SitesBLAST
Comparing WP_012410502.1 NCBI__GCF_000020025.1:WP_012410502.1 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)
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
36% identity, 97% coverage: 7:377/384 of query aligns to 11:385/400 of 6pk3B
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)
36% identity, 97% coverage: 7:377/384 of query aligns to 12:386/401 of Q56YA5
- TGT 68:70 (≠ SGT 62:64) binding pyridoxal 5'-phosphate
- T148 (= T142) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 193:194) binding pyridoxal 5'-phosphate
- K201 (= K194) binding 3-hydroxypyruvate
- P251 (= P243) mutation to L: Abolishes aminotransferase activity.
- R347 (= R337) binding 3-hydroxypyruvate
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
36% identity, 97% coverage: 7:377/384 of query aligns to 10:384/399 of 6pk1A
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
34% identity, 94% coverage: 4:363/384 of query aligns to 16:375/381 of 2dr1A
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
33% identity, 92% coverage: 6:360/384 of query aligns to 20:376/377 of 1vjoA
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
35% identity, 93% coverage: 7:363/384 of query aligns to 3:347/348 of 1iugA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
29% identity, 98% coverage: 7:383/384 of query aligns to 10:387/387 of 3islA
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: 7:384/384 of query aligns to 14:410/416 of O32148
- Q37 (≠ H30) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K194) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ T239) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
33% identity, 89% coverage: 6:348/384 of query aligns to 21:368/387 of 1j04A
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)
33% identity, 89% coverage: 6:348/384 of query aligns to 19:366/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ T64), G77 (= G65), H78 (vs. gap), W103 (≠ F89), S153 (≠ T142), D178 (= D168), V180 (= V170), Q203 (= Q193), K204 (= K194), Y255 (vs. gap), T258 (= T242)
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)
33% identity, 89% coverage: 6:348/384 of query aligns to 24:371/392 of P21549
- R36 (≠ A18) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ L23) 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 (= G29) 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 (= G65) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F89) 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 (≠ W93) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A134) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ I136) 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 (≠ S140) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T142) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G145) 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 (= L150) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ N154) 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 (≠ V157) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D168) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S172) 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 (= I187) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S190) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K194) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ G203) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ A218) 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 (≠ L227) 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 (≠ K236) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ M258) to T: in dbSNP:rs140992177
- A280 (≠ K259) to V: in dbSNP:rs73106685
- V326 (vs. gap) to I: in dbSNP:rs115057148
- I340 (≠ K317) 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
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
33% identity, 89% coverage: 6:348/384 of query aligns to 19:366/384 of 6rv0A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
32% identity, 89% coverage: 6:348/384 of query aligns to 21:366/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P10), G26 (= G11), L346 (≠ Q328), R355 (= R337)
- binding pyridoxal-5'-phosphate: S78 (≠ T64), G79 (= G65), H80 (vs. gap), W105 (≠ F89), S153 (≠ T142), D178 (= D168), V180 (= V170), K204 (= K194)
Sites not aligning to the query:
3zrqA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
32% identity, 99% coverage: 3:381/384 of query aligns to 1:379/382 of 3zrqA
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
31% identity, 88% coverage: 6:342/384 of query aligns to 21:361/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
31% identity, 88% coverage: 6:342/384 of query aligns to 21:361/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
31% identity, 88% coverage: 6:342/384 of query aligns to 21:361/385 of 2hufA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
31% identity, 88% coverage: 6:342/384 of query aligns to 21:361/393 of Q3LSM4
- SGH 78:80 (≠ SGT 62:64) binding in other chain
- S155 (≠ T142) binding glyoxylate; binding L-alanine
- Q205 (= Q193) binding in other chain
- K206 (= K194) modified: N6-(pyridoxal phosphate)lysine
- Y257 (≠ T239) binding pyridoxal 5'-phosphate
- T260 (= T242) binding pyridoxal 5'-phosphate
- R356 (= R337) binding glyoxylate
3zrrA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
32% identity, 98% coverage: 7:381/384 of query aligns to 1:376/379 of 3zrrA
- binding 3-[o-phosphonopyridoxyl]--amino-benzoic acid: V4 (≠ P10), F24 (≠ H30), G58 (≠ S62), G59 (= G63), T60 (= T64), F84 (= F89), T134 (= T142), D159 (= D168), V161 (= V170), Y236 (≠ P240), T239 (= T242), R333 (= R337)
3zrpA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
32% identity, 97% coverage: 11:381/384 of query aligns to 4:375/377 of 3zrpA
Query Sequence
>WP_012410502.1 NCBI__GCF_000020025.1:WP_012410502.1
MNDKLMLMIPGPTPVPEAALLALAKHPIGHRTSEFSNILAEVTENLKWLHQTQTDVLTLN
VSGTGAVEAGIINFLSPGDRILVGSNGKFGERWVEVGQAYGLNVEEVKVEWGKPLDPAVF
AEKLQADTQKQIKAVIITHSETSTGVLNDLESINRHVKAHGEALIIVDAVTSLGAFNLPV
DAWGLDIVASGSQKGYMIPPGLGFVSVSPKAWEAYKTAKLPKYYLDLGKYRKATAKNTTP
FTPPVNLIVALHTTLRIMKEEGLESIFARHERLKNATRAAIQGLNLPLFAADSSASPAIT
AVAPQGIESDKIRSLMKKRFDIALAGGQDHLSNKIFRIGHLGFVSDRDILSCIASLEVTL
TELGYEDFTPGSGIAAAVKVFSQS
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