SitesBLAST
Comparing BPHYT_RS02160 FitnessBrowser__BFirm:BPHYT_RS02160 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)
2g6wA Suicide inhibition of a-oxamine synthase: structures of the covalent adducts of 8-amino-7-oxonanoate synthase with trifluoroalanine (see paper)
45% identity, 89% coverage: 34:382/394 of query aligns to 33:375/383 of 2g6wA
- active site: N46 (= N47), H132 (= H137), E174 (≠ D179), S178 (= S183), D203 (= D208), H206 (= H211), K235 (= K242)
- binding (4-{(e)-[(2,2-difluoroethyl)imino]methyl}-5-hydroxy-6-methylpyridin-3-yl)methyl dihydrogen phosphate: N46 (= N47), G107 (= G112), H132 (= H137), E174 (≠ D179), S178 (= S183), D203 (= D208), A205 (= A210), H206 (= H211), K235 (= K242)
P12998 8-amino-7-oxononanoate synthase; AONS; 7-keto-8-amino-pelargonic acid synthase; 7-KAP synthase; KAPA synthase; 8-amino-7-ketopelargonate synthase; EC 2.3.1.47 from Escherichia coli (strain K12) (see 2 papers)
45% identity, 89% coverage: 34:382/394 of query aligns to 34:376/384 of P12998
- GF 108:109 (≠ GY 112:113) binding
- H133 (= H137) binding
- S179 (= S183) binding
- H207 (= H211) binding
- T233 (= T239) binding
- K236 (= K242) modified: N6-(pyridoxal phosphate)lysine
- T352 (= T358) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 21 binding
1djeA Crystal structure of the plp-bound form of 8-amino-7-oxonanoate synthase (see paper)
44% identity, 94% coverage: 14:382/394 of query aligns to 10:375/383 of 1djeA
- active site: N46 (= N47), H132 (= H137), E174 (≠ D179), S178 (= S183), D203 (= D208), H206 (= H211), K235 (= K242)
- binding pyridoxal-5'-phosphate: G107 (= G112), F108 (≠ Y113), H132 (= H137), E174 (≠ D179), S178 (= S183), D203 (= D208), A205 (= A210), H206 (= H211), T232 (= T239), K235 (= K242)
1dj9A Crystal structure of 8-amino-7-oxonanoate synthase (or 7-keto- 8aminipelargonate or kapa synthase) complexed with plp and the product 8(s)-amino-7-oxonanonoate (or kapa). The enzyme of biotin biosynthetic pathway. (see paper)
44% identity, 94% coverage: 14:382/394 of query aligns to 10:375/383 of 1dj9A
- active site: N46 (= N47), H132 (= H137), E174 (≠ D179), S178 (= S183), D203 (= D208), H206 (= H211), K235 (= K242)
- binding n-[7-keto-8-aminopelargonic acid]-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane]: R20 (= R20), G107 (= G112), F108 (≠ Y113), H132 (= H137), E174 (≠ D179), D203 (= D208), A205 (= A210), H206 (= H211), T232 (= T239), K235 (= K242), I347 (= I354), T351 (= T358)
7poaA An irreversible, promiscuous and highly thermostable claisen- condensation biocatalyst drives the synthesis of substituted pyrroles
35% identity, 97% coverage: 9:392/394 of query aligns to 14:393/398 of 7poaA
- binding pyridoxal-5'-phosphate: G113 (= G112), F114 (≠ Y113), H138 (= H137), S140 (= S139), D210 (= D208), A212 (= A210), H213 (= H211), T242 (= T239), K245 (= K242), S274 (≠ T271), T275 (= T272)
3tqxA Structure of the 2-amino-3-ketobutyrate coenzyme a ligase (kbl) from coxiella burnetii (see paper)
34% identity, 99% coverage: 4:392/394 of query aligns to 8:392/396 of 3tqxA
- active site: N48 (= N47), H134 (= H137), D179 (= D179), S183 (= S183), D208 (= D208), H211 (= H211), K242 (= K242)
- binding pyridoxal-5'-phosphate: S108 (≠ T111), C109 (≠ G112), F110 (≠ Y113), H134 (= H137), D208 (= D208), S210 (≠ A210), H211 (= H211), T239 (= T239), K242 (= K242), F271 (= F270), S272 (≠ T271), N273 (≠ T272)
P0AB77 2-amino-3-ketobutyrate coenzyme A ligase; AKB ligase; Glycine acetyltransferase; EC 2.3.1.29 from Escherichia coli (strain K12) (see paper)
35% identity, 99% coverage: 2:392/394 of query aligns to 4:393/398 of P0AB77
- H136 (= H137) binding
- S185 (= S183) binding in other chain
- R368 (= R367) binding
1fc4A 2-amino-3-ketobutyrate coa ligase (see paper)
35% identity, 99% coverage: 2:392/394 of query aligns to 7:396/401 of 1fc4A
- active site: N53 (= N47), H139 (= H137), D184 (= D179), S188 (= S183), D213 (= D208), H216 (= H211), K247 (= K242)
- binding 2-amino-3-ketobutyric acid: N53 (= N47), H139 (= H137), S188 (= S183), H216 (= H211), K247 (= K242), R371 (= R367)
- binding pyridoxal-5'-phosphate: S113 (≠ T111), C114 (≠ G112), F115 (≠ Y113), H139 (= H137), S188 (= S183), D213 (= D208), S215 (≠ A210), H216 (= H211), T244 (= T239), K247 (= K242), F276 (= F270), S277 (≠ T271), N278 (≠ T272)
Q8GW43 8-amino-7-oxononanoate synthase; AONS; 7-keto-8-amino-pelargonic acid synthase; 7-KAP synthase; KAPA synthase; 8-amino-7-ketopelargonate synthase; Biotin synthase 4; Biotin synthase F; AtbioF; EC 2.3.1.47 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
35% identity, 87% coverage: 39:382/394 of query aligns to 102:451/476 of Q8GW43
Sites not aligning to the query:
- 474:476 Peroxisomal targeting signal PTS1; mutation Missing: Incorrect cytosolic localization and loss of biotin synthase activity.
P22557 5-aminolevulinate synthase, erythroid-specific, mitochondrial; ALAS-E; 5-aminolevulinic acid synthase 2; Delta-ALA synthase 2; Delta-aminolevulinate synthase 2; EC 2.3.1.37 from Homo sapiens (Human) (see 11 papers)
36% identity, 94% coverage: 5:375/394 of query aligns to 151:525/587 of P22557
- K156 (≠ G10) to E: in SIDBA1; significantly reduced activity
- R170 (= R24) to H: in SIDBA1; significantly increased thermosensitivity
- R204 (≠ A54) to Q: in SIDBA1; 15% to 35% activity of wild-type; dbSNP:rs1338391423
- R218 (= R68) to H: in SIDBA1; significantly increased thermosensitivity; dbSNP:rs185504937
- E242 (≠ D92) to K: in SIDBA1; significantly reduced activity
- C258 (≠ G112) binding in other chain
- F259 (≠ Y113) binding in other chain
- D263 (≠ L117) to N: in SIDBA1; significantly reduced activity
- P339 (= P190) to L: in SIDBA1; significantly reduced activity
- H360 (= H211) binding in other chain
- R375 (≠ Q226) to C: in SIDBA1; significantly reduced activity
- T388 (= T239) binding in other chain
- K391 (= K242) modified: N6-(pyridoxal phosphate)lysine
- R411 (≠ V262) to C: in SIDBA1; 12% to 25% activity of wild-type; dbSNP:rs137852305; to H: in SIDBA1; significantly reduced activity
- T420 (= T271) binding
- T421 (= T272) binding
- R452 (≠ Q303) to G: in SIDBA1; does not affect activity
- R511 (≠ T361) mutation to E: 2-fold increased enzyme activity with a lower specificity for glycine and higher for succinyl-CoA.
- P520 (≠ L370) to L: in SIDBA1; likely benign; associated in cis with H-560 in a patient; dbSNP:rs201062903
Sites not aligning to the query:
- 1:49 modified: transit peptide, Mitochondrion
- 560 R → H: in SIDBA1; associated in cis with L-520 in a patient; dbSNP:rs892041887
- 572 R → H: in SIDBA1; does not affect activity
- 586 Y → F: rare variant found in a congenital erythropoietic porphyria patient that also carries UROS mutations R-73 and Q-248; increased enzyme activity; dbSNP:rs139596860
6hrhA Structure of human erythroid-specific 5'-aminolevulinate synthase, alas2
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 6hrhA
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), H218 (= H211), T246 (= T239), K249 (= K242), T278 (= T271), T279 (= T272)
5qreA Pandda analysis group deposition -- crystal structure of human alas2a in complex with z117233350
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qreA
- binding pyridoxal-5'-phosphate: C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), T246 (= T239), K249 (= K242), T278 (= T271), T279 (= T272)
Sites not aligning to the query:
5qrcA Pandda analysis group deposition -- crystal structure of human alas2a in complex with z31721798
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qrcA
- binding 3-cyclohexyl-1-(morpholin-4-yl)propan-1-one: K129 (≠ G125), I130 (vs. gap), Y271 (≠ R264)
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), K249 (= K242), T278 (= T271), T279 (= T272)
5qraA Pandda analysis group deposition -- crystal structure of human alas2a in complex with z1101755952
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qraA
- binding [(4R)-4-methyl-2,3,4,5-tetrahydro-1H-azepin-1-yl](1,3-thiazol-4-yl)methanone: K129 (≠ G125), I130 (vs. gap), Y271 (≠ R264)
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), T246 (= T239), K249 (= K242), T278 (= T271), T279 (= T272)
5qr9A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z31478129
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qr9A
- binding ethyl benzylcarbamate: H206 (≠ E199), L211 (≠ W204), D241 (≠ L234)
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), K249 (= K242), T278 (= T271), T279 (= T272)
5qr3A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z915492990
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qr3A
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), K249 (= K242), T278 (= T271), T279 (= T272)
Sites not aligning to the query:
5qr1A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z396380540
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qr1A
- binding ~{N}-(cyclobutylmethyl)-1,5-dimethyl-pyrazole-4-carboxamide: I130 (vs. gap), Y271 (≠ R264)
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), T246 (= T239), K249 (= K242), T278 (= T271), T279 (= T272)
5qr0A Pandda analysis group deposition -- crystal structure of human alas2a in complex with z730649594
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qr0A
- binding N-[2-(4-hydroxyphenyl)ethyl]pyridine-2-carboxamide: H206 (≠ E199), L211 (≠ W204), D241 (≠ L234), T261 (≠ H254), L264 (≠ V257), E300 (= E293), A303 (= A296), A307 (= A299), P380 (≠ A372), H381 (≠ A373)
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), K249 (= K242), T278 (= T271), T279 (= T272)
5qqyA Pandda analysis group deposition -- crystal structure of human alas2a in complex with z2856434899
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qqyA
- binding 1-[(2,5-dihydrothiophen-3-yl)methyl]piperidin-4-ol: K16 (≠ T6), E19 (= E9), K129 (≠ G125), Y271 (≠ R264)
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), T246 (= T239), K249 (= K242), T278 (= T271), T279 (= T272)
Sites not aligning to the query:
5qqxA Pandda analysis group deposition -- crystal structure of human alas2a in complex with z373768900
36% identity, 94% coverage: 5:375/394 of query aligns to 15:383/429 of 5qqxA
- binding pyridoxal-5'-phosphate: S115 (≠ T111), C116 (≠ G112), F117 (≠ Y113), H143 (= H137), E186 (≠ D179), S190 (= S183), D215 (= D208), V217 (≠ A210), H218 (= H211), K249 (= K242), T278 (= T271), T279 (= T272)
Sites not aligning to the query:
Query Sequence
>BPHYT_RS02160 FitnessBrowser__BFirm:BPHYT_RS02160
MHLLDTLTEGLKEIDARGLRRRRRTADTPCAAHMTVDGRAIIGFASNDYLGLAAHPQLIA
AIAEGAQRYGAGSGGSHLLGGHSRAHAQLEDDLAEFAGGFVDNARALYFSTGYMANLATL
TALAGRGTTLFSDALNHASLIDGARLSRADVQIYPHCDTEALSAMLEASDADVKVIVSDT
VFSMDGDIAPLPRLLELAEQHGAWLIVDDAHGFGVLGPQGRGAIAQAALRSPNLISIGTL
GKAAGVSGAFVTAHETVIEWLVQRARPYIFTTASVPAAAHAVSASLRIIGGEEGDARRAH
LQQLIERTRAMLKATPWLPVDSHTAVQPLIIGANDATLDIAATLDRAGLWVPAIRPPTVP
TGTSRLRISLSAAHSQADLDRLEAGLQQLGAKAA
Or try a new SitesBLAST search
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