22 (≠ S49), Y142 (≠ F166), E217 (= E234), D250 (= D266), N253 (≠ P269), K280 (= K295), T309 (= T325), R408 (≠ T424)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ S81), Y84 (≠ R109), G115 (= G139), S116 (≠ T140), Y142 (≠ F166), H143 (= H167), D222 (≠ T239), D250 (= D266), V252 (≠ I268), N253 (≠ P269), K280 (= K295), F308 (≠ Y324), T309 (= T325), R408 (≠ T424)
O58478 Alanine/serine racemase; ASR; Ala/Ser racemase; EC 5.1.1.-; EC 5.1.1.1 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
31% identity, 89% coverage: 38:447/463 of query aligns to 35:458/474 of O58478
- D251 (≠ T239) mutation to A: Loss of activity.
- K308 (= K295) mutation to A: Loss of activity.
6io1B Crystal structure of a novel thermostable (s)-enantioselective omega- transaminase from thermomicrobium roseum (see paper)
32% identity, 85% coverage: 58:450/463 of query aligns to 34:446/448 of 6io1B
- active site: Y151 (≠ F166), D257 (= D266), K286 (= K295)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (= G138), G118 (= G139), A119 (≠ T140), N122 (= N143), Y151 (≠ F166), H152 (= H167), D257 (= D266), V259 (≠ I268), I260 (≠ P269), K286 (= K295)
Sites not aligning to the query:
1zobA Crystal structure of dialkylglycine decarboxylases bound with calcium ion
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1zobA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding calcium ion: L76 (≠ S106), S78 (≠ R108), V303 (≠ E327), S304 (≠ K328), D305 (≠ S329)
- binding pyridoxal-5'-phosphate: T108 (≠ G138), A110 (≠ T140), N113 (= N143), W136 (≠ F166), H137 (= H167), E208 (= E234), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295)
Sites not aligning to the query:
1zc9A The crystal structure of dialkylglycine decarboxylase complex with pyridoxamine 5-phosphate (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1zc9A
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G109 (= G139), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295)
Sites not aligning to the query:
1m0qA Structure of dialkylglycine decarboxylase complexed with s-1- aminoethanephosphonate (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1m0qA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding (1s)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]ethylphosphonic acid: Q50 (≠ N80), T108 (≠ G138), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), S213 (≠ T239), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
Sites not aligning to the query:
1m0pA Structure of dialkylglycine decarboxylase complexed with 1-amino-1- phenylethanephosphonate (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1m0pA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding (1r)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]-1-phenylethylphosphonic acid: Q50 (≠ N80), T108 (≠ G138), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), S213 (≠ T239), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
Sites not aligning to the query:
1m0oA Structure of dialkylglycine decarboxylase complexed with 1-amino-1- methylpropanephosphonate (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1m0oA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding (1r)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]-1-methylpropylphosphonic acid: Q50 (≠ N80), G109 (= G139), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
Sites not aligning to the query:
1m0nA Structure of dialkylglycine decarboxylase complexed with 1- aminocyclopentanephosphonate (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1m0nA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding 1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]cyclopentylphosphonic acid: Q50 (≠ N80), M51 (≠ S81), A110 (≠ T140), N113 (= N143), W136 (≠ F166), H137 (= H167), E208 (= E234), S213 (≠ T239), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
Sites not aligning to the query:
1d7vA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with nma (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1d7vA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding potassium ion: H75 (≠ F105), L76 (≠ S106), F77 (≠ P107), S78 (≠ R108), T301 (= T325), H302 (= H326), V303 (≠ E327), S304 (≠ K328), D305 (≠ S329)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-2-methylalanine: A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), S213 (≠ T239), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
Sites not aligning to the query:
1d7uA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with lcs (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1d7uA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding potassium ion: H75 (≠ F105), L76 (≠ S106), F77 (≠ P107), S78 (≠ R108), T301 (= T325), H302 (= H326), V303 (≠ E327), S304 (≠ K328), D305 (≠ S329)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G109 (= G139), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
Sites not aligning to the query:
1d7sA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with dcs (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1d7sA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: Q50 (≠ N80), G109 (= G139), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
- binding potassium ion: H75 (≠ F105), L76 (≠ S106), F77 (≠ P107), S78 (≠ R108), T301 (= T325), H302 (= H326), V303 (≠ E327), S304 (≠ K328), D305 (≠ S329)
Sites not aligning to the query:
1d7rA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with 5pa (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1d7rA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: G109 (= G139), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), S213 (≠ T239), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295), R404 (≠ T424)
- binding potassium ion: H75 (≠ F105), L76 (≠ S106), F77 (≠ P107), S78 (≠ R108), T301 (= T325), H302 (= H326), V303 (≠ E327), S304 (≠ K328), D305 (≠ S329)
Sites not aligning to the query:
1dgdA An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase (see paper)
32% identity, 85% coverage: 58:449/463 of query aligns to 27:429/431 of 1dgdA
- active site: W136 (≠ F166), E208 (= E234), D241 (= D266), Q244 (≠ P269), K270 (= K295), T301 (= T325), R404 (≠ T424)
- binding pyridoxal-5'-phosphate: T108 (≠ G138), G109 (= G139), A110 (≠ T140), W136 (≠ F166), H137 (= H167), E208 (= E234), D241 (= D266), A243 (≠ I268), Q244 (≠ P269), K270 (= K295)
Sites not aligning to the query:
O50131 Ornithine aminotransferase; Orn-AT; Ornithine delta-aminotransferase; EC 2.6.1.13 from Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (see paper)
33% identity, 86% coverage: 57:455/463 of query aligns to 39:450/454 of O50131
- T92 (≠ R108) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (≠ R109) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G139) binding pyridoxal 5'-phosphate
- T125 (= T140) binding pyridoxal 5'-phosphate
- Q267 (≠ P269) binding pyridoxal 5'-phosphate
- K293 (= K295) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T325) binding pyridoxal 5'-phosphate
7vo1A Structure of aminotransferase-substrate complex (see paper)
33% identity, 86% coverage: 57:455/463 of query aligns to 37:448/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ N80), S121 (≠ G138), G122 (= G139), T123 (= T140), F149 (= F166), H150 (= H167), R152 (≠ A169), E234 (≠ T239), D262 (= D266), V264 (≠ I268), Q265 (≠ P269), K291 (= K295), N318 (≠ Y324), T319 (= T325), R417 (≠ T424)
7vntA Structure of aminotransferase-substrate complex (see paper)
33% identity, 86% coverage: 57:455/463 of query aligns to 37:448/452 of 7vntA
- binding L-ornithine: F149 (= F166), R152 (≠ A169), E234 (≠ T239), K291 (= K295)
- binding pyridoxal-5'-phosphate: G122 (= G139), T123 (= T140), F149 (= F166), H150 (= H167), E229 (= E234), D262 (= D266), V264 (≠ I268), Q265 (≠ P269), K291 (= K295)
7vnoA Structure of aminotransferase (see paper)
33% identity, 86% coverage: 57:455/463 of query aligns to 37:448/452 of 7vnoA
Query Sequence
>WP_092350282.1 NCBI__GCF_900107645.1:WP_092350282.1
MSKVDKSAADRTEGDINQSVHRSSWQKKVLNEETCALLAEDEKYFIHQSLSTPCLTALER
SHGSYLFDTNGKSYLDFHGNSSHQVGYGHPHVVAAITEEMQRLPFSPRRFTNRPAVELAK
KLAQLSPGNLNRMLFAPGGTSANGIALKLARSVTGRFKTLSFWDAFHGASLDAISVGGEA
LFRRNMGPLLPGCIQVPAPGSHCFGVDKLDWQKALGYIEYVMVHEGDVAAFIAEPMRCTT
IDIPPVQFWRQIREICDRHGVLLIFDEIPLCLGRTGFMFACEYYAVVPDILCLGKGLGGG
IFPMAATLIREDLEIDPAQALGHYTHEKSPVGCAAALATLEVIADEHLLQRSRELGRHTL
AALHRLRSEHPLISAVRGVGLMLGIEITPPAGFTCSATDAAEQILYAAFTQGLSFKISAG
NVLTLTPPLTISDAEMDAALNIIAASIAQVEVKFGLNRQSRNI
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory