SitesBLAST
Comparing BPHYT_RS31765 FitnessBrowser__BFirm:BPHYT_RS31765 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)
4aoaA Biochemical properties and crystal structure of a novel beta-phenylalanine aminotransferase from variovorax paradoxus (see paper)
60% identity, 97% coverage: 13:440/443 of query aligns to 1:427/430 of 4aoaA
- active site: N35 (= N47), Y155 (= Y167), E203 (= E215), D236 (= D248), M239 (= M251), K263 (= K275), V398 (≠ T411)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: R37 (= R49), V39 (= V51), S127 (= S139), G128 (= G140), T129 (= T141), Y155 (= Y167), H156 (= H168), E203 (= E215), D236 (= D248), V238 (= V250), K263 (= K275), S294 (≠ A307), G295 (= G308), T296 (= T309)
H8WR05 Beta-phenylalanine transaminase; Aromatic beta-amino acid aminotransferase; Beta-phenylalanine aminotransferase; VpAT; EC 2.6.1.- from Variovorax paradoxus (see paper)
59% identity, 98% coverage: 9:440/443 of query aligns to 1:431/434 of H8WR05
- R41 (= R49) mutation to A: Loss of catalytic activity.
4ao9A Biochemical properties and crystal structure of a novel beta-phenylalanine aminotransferase from variovorax paradoxus (see paper)
60% identity, 97% coverage: 13:440/443 of query aligns to 4:430/433 of 4ao9A
- active site: N38 (= N47), Y158 (= Y167), E206 (= E215), D239 (= D248), M242 (= M251), K266 (= K275), V401 (≠ T411)
- binding pyridoxal-5'-phosphate: S130 (= S139), G131 (= G140), T132 (= T141), Y158 (= Y167), H159 (= H168), G160 (= G169), D239 (= D248), V241 (= V250), K266 (= K275)
2ykvA Structural determinants of the beta-selectivity of a bacterial aminotransferase (see paper)
51% identity, 94% coverage: 25:439/443 of query aligns to 18:432/432 of 2ykvA
- active site: N40 (= N47), Y160 (= Y167), E208 (= E215), D241 (= D248), M244 (= M251), K268 (= K275), A404 (≠ T411)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: R42 (= R49), S132 (= S139), G133 (= G140), T134 (= T141), Y160 (= Y167), H161 (= H168), E208 (= E215), D241 (= D248), V243 (= V250), M244 (= M251), K268 (= K275), A300 (= A307), G301 (= G308), T302 (= T309)
2ykuA Structural determinants of the beta-selectivity of a bacterial aminotransferase (see paper)
51% identity, 94% coverage: 25:439/443 of query aligns to 18:432/433 of 2ykuA
- active site: N40 (= N47), Y160 (= Y167), E208 (= E215), D241 (= D248), M244 (= M251), K268 (= K275), A404 (≠ T411)
- binding pyridoxal-5'-phosphate: S132 (= S139), G133 (= G140), T134 (= T141), Y160 (= Y167), H161 (= H168), G162 (= G169), E208 (= E215), D241 (= D248), V243 (= V250), M244 (= M251), K268 (= K275)
4ao4A Structural determinants of the beta-selectivity of a bacterial aminotransferase (see paper)
51% identity, 94% coverage: 25:439/443 of query aligns to 17:431/432 of 4ao4A
- active site: N39 (= N47), Y159 (= Y167), E207 (= E215), D240 (= D248), M243 (= M251), K267 (= K275), A403 (≠ T411)
- binding (3r)-3-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]-5-methylhexanoic acid: R41 (= R49), I43 (≠ V51), Y76 (≠ F84), G132 (= G140), T133 (= T141), Y159 (= Y167), H160 (= H168), E207 (= E215), A212 (= A220), D240 (= D248), V242 (= V250), M243 (= M251), K267 (= K275), G300 (= G308), T301 (= T309)
2ykyA Structural determinants of the beta-selectivity of a bacterial aminotransferase (see paper)
51% identity, 94% coverage: 25:439/443 of query aligns to 17:431/431 of 2ykyA
- active site: N39 (= N47), Y159 (= Y167), E207 (= E215), D240 (= D248), M243 (= M251), K267 (= K275), A403 (≠ T411)
- binding pyridoxal-5'-phosphate: G132 (= G140), T133 (= T141), Y159 (= Y167), H160 (= H168), E207 (= E215), D240 (= D248), V242 (= V250), M243 (= M251), K267 (= K275), G300 (= G308), T301 (= T309)
- binding (3S)-3-amino-3-phenylpropanoic acid: R41 (= R49), I43 (≠ V51), Y76 (≠ F84), Y159 (= Y167), P208 (= P216), A212 (= A220), A218 (≠ G226), R220 (≠ P228), L256 (= L264), K267 (= K275), G300 (= G308), T301 (= T309), L355 (= L363), R399 (= R407)
2ykxA Structural determinants of the beta-selectivity of a bacterial aminotransferase (see paper)
51% identity, 94% coverage: 25:439/443 of query aligns to 17:431/431 of 2ykxA
- active site: N39 (= N47), Y159 (= Y167), E207 (= E215), D240 (= D248), M243 (= M251), K267 (= K275), A403 (≠ T411)
- binding 2-oxoglutaric acid: R41 (= R49), I43 (≠ V51), Y76 (≠ F84), Y159 (= Y167), A299 (= A307), G300 (= G308), T301 (= T309), R399 (= R407)
- binding pyridoxal-5'-phosphate: S131 (= S139), G132 (= G140), T133 (= T141), Y159 (= Y167), H160 (= H168), G161 (= G169), E207 (= E215), D240 (= D248), V242 (= V250), M243 (= M251), K267 (= K275), G300 (= G308), T301 (= T309)
6k8hB Crystal structure of an omega-transaminase from sphaerobacter thermophilus (see paper)
36% identity, 94% coverage: 24:438/443 of query aligns to 2:440/441 of 6k8hB
- active site: N27 (= N47), Y147 (= Y167), D215 (≠ E215), D248 (= D248), I251 (≠ M251), K275 (= K275), C413 (≠ T411)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: G120 (= G140), T121 (= T141), Y147 (= Y167), H148 (= H168), D248 (= D248), V250 (= V250), I251 (≠ M251), K275 (= K275)
P23893 Glutamate-1-semialdehyde 2,1-aminomutase; GSA; Glutamate-1-semialdehyde aminotransferase; GSA-AT; EC 5.4.3.8 from Escherichia coli (strain K12) (see paper)
37% identity, 89% coverage: 36:429/443 of query aligns to 8:420/426 of P23893
- K265 (= K275) mutation to R: 2% of wild-type activity.
6ssgA Transaminase with dcs bound (see paper)
35% identity, 89% coverage: 32:427/443 of query aligns to 7:410/424 of 6ssgA
- binding [4-[(~{Z})-[(2~{R},5~{R})-5-(azanyloxymethyl)-3,6-bis(oxidanylidene)piperazin-2-yl]methoxyiminomethyl]-6-methyl-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate: S59 (≠ F84), G115 (= G140), T116 (= T141), Y142 (= Y167), H143 (= H168), W207 (≠ G219), D236 (= D248), V238 (= V250), K263 (= K275), S296 (≠ A307), G297 (= G308), S298 (≠ T309)
6ssfA Transaminase with lcs bound (see paper)
35% identity, 89% coverage: 32:427/443 of query aligns to 7:410/424 of 6ssfA
- binding [4-[(~{Z})-[(2~{S},5~{S})-5-(azanyloxymethyl)-3,6-bis(oxidanylidene)piperazin-2-yl]methoxyiminomethyl]-6-methyl-5-oxidanyl-pyridin-3-yl]methyl dihydrogen phosphate: G115 (= G140), T116 (= T141), Y142 (= Y167), H143 (= H168), W207 (≠ G219), R208 (≠ A220), D236 (= D248), V238 (= V250), K263 (= K275), G297 (= G308), S298 (≠ T309)
6sseA Transaminase with pmp bound (see paper)
35% identity, 89% coverage: 32:427/443 of query aligns to 7:410/424 of 6sseA
6ssdA Transaminase with plp bound (see paper)
35% identity, 89% coverage: 32:427/443 of query aligns to 7:410/424 of 6ssdA
3k28A Crystal structure of a glutamate-1-semialdehyde aminotransferase from bacillus anthracis with bound pyridoxal 5'phosphate
37% identity, 88% coverage: 32:420/443 of query aligns to 7:405/423 of 3k28A
- active site: V22 (≠ N47), Y145 (= Y167), E202 (= E215), D235 (= D248), M238 (= M251), K263 (= K275), G396 (≠ T411)
- binding calcium ion: I103 (≠ C125), V106 (≠ F128), P107 (= P129), I109 (≠ V131)
- binding pyridoxal-5'-phosphate: G118 (= G140), T119 (= T141), Y145 (= Y167), H146 (= H168), G147 (= G169), E202 (= E215), D235 (= D248), V237 (= V250), M238 (= M251), K263 (= K275)
Q42522 Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic; GSA 2; Glutamate-1-semialdehyde aminotransferase 2; GSA-AT 2; EC 5.4.3.8 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
36% identity, 91% coverage: 32:434/443 of query aligns to 51:471/472 of Q42522
- R92 (≠ W70) mutation to K: In gsa2-1; suppression of enf1 mutant pleiotropic developmental phenotypes; when associated with S-162.
- G162 (= G140) mutation to S: In gsa2-1; suppression of enf1 mutant pleiotropic developmental phenotypes; when associated with K-92.
3bs8A Crystal structure of glutamate 1-semialdehyde aminotransferase complexed with pyridoxamine-5'-phosphate from bacillus subtilis (see paper)
34% identity, 93% coverage: 26:436/443 of query aligns to 1:429/430 of 3bs8A
- active site: V22 (≠ N47), Y145 (= Y167), E207 (= E215), D240 (= D248), M243 (= M251), K268 (= K275), G401 (vs. gap)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G118 (= G140), T119 (= T141), Y145 (= Y167), H146 (= H168), E207 (= E215), N212 (≠ A220), D240 (= D248), V242 (= V250), K268 (= K275)
3usfA Crystal structure of dava-4
36% identity, 89% coverage: 36:430/443 of query aligns to 10:422/427 of 3usfA
- active site: V21 (≠ N47), Y144 (= Y167), D239 (= D248), M242 (= M251), K267 (= K275), A401 (≠ T411)
- binding (4s)-4,5-diaminopentanoic acid: S23 (≠ R49), V25 (= V51), S157 (= S176), K267 (= K275), E400 (≠ L410)
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: G117 (= G140), T118 (= T141), Y144 (= Y167), N211 (≠ A220), D239 (= D248), V241 (= V250), K267 (= K275)
3fq7A Gabaculine complex of gsam (see paper)
36% identity, 89% coverage: 36:430/443 of query aligns to 10:422/427 of 3fq7A
- active site: V21 (≠ N47), Y144 (= Y167), D239 (= D248), M242 (= M251), K267 (= K275), A401 (≠ T411)
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: S23 (≠ R49), V25 (= V51), W61 (≠ F84), G117 (= G140), T118 (= T141), Y144 (= Y167), H145 (= H168), E206 (= E215), N211 (≠ A220), D239 (= D248), V241 (= V250), M242 (= M251), K267 (= K275), G298 (= G308), T299 (= T309), E400 (≠ L410)
2hp2A Inter-subunit signaling in gsam (see paper)
36% identity, 89% coverage: 36:430/443 of query aligns to 10:422/427 of 2hp2A
- active site: V21 (≠ N47), Y144 (= Y167), D239 (= D248), M242 (= M251), K267 (= K275), A401 (≠ T411)
- binding (4s)-4,5-diaminopentanoic acid: G298 (= G308), T299 (= T309)
- binding (4r)-5-amino-4-[({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)amino]pentanoic acid: S23 (≠ R49), G117 (= G140), T118 (= T141), Y144 (= Y167), H145 (= H168), E206 (= E215), N211 (≠ A220), D239 (= D248), V241 (= V250), M242 (= M251), K267 (= K275)
- binding pyridoxal-5'-phosphate: G298 (= G308), T299 (= T309)
Query Sequence
>BPHYT_RS31765 FitnessBrowser__BFirm:BPHYT_RS31765
MLNSSTQSLSATALTDALMHSTQGYVRANPASAAQFIKATEAMPGGNTRSVLYYAPFPLT
IVKGKEARLWDADGHEYRDFIAEFSAGIYGHSNPVIRSAIDAALDGGINLSGHNLIEAEL
AAAVCERFPTVERVRFTNSGTEANLLVLAVAKVFTKRQKIVVFKGGYHGGVLSFGSGPNP
VNVPHDFLFANYNDLSSVERLFEQHGRDIAAVLVEPMQGASGCIVGQPDFLRGVRELCTR
FGALLAFDEVMTSRLAPGGMQEKLGIHADLTSLGKYIGGGMSFGAFGGRQEIMAQFDPRA
EGALAHAGTFNNNVMTMAAGVTGLRELYTPQAAIRLNARGDQLRDTLNEVFAAAGVAMRF
IGLGSLMNLQSTDQNIRSVDDLAGLEHRLKDLYFFHLVEAGVYLARRGYLTLSLPLSEED
ISHFVRATRSFVERYRALLPTSR
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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