SitesBLAST
Comparing 8500978 FitnessBrowser__Miya:8500978 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)
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
32% identity, 90% coverage: 4:355/389 of query aligns to 16:370/381 of 2dr1A
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
33% identity, 86% coverage: 7:342/389 of query aligns to 3:329/348 of 1iugA
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
28% identity, 86% coverage: 4:339/389 of query aligns to 8:351/400 of 6pk3B
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
28% identity, 86% coverage: 4:339/389 of query aligns to 7:350/399 of 6pk1A
Q56YA5 Serine--glyoxylate aminotransferase; Alanine--glyoxylate aminotransferase; AGT; Asparagine aminotransferase; Serine--pyruvate aminotransferase; EC 2.6.1.45; EC 2.6.1.44; EC 2.6.1.-; EC 2.6.1.51 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
28% identity, 86% coverage: 4:339/389 of query aligns to 9:352/401 of Q56YA5
- TGT 68:70 (≠ SGS 62:64) binding
- T148 (= T140) binding
- QK 200:201 (= QK 190:191) binding
- K201 (= K191) binding
- P251 (≠ T240) mutation to L: Abolishes aminotransferase activity.
- R347 (= R334) binding
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
31% identity, 91% coverage: 7:360/389 of query aligns to 25:385/388 of 3kgwB
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
31% identity, 91% coverage: 7:360/389 of query aligns to 21:380/383 of 3kgxA
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
31% identity, 86% coverage: 7:339/389 of query aligns to 20:360/384 of 6rv0A
5hhyA Structure of human alanine:glyoxylate aminotransferase major allele (agt-ma) showing x-ray induced reduction of plp internal aldimine to 4'-deoxy-piridoxine-phosphate (plr) (see paper)
31% identity, 86% coverage: 7:339/389 of query aligns to 20:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S64), G77 (= G65), H78 (vs. gap), W103 (≠ F89), S153 (≠ T140), D178 (= D165), V180 (≠ I167), Q203 (= Q190), K204 (= K191), Y255 (≠ F238), T258 (= T239)
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
30% identity, 86% coverage: 7:340/389 of query aligns to 21:358/377 of 1vjoA
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
35% identity, 86% coverage: 7:339/389 of query aligns to 3:331/352 of 2yrrA
2yriA Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine
35% identity, 86% coverage: 7:339/389 of query aligns to 3:331/352 of 2yriA
- binding (s,e)-3-hydroxy-2-((3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)methyleneamino)-2-methylpropanoic acid: G7 (= G11), S60 (= S64), G61 (= G65), S62 (≠ V66), F85 (= F89), T135 (= T140), D160 (= D165), V162 (≠ I167), K186 (= K191), R326 (= R334)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y229 (≠ T236), T232 (= T239)
P21549 Alanine--glyoxylate aminotransferase; AGT; Serine--pyruvate aminotransferase; SPT; EC 2.6.1.44; EC 2.6.1.51 from Homo sapiens (Human) (see 24 papers)
31% identity, 86% coverage: 7:339/389 of query aligns to 25:365/392 of P21549
- R36 (= R18) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M23) to E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of protein stability; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; partial mitochondrial mistargeting; intraperoxisomal protein aggregation seen; dbSNP:rs121908523; to V: in HP1; reduced alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177168
- G47 (≠ H29) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; reduced expression levels; reduced pyridoxal phosphate binding; reduced dimerization; reduced thermostability; increased propensity to aggregation; increased susceptibility to proteolytic degradation within the N-terminal region; mitochondrial mistargeting; exposure to pyridoxine can rescue the functionality by partially preventing aggregation and degradation and by redirecting all the protein to the peroxisome; dbSNP:rs180177173
- G82 (= G65) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F89) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs180177197
- A112 (≠ W93) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A131) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ V133) to I: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein destabilization; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; mitochondrial mistargeting; dbSNP:rs121908524
- G156 (≠ S138) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T140) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G143) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization; dbSNP:rs180177227; to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; loss of dimerization; dbSNP:rs180177227; to S: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; reduced expression levels; decreased protein stability; protein aggregation seen in the cytosol with a decreased aggregation propensity in the presence of pyridoxal phosphate; reduced peroxisomal localization; dbSNP:rs180177227
- L166 (≠ V148) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ A152) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in mitochondrial mistargeting; slight decrease in alanine--glyoxylate aminotransferase activity; loss of dimerization; partial loss of protein stability but protein stability increases in the presence of pyridoxal phosphate; causes protein aggregation; dbSNP:rs121908529
- C173 (≠ T155) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D165) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ A169) to F: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization but improved dimerization in the presence of pyridoxal phosphate; decreased protein stability; dbSNP:rs180177238
- I202 (≠ C184) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ T187) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K191) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ G200) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ D213) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908526; to H: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908527
- I244 (≠ F224) to T: in HP1; prevalent mutation in the Canary islands; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; partial mitochondrial mistargeting; dbSNP:rs121908525
- C253 (vs. gap) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ F255) to T: in dbSNP:rs140992177
- A280 (≠ R256) to V: in dbSNP:rs73106685
- V326 (≠ L300) to I: in dbSNP:rs115057148
- I340 (≠ A314) to M: associated with hyperoxaluria; dbSNP:rs4426527
Sites not aligning to the query:
- 9 T → N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
- 11 P → L: reduction of specific alanine--glyoxylate aminotransferase activity in vitro; causes mitochondrial mistargeting when associated with R-170; dbSNP:rs34116584
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
31% identity, 86% coverage: 7:339/389 of query aligns to 22:362/387 of 1j04A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
31% identity, 86% coverage: 7:339/389 of query aligns to 22:360/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P10), G26 (= G11), L346 (≠ Q325), R355 (= R334)
- binding pyridoxal-5'-phosphate: S78 (= S64), G79 (= G65), H80 (vs. gap), W105 (≠ F89), S153 (≠ T140), D178 (= D165), V180 (≠ I167), K204 (= K191)
Sites not aligning to the query:
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
28% identity, 86% coverage: 7:340/389 of query aligns to 10:347/387 of 3islA
3zrrA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
30% identity, 91% coverage: 7:361/389 of query aligns to 1:360/379 of 3zrrA
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: V4 (≠ P10), F24 (≠ H30), G58 (≠ S64), G59 (= G65), T60 (≠ V66), F84 (= F89), T134 (= T140), D159 (= D165), V161 (≠ I167), Y236 (≠ T236), T239 (= T239), R333 (= R334)
3zrqA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
30% identity, 91% coverage: 7:361/389 of query aligns to 4:363/382 of 3zrqA
Q988B8 Pyridoxamine--pyruvate transaminase; Pyridoxamine-pyruvate aminotransferase; EC 2.6.1.30 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see 2 papers)
28% identity, 96% coverage: 8:379/389 of query aligns to 14:391/393 of Q988B8
- E68 (≠ S64) binding ; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
- Y95 (≠ F89) binding
- T146 (= T140) binding
- K197 (= K191) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
- C198 (≠ G192) mutation to A: No effect on enzyme activity.
- R336 (≠ Q325) mutation to A: Strongly decreased affinity for pyruvate.
- R345 (= R334) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2z9xA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxyl-l-alanine (see paper)
28% identity, 96% coverage: 8:379/389 of query aligns to 13:390/392 of 2z9xA
Query Sequence
>8500978 FitnessBrowser__Miya:8500978
MLDKPRLLTPGPTPTPERVRLAMAHDMIHHRKPAFKAIMAAVQPKLRELFGTAQPVLPMA
CSGSGVMTAAVHGLFRPGEKVIVVEGGKFGQRWREIAAVRGLNVVSVVVDWGRPVTPAEV
EAALNEHPDAAGVLVQLSETSTGTLHPVREIARLTAGRDTLLVVDGISAVSISPCPMDEW
GIDCLLTGSQKGLMLPPGLGLIALSERAWRKADTVPPSCFYFNFRGELANLEKQQTLFTT
PVSLIIGLNESLDMFREVGLETVYRKQWALTQMARRGVTAMGLEPLVKEGYTWGLTSVLL
PEGVPATGVLRVAAERFGVIMAAGQDHMKERIIRIGHMGWLDWADLAAGLHALAEGFRAC
GGYIGTRDVLEQALAAYQAGLAVAPGTEI
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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