SitesBLAST
Comparing WP_013011685.1 NCBI__GCF_000025725.1:WP_013011685.1 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)
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)
34% identity, 99% coverage: 3:380/382 of query aligns to 9:394/401 of Q56YA5
- TGT 68:70 (≠ SGT 61:63) binding pyridoxal 5'-phosphate
- T148 (= T139) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 190:191) binding pyridoxal 5'-phosphate
- K201 (= K191) binding 3-hydroxypyruvate
- P251 (= P240) mutation to L: Abolishes aminotransferase activity.
- R347 (= R333) binding 3-hydroxypyruvate
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
34% identity, 99% coverage: 3:380/382 of query aligns to 8:393/400 of 6pk3B
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
34% identity, 99% coverage: 3:380/382 of query aligns to 7:392/399 of 6pk1A
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
35% identity, 90% coverage: 5:346/382 of query aligns to 2:334/348 of 1iugA
3zrqA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
35% identity, 98% coverage: 4:376/382 of query aligns to 2:379/382 of 3zrqA
3zrrA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
35% identity, 97% coverage: 6:376/382 of query aligns to 1:376/379 of 3zrrA
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: V4 (≠ P9), F24 (≠ H29), G58 (≠ S61), G59 (= G62), T60 (= T63), F84 (= F88), T134 (= T139), D159 (= D165), V161 (≠ I167), Y236 (= Y238), T239 (= T239), R333 (= R333)
3zrpA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
35% identity, 96% coverage: 10:376/382 of query aligns to 4:375/377 of 3zrpA
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
32% identity, 87% coverage: 6:339/382 of query aligns to 19:355/381 of 2dr1A
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
30% identity, 98% coverage: 4:378/382 of query aligns to 8:387/387 of 3islA
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
30% identity, 93% coverage: 3:357/382 of query aligns to 18:377/377 of 1vjoA
O32148 (S)-ureidoglycine--glyoxylate transaminase; UGXT; (S)-ureidoglycine--glyoxylate aminotransferase; Purine catabolism protein PucG; EC 2.6.1.112 from Bacillus subtilis (strain 168) (see paper)
28% identity, 98% coverage: 4:378/382 of query aligns to 12:409/416 of O32148
- Q37 (≠ H29) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K191) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ T236) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
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)
27% identity, 96% coverage: 10:377/382 of query aligns to 17:390/393 of Q988B8
- E68 (≠ S61) binding pyridoxal 5'-phosphate; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
- Y95 (≠ F88) binding pyridoxal 5'-phosphate
- T146 (= T139) binding pyridoxal 5'-phosphate
- K197 (= K191) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
- C198 (≠ A192) mutation to A: No effect on enzyme activity.
- R336 (≠ Q324) mutation to A: Strongly decreased affinity for pyruvate.
- R345 (= R333) binding pyridoxal 5'-phosphate
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)
27% identity, 96% coverage: 10:377/382 of query aligns to 16:389/392 of 2z9xA
2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
27% identity, 96% coverage: 10:377/382 of query aligns to 16:389/392 of 2z9wA
2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
27% identity, 96% coverage: 10:377/382 of query aligns to 16:389/392 of 2z9vA
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)
28% identity, 91% coverage: 4:350/382 of query aligns to 23:377/392 of P21549
- R36 (≠ K17) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M22) to E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; to R: in HP1; associated in cis with L-11 and M-340; 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 (≠ H28) to R: in HP1; associated in cis with L-11 and M-340; 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 (= G62) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F88) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs180177197
- A112 (≠ W92) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ K130) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ V132) to I: in HP1; associated in cis with L-11 and M-340; results in protein destabilization; no loss of dimerization; decreased alanine--glyoxylate aminotransferase activity; loss of alanine--glyoxylate aminotransferase activity when associated with L-11 and M-340; mitochondrial mistargeting when associated with L-11 and M-340; dbSNP:rs121908524
- G156 (= G136) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T139) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (≠ T142) to C: in HP1; associated in cis with L-11 and M-340; 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; associated in cis with L-11 and M-340; 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 (≠ V147) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ A151) to R: in HP1; associated in cis with L-11 and M-340; 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; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and M-340; results in mitochondrial mistargeting when associated with L-11 and M-340; dbSNP:rs121908529
- C173 (≠ V154) 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 (= S169) 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 (= I184) 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 (= S200) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ E213) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908526; to H: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908527
- I244 (≠ L224) to T: in HP1; associated in cis with L-11 and M-340; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity in vitro; no loss of dimerization; partial mitochondrial mistargeting; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and M-340; dbSNP:rs121908525
- C253 (≠ L228) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ F255) to T: in dbSNP:rs140992177
- A280 (≠ E256) to V: in dbSNP:rs73106685
- V326 (≠ L299) to I: in dbSNP:rs115057148
- I340 (≠ R313) to M: in allele minor; associated in cis with L-11; no effect on alanine--glyoxylate aminotransferase activity in vitro; decreased specific alanine--glyoxylate aminotransferase activity in vitro when associated with L-11; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and I-152; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and R-170; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with L-11 and T-244; results in mitochondrial mistargeting when associated with L-11 and R-170; dbSNP:rs4426527
Sites not aligning to the query:
- 9 T → N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
- 11 P → L: in allele minor; associated in cis with M-340; decreased specific alanine--glyoxylate aminotransferase activity in vitro when associated with M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with I-152 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with R-170 and M-340; loss of alanine--glyoxylate aminotransferase activity in vitro when associated with T-244 and M-340; causes mitochondrial mistargeting when associated with R-170 and M-340; dbSNP:rs34116584
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)
28% identity, 91% coverage: 4:350/382 of query aligns to 18:372/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S61), G77 (= G62), H78 (≠ T63), W103 (≠ F88), S153 (≠ T139), D178 (= D165), V180 (≠ I167), Q203 (= Q190), K204 (= K191), Y255 (≠ T235), T258 (≠ Y238)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
28% identity, 91% coverage: 3:350/382 of query aligns to 17:372/384 of 6rv0A
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
28% identity, 91% coverage: 4:350/382 of query aligns to 20:374/387 of 1j04A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
28% identity, 91% coverage: 4:350/382 of query aligns to 20:372/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P9), G26 (= G10), L346 (≠ Q324), R355 (= R333)
- binding pyridoxal-5'-phosphate: S78 (= S61), G79 (= G62), H80 (≠ T63), W105 (≠ F88), S153 (≠ T139), D178 (= D165), V180 (≠ I167), K204 (= K191)
Sites not aligning to the query:
Query Sequence
>WP_013011685.1 NCBI__GCF_000025725.1:WP_013011685.1
MLKKYLIAPGPTPVPEKVLLEMTKPVIHHRTSEFSATFEKVANGLKKVFSTEQDVLMLAG
SGTAAMEAAVVNTLNPGDNVLVINAGKFGQRWRDICKTYGILVSTIDMDWGKAAKPEEIE
QFLKANPDTKAVLLQGSETSTTVYHPVEEIAKVVRKNENTLLIVDGITSIGVHDTKFDEW
GIDIAITGSQKAFMLPPGLSLICLSKKAWNFVEKSTIPRYYLDLRKELKSQKQATTAYTP
ALTLINGLAVVLEMFEEEGLENVYKRHAVNGEATRAAVKAMGFKLLAETPSNAATGFYLP
EDIDGGKLVKFMREKVGITYAGGQDHLKGRIVRISHLGYHDAFDTITAISGLEMGLRKFG
VDIKLGSGIAAAEEILQNYIGE
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