SitesBLAST
Comparing SMa2400 FitnessBrowser__Smeli:SMa2400 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)
6rl5G The first crystal structure of the daba aminotransferase ectb in the ectoine biosynthesis pathway of the model organism chromohalobacter salexigens dsm 3034 (see paper)
38% identity, 89% coverage: 36:451/470 of query aligns to 6:404/422 of 6rl5G
- active site: S16 (≠ P46), F137 (≠ Y167), D237 (= D275), K266 (= K304)
- binding pyridoxal-5'-phosphate: G110 (= G140), T111 (= T141), F137 (≠ Y167), H138 (= H168), D237 (= D275), I239 (≠ V277), Q240 (= Q278), K266 (= K304), G294 (= G331), T295 (= T332)
1wkhA Acetylornithine aminotransferase from thermus thermophilus hb8
38% identity, 86% coverage: 57:462/470 of query aligns to 27:386/387 of 1wkhA
- active site: F132 (≠ Y167), E184 (= E242), D217 (= D275), Q220 (= Q278), K246 (= K304), T275 (= T332), R363 (= R439)
- binding 4-[(1,3-dicarboxy-propylamino)-methyl]-3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridinium: Y46 (≠ A76), S104 (= S139), G105 (= G140), T106 (= T141), F132 (≠ Y167), S133 (≠ H168), E184 (= E242), E189 (= E247), D217 (= D275), I219 (≠ V277), K246 (= K304), R363 (= R439)
Sites not aligning to the query:
1wkgA Acetylornithine aminotransferase from thermus thermophilus hb8
38% identity, 86% coverage: 57:462/470 of query aligns to 27:386/387 of 1wkgA
- active site: F132 (≠ Y167), E184 (= E242), D217 (= D275), Q220 (= Q278), K246 (= K304), T275 (= T332), R363 (= R439)
- binding n~2~-acetyl-n~5~-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-l-ornithine: Y46 (≠ A76), G105 (= G140), T106 (= T141), F132 (≠ Y167), S133 (≠ H168), R135 (≠ M170), E184 (= E242), D217 (= D275), I219 (≠ V277), Q220 (= Q278), K246 (= K304), G273 (≠ A330), T274 (≠ G331), T275 (= T332)
Sites not aligning to the query:
1vefA Acetylornithine aminotransferase from thermus thermophilus hb8
38% identity, 86% coverage: 57:462/470 of query aligns to 27:386/387 of 1vefA
- active site: F132 (≠ Y167), D217 (= D275), K246 (= K304), T275 (= T332), R363 (= R439)
- binding pyridoxal-5'-phosphate: G105 (= G140), T106 (= T141), F132 (≠ Y167), S133 (≠ H168), E184 (= E242), D217 (= D275), I219 (≠ V277), K246 (= K304)
Sites not aligning to the query:
1sffA Structure of gamma-aminobutyrate aminotransferase complex with aminooxyacetate (see paper)
33% identity, 91% coverage: 35:464/470 of query aligns to 8:422/425 of 1sffA
- active site: V18 (≠ Y45), Y137 (= Y167), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T332), R397 (= R439)
- binding 4'-deoxy-4'-acetylyamino-pyridoxal-5'-phosphate: Q78 (≠ D106), G110 (= G140), S111 (≠ T141), Y137 (= Y167), H138 (= H168), R140 (≠ M170), E205 (= E242), D238 (= D275), V240 (= V277), Q241 (= Q278), K267 (= K304), T296 (= T332)
- binding sulfate ion: N152 (≠ G182), Y393 (≠ G435)
1sf2A Structure of e. Coli gamma-aminobutyrate aminotransferase (see paper)
33% identity, 91% coverage: 35:464/470 of query aligns to 8:422/425 of 1sf2A
- active site: V18 (≠ Y45), Y137 (= Y167), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T332), R397 (= R439)
- binding pyridoxal-5'-phosphate: G110 (= G140), S111 (≠ T141), Y137 (= Y167), H138 (= H168), E205 (= E242), D238 (= D275), V240 (= V277), Q241 (= Q278), K267 (= K304)
- binding sulfate ion: N152 (≠ G182), Y393 (≠ G435)
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)
33% identity, 91% coverage: 35:464/470 of query aligns to 9:423/426 of P22256
- I50 (≠ A76) mutation to Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA.
- GS 111:112 (≠ GT 140:141) binding
- E211 (= E247) mutation to S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA.
- V241 (= V277) mutation to A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA.
- Q242 (= Q278) binding
- K268 (= K304) modified: N6-(pyridoxal phosphate)lysine
- T297 (= T332) binding
Q5SHH5 [LysW]-aminoadipate semialdehyde transaminase; EC 2.6.1.118 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
38% identity, 86% coverage: 57:462/470 of query aligns to 35:394/395 of Q5SHH5
- GT 113:114 (= GT 140:141) binding
- K254 (= K304) modified: N6-(pyridoxal phosphate)lysine
- T283 (= T332) binding
1szkA The structure of gamma-aminobutyrate aminotransferase mutant: e211s (see paper)
33% identity, 91% coverage: 35:464/470 of query aligns to 8:422/425 of 1szkA
- active site: V18 (≠ Y45), Y137 (= Y167), E205 (= E242), D238 (= D275), Q241 (= Q278), K267 (= K304), T296 (= T332), R397 (= R439)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G110 (= G140), S111 (≠ T141), Y137 (= Y167), H138 (= H168), E205 (= E242), D238 (= D275), V240 (= V277), Q241 (= Q278), K267 (= K304)
7vo1A Structure of aminotransferase-substrate complex (see paper)
33% identity, 93% coverage: 32:468/470 of query aligns to 17:450/452 of 7vo1A
- binding N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid: I61 (≠ A76), S121 (= S139), G122 (= G140), T123 (= T141), F149 (≠ Y167), H150 (= H168), R152 (≠ M170), E234 (= E247), D262 (= D275), V264 (= V277), Q265 (= Q278), K291 (= K304), N318 (≠ G331), T319 (= T332), R417 (= R439)
7vntA Structure of aminotransferase-substrate complex (see paper)
33% identity, 93% coverage: 32:468/470 of query aligns to 17:450/452 of 7vntA
- binding L-ornithine: F149 (≠ Y167), R152 (≠ M170), E234 (= E247), K291 (= K304)
- binding pyridoxal-5'-phosphate: G122 (= G140), T123 (= T141), F149 (≠ Y167), H150 (= H168), E229 (= E242), D262 (= D275), V264 (= V277), Q265 (= Q278), K291 (= K304)
7vnoA Structure of aminotransferase (see paper)
33% identity, 93% coverage: 32:468/470 of query aligns to 17:450/452 of 7vnoA
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, 93% coverage: 32:468/470 of query aligns to 19:452/454 of O50131
- T92 (≠ L105) mutation to V: Slightly increases the specific activity. Increases KM for L-ornithine.
- D93 (= D106) mutation to L: Reduces the specific activity. Increases KM for L-ornithine.
- G124 (= G140) binding
- T125 (= T141) binding
- Q267 (= Q278) binding
- K293 (= K304) modified: N6-(pyridoxal phosphate)lysine
- T321 (= T332) binding
A0QYS9 Acetylornithine aminotransferase; ACOAT; EC 2.6.1.11 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
35% identity, 92% coverage: 32:463/470 of query aligns to 1:384/390 of A0QYS9
- K304 (≠ R364) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P50457 4-aminobutyrate aminotransferase PuuE; GABA aminotransferase; GABA-AT; Gamma-amino-N-butyrate transaminase; GABA transaminase; Glutamate:succinic semialdehyde transaminase; EC 2.6.1.19 from Escherichia coli (strain K12) (see paper)
35% identity, 91% coverage: 26:452/470 of query aligns to 2:409/421 of P50457
- K267 (= K304) mutation to A: No GABA-AT activity.
1zobA Crystal structure of dialkylglycine decarboxylases bound with calcium ion
34% identity, 90% coverage: 41:464/470 of query aligns to 10:429/431 of 1zobA
- active site: G19 (vs. gap), W136 (≠ Y167), E208 (= E242), D241 (= D275), Q244 (= Q278), K270 (= K304), T301 (= T332), R404 (= R439)
- binding calcium ion: L76 (= L102), S78 (≠ T104), V303 (≠ R334), S304 (≠ G335), D305 (≠ N336)
- binding pyridoxal-5'-phosphate: T108 (≠ S139), A110 (≠ T141), N113 (≠ V144), W136 (≠ Y167), H137 (= H168), E208 (= E242), D241 (= D275), A243 (≠ V277), Q244 (= Q278), K270 (= K304)
1zc9A The crystal structure of dialkylglycine decarboxylase complex with pyridoxamine 5-phosphate (see paper)
34% identity, 90% coverage: 41:464/470 of query aligns to 10:429/431 of 1zc9A
- active site: G19 (vs. gap), W136 (≠ Y167), E208 (= E242), D241 (= D275), Q244 (= Q278), K270 (= K304), T301 (= T332), R404 (= R439)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: G109 (= G140), A110 (≠ T141), W136 (≠ Y167), H137 (= H168), E208 (= E242), D241 (= D275), A243 (≠ V277), Q244 (= Q278), K270 (= K304)
1m0qA Structure of dialkylglycine decarboxylase complexed with s-1- aminoethanephosphonate (see paper)
34% identity, 90% coverage: 41:464/470 of query aligns to 10:429/431 of 1m0qA
- active site: G19 (vs. gap), W136 (≠ Y167), E208 (= E242), D241 (= D275), Q244 (= Q278), K270 (= K304), T301 (= T332), R404 (= R439)
- binding (1s)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]ethylphosphonic acid: Q50 (≠ A76), T108 (≠ S139), A110 (≠ T141), W136 (≠ Y167), H137 (= H168), E208 (= E242), S213 (≠ E247), D241 (= D275), A243 (≠ V277), Q244 (= Q278), K270 (= K304), R404 (= R439)
1m0pA Structure of dialkylglycine decarboxylase complexed with 1-amino-1- phenylethanephosphonate (see paper)
34% identity, 90% coverage: 41:464/470 of query aligns to 10:429/431 of 1m0pA
- active site: G19 (vs. gap), W136 (≠ Y167), E208 (= E242), D241 (= D275), Q244 (= Q278), K270 (= K304), T301 (= T332), R404 (= R439)
- binding (1r)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]-1-phenylethylphosphonic acid: Q50 (≠ A76), T108 (≠ S139), A110 (≠ T141), W136 (≠ Y167), H137 (= H168), E208 (= E242), S213 (≠ E247), D241 (= D275), A243 (≠ V277), Q244 (= Q278), K270 (= K304), R404 (= R439)
1m0oA Structure of dialkylglycine decarboxylase complexed with 1-amino-1- methylpropanephosphonate (see paper)
34% identity, 90% coverage: 41:464/470 of query aligns to 10:429/431 of 1m0oA
- active site: G19 (vs. gap), W136 (≠ Y167), E208 (= E242), D241 (= D275), Q244 (= Q278), K270 (= K304), T301 (= T332), R404 (= R439)
- binding (1r)-1-[((1e)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylene)amino]-1-methylpropylphosphonic acid: Q50 (≠ A76), G109 (= G140), A110 (≠ T141), W136 (≠ Y167), H137 (= H168), E208 (= E242), D241 (= D275), Q244 (= Q278), K270 (= K304), R404 (= R439)
Query Sequence
>SMa2400 FitnessBrowser__Smeli:SMa2400
MPADLAARTSSKIFNGVDLMDASARADNAFYLDRQERRESNARSYPRRFPVALKSASGCI
VTDVDGRSYLDCLAGAGTLALGHNHPEVIETLQQVLGSGLPLHTLDLTTPVKDRFVSDIF
GTLPAGLRDEAKIQFCSPSGTDAVEAAIKLAKTATGRTDLVSFRGAYHGMSQGSLSLMGS
LGPKASVGQLVPGAHFFPYPYAYRCPFGRGGNETATLAAEYFERALRDPEGGINRPAAVI
LEAVQGEGGVIPAPVEWLRAVRRVTRDLGIPLIVDEVQSGVGRTGSFYAFQKAGIIPDVV
VLSKAIGGGLPLAVVIYREDLDLWKPGAHAGTFRGNQLAMAAGSKTLEIIERERLVERAA
IAGRRLRANLERIAAQTPYIGEVRGEGLMLGVEVVDPEGLPDALGHPPHGQEIARMIQHE
MFRAGIILETGGRFGSVLRLLPPLVISDAEIDQVSGALAAAFERLGRKAA
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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