SitesBLAST
Comparing BPHYT_RS10155 FitnessBrowser__BFirm:BPHYT_RS10155 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)
1d7vA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with nma (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1d7vA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding potassium ion: H75 (= H77), L76 (= L78), F77 (= F79), S78 (= S80), T301 (= T303), H302 (= H304), V303 (= V305), S304 (= S306), D305 (= D307)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-2-methylalanine: A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), S213 (= S215), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272), R404 (= R406)
1d7uA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with lcs (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1d7uA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding potassium ion: H75 (= H77), L76 (= L78), F77 (= F79), S78 (= S80), T301 (= T303), H302 (= H304), V303 (= V305), S304 (= S306), D305 (= D307)
- binding [5-hydroxy-6-methyl-4-({[(4E)-3-oxo-1,2-oxazolidin-4-ylidene]amino}methyl)pyridin-3-yl]methyl dihydrogen phosphate: G109 (= G111), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272), R404 (= R406)
1d7sA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with dcs (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1d7sA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding d-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-n,o-cycloserylamide: Q50 (= Q52), G109 (= G111), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272), R404 (= R406)
- binding potassium ion: H75 (= H77), L76 (= L78), F77 (= F79), S78 (= S80), T301 (= T303), H302 (= H304), V303 (= V305), S304 (= S306), D305 (= D307)
1d7rA Crystal structure of the complex of 2,2-dialkylglycine decarboxylase with 5pa (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1d7rA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding n-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-y-lmethyl]-1-amino-cyclopropanecarboxylic acid: G109 (= G111), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), S213 (= S215), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272), R404 (= R406)
- binding potassium ion: H75 (= H77), L76 (= L78), F77 (= F79), S78 (= S80), T301 (= T303), H302 (= H304), V303 (= V305), S304 (= S306), D305 (= D307)
1dgdA An alkali metal ion size-dependent switch in the active site structure of dialkylglycine decarboxylase (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1dgdA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding pyridoxal-5'-phosphate: T108 (= T110), G109 (= G111), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272)
1zobA Crystal structure of dialkylglycine decarboxylases bound with calcium ion
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1zobA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding calcium ion: L76 (= L78), S78 (= S80), V303 (= V305), S304 (= S306), D305 (= D307)
- binding pyridoxal-5'-phosphate: T108 (= T110), A110 (= A112), N113 (= N115), W136 (= W138), H137 (= H139), E208 (= E210), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272)
1zc9A The crystal structure of dialkylglycine decarboxylase complex with pyridoxamine 5-phosphate (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1zc9A
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G109 (= G111), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272)
1m0qA Structure of dialkylglycine decarboxylase complexed with s-1- aminoethanephosphonate (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1m0qA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding (1s)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]ethylphosphonic acid: Q50 (= Q52), T108 (= T110), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), S213 (= S215), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272), R404 (= R406)
1m0pA Structure of dialkylglycine decarboxylase complexed with 1-amino-1- phenylethanephosphonate (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1m0pA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding (1r)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]-1-phenylethylphosphonic acid: Q50 (= Q52), T108 (= T110), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), S213 (= S215), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272), R404 (= R406)
1m0oA Structure of dialkylglycine decarboxylase complexed with 1-amino-1- methylpropanephosphonate (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1m0oA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding (1r)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]-1-methylpropylphosphonic acid: Q50 (= Q52), G109 (= G111), A110 (= A112), W136 (= W138), H137 (= H139), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), R404 (= R406)
1m0nA Structure of dialkylglycine decarboxylase complexed with 1- aminocyclopentanephosphonate (see paper)
93% identity, 99% coverage: 4:433/433 of query aligns to 2:431/431 of 1m0nA
- active site: G19 (= G21), W136 (= W138), E208 (= E210), D241 (= D243), Q244 (= Q246), K270 (= K272), T301 (= T303), R404 (= R406)
- binding 1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]cyclopentylphosphonic acid: Q50 (= Q52), M51 (= M53), A110 (= A112), N113 (= N115), W136 (= W138), H137 (= H139), E208 (= E210), S213 (= S215), D241 (= D243), A243 (= A245), Q244 (= Q246), K270 (= K272), R404 (= R406)
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
31% identity, 99% coverage: 4:432/433 of query aligns to 1:423/425 of 1szkA
- active site: V18 (≠ G21), Y137 (≠ W138), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T303), R397 (= R406)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G111), S111 (≠ A112), Y137 (≠ W138), H138 (= H139), E205 (= E210), D238 (= D243), V240 (≠ A245), Q241 (= Q246), K267 (= K272)
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
31% identity, 99% coverage: 4:432/433 of query aligns to 1:423/425 of 1sffA
- active site: V18 (≠ G21), Y137 (≠ W138), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T303), R397 (= R406)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ S80), G110 (= G111), S111 (≠ A112), Y137 (≠ W138), H138 (= H139), R140 (≠ M141), E205 (= E210), D238 (= D243), V240 (≠ A245), Q241 (= Q246), K267 (= K272), T296 (= T303)
- binding sulfate ion: N152 (vs. gap), Y393 (≠ G402)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
31% identity, 99% coverage: 4:432/433 of query aligns to 1:423/425 of 1sf2A
- active site: V18 (≠ G21), Y137 (≠ W138), E205 (= E210), D238 (= D243), Q241 (= Q246), K267 (= K272), T296 (= T303), R397 (= R406)
- binding pyridoxal-5'-phosphate: G110 (= G111), S111 (≠ A112), Y137 (≠ W138), H138 (= H139), E205 (= E210), D238 (= D243), V240 (≠ A245), Q241 (= Q246), K267 (= K272)
- binding sulfate ion: N152 (vs. gap), Y393 (≠ G402)
P22256 4-aminobutyrate aminotransferase GabT; 5-aminovalerate transaminase; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; L-AIBAT; EC 2.6.1.19; EC 2.6.1.48 from Escherichia coli (strain K12) (see 2 papers)
31% identity, 99% coverage: 4:432/433 of query aligns to 2:424/426 of P22256
- I50 (≠ Q52) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GA 111:112) binding
- E211 (≠ S215) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (≠ A245) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q246) binding
- K268 (= K272) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T303) binding
5wyaA Structure of amino acid racemase, 2.65 a (see paper)
30% identity, 94% coverage: 23:429/433 of query aligns to 23:429/439 of 5wyaA
- active site: Y140 (≠ W138), E215 (= E210), D248 (= D243), N251 (≠ Q246), K278 (= K272), T307 (≠ Y301), R406 (= R406)
- binding (2S,3S)-3-methyl-2-[[2-methyl-3-oxidanyl-5-(phosphonooxymethyl)pyridin-4-yl]methylamino]pentanoic acid: A52 (≠ Q52), Y82 (≠ M82), S112 (≠ T110), G113 (= G111), S114 (≠ A112), Y140 (≠ W138), H141 (= H139), E215 (= E210), D248 (= D243), V250 (≠ A245), N251 (≠ Q246), K278 (= K272), F306 (= F300), T307 (≠ Y301), R406 (= R406)
Sites not aligning to the query:
5wyfA Structure of amino acid racemase, 2.12 a (see paper)
30% identity, 94% coverage: 23:429/433 of query aligns to 25:431/446 of 5wyfA
- active site: Y142 (≠ W138), E217 (= E210), D250 (= D243), N253 (≠ Q246), K280 (= K272), T309 (≠ Y301), R408 (= R406)
- binding n-[o-phosphono-pyridoxyl]-isoleucine: A54 (≠ Q52), Y84 (≠ M82), G115 (= G111), S116 (≠ A112), Y142 (≠ W138), H143 (= H139), D222 (≠ S215), D250 (= D243), V252 (≠ A245), N253 (≠ Q246), K280 (= K272), F308 (= F300), T309 (≠ Y301), R408 (= R406)
Sites not aligning to the query:
4ysnC Structure of aminoacid racemase in complex with plp (see paper)
30% identity, 94% coverage: 23:429/433 of query aligns to 32:438/448 of 4ysnC
- active site: Y149 (≠ W138), E224 (= E210), D257 (= D243), N260 (≠ Q246), K287 (= K272), T316 (≠ Y301), R415 (= R406)
- binding pyridoxal-5'-phosphate: S121 (≠ T110), G122 (= G111), S123 (≠ A112), Y149 (≠ W138), H150 (= H139), E224 (= E210), D257 (= D243), V259 (≠ A245), K287 (= K272), F315 (= F300), T316 (≠ Y301)
Sites not aligning to the query:
6io1B Crystal structure of a novel thermostable (s)-enantioselective omega- transaminase from thermomicrobium roseum (see paper)
36% identity, 94% coverage: 26:433/433 of query aligns to 31:447/448 of 6io1B
- active site: Y151 (≠ W138), D257 (= D243), K286 (= K272)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G117 (≠ T110), G118 (= G111), A119 (= A112), N122 (= N115), Y151 (≠ W138), H152 (= H139), D257 (= D243), V259 (≠ A245), I260 (≠ Q246), K286 (= K272)
Sites not aligning to the query:
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, 94% coverage: 26:433/433 of query aligns to 53:462/474 of O58478
- D251 (≠ S215) mutation to A: Loss of activity.
- K308 (= K272) mutation to A: Loss of activity.
Query Sequence
>BPHYT_RS10155 FitnessBrowser__BFirm:BPHYT_RS10155
MSRNNDAVFWRNAKQHLIRYGGTFEPMIIERAQGSFVYDADGRAILDFTSGQMSAVLGHS
HPEIVSVINEYAGKLDHLFSGMLSRPVVDLATRLAEITPDGLDRALLLSTGAESNEAAIR
MAKLVTGKYEIVGFAQSWHGMTAAAASATYSAGRKGVGPAAVGSFAIPAPFLYRPRFERH
GDYDYLAELDYAFDLIDRQSSGNLAAFIAEPILSSGGIIELPEGYMTALKRKCEERGMLL
ILDEAQTGVGRTGTMFACQRDGVTPDILTLSKTLGAGLPLAAVVTSAQIEERAHELGYLF
YTTHVSDPLPAAVGLRVLEVVERDGLVARANLMGARLKRGLLDLMERFDCIGDIRGRGLL
LGMEIVKDRRTKEPADGLGAKITRECMNLGLSMNIVQLPGMGGVFRIAPPLTVHEDEIDL
GLDLLGQAIERSL
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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