SitesBLAST
Comparing WP_013257548.1 NCBI__GCF_000143965.1:WP_013257548.1 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)
33% identity, 99% coverage: 3:380/380 of query aligns to 8:393/400 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)
34% identity, 99% coverage: 6:380/380 of query aligns to 12:394/401 of Q56YA5
- TGT 68:70 (≠ SGT 61:63) binding pyridoxal 5'-phosphate
- T148 (= T139) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 189:190) binding pyridoxal 5'-phosphate
- K201 (= K190) binding 3-hydroxypyruvate
- P251 (≠ S239) mutation to L: Abolishes aminotransferase activity.
- R347 (= R333) binding 3-hydroxypyruvate
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
34% identity, 99% coverage: 6:380/380 of query aligns to 10:392/399 of 6pk1A
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
34% identity, 91% coverage: 3:347/380 of query aligns to 16:362/381 of 2dr1A
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
35% identity, 90% coverage: 6:346/380 of query aligns to 3:334/348 of 1iugA
3zrqA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
32% identity, 98% coverage: 6:376/380 of query aligns to 4:379/382 of 3zrqA
3zrrA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
32% identity, 98% coverage: 6:376/380 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 (= D164), V161 (= V166), Y236 (≠ F237), T239 (= T238), R333 (= R333)
3zrpA Crystal structure and substrate specificity of a thermophilic archaeal serine : pyruvate aminotransferase from sulfolobus solfataricus (see paper)
32% identity, 97% coverage: 7:376/380 of query aligns to 1:375/377 of 3zrpA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
27% identity, 98% coverage: 5:376/380 of query aligns to 9:385/387 of 3islA
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
30% identity, 88% coverage: 6:338/380 of query aligns to 22:360/385 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 (= D164), V180 (= V166), K204 (= K190)
Sites not aligning to the query:
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
30% identity, 92% coverage: 6:356/380 of query aligns to 21:376/377 of 1vjoA
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
28% identity, 91% coverage: 6:350/380 of query aligns to 21:370/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ T63), A78 (≠ G64), H79 (vs. gap), W104 (≠ F88), S154 (≠ T139), D179 (= D164), V181 (= V166), Q204 (= Q189), K205 (= K190), Y256 (≠ G235), T259 (= T238)
Q7PRG3 3-hydroxykynurenine transaminase; AgHKT; Alanine--glyoxylate aminotransferase; EC 2.6.1.63; EC 2.6.1.44 from Anopheles gambiae (African malaria mosquito) (see paper)
27% identity, 90% coverage: 6:347/380 of query aligns to 21:370/396 of Q7PRG3
- SAH 77:79 (≠ TG- 63:64) binding in other chain
- S154 (≠ T139) binding in other chain
- Q204 (= Q189) binding in other chain
- K205 (= K190) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding pyridoxal 5'-phosphate
- T259 (vs. gap) binding pyridoxal 5'-phosphate
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
27% identity, 90% coverage: 6:347/380 of query aligns to 20:369/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ T63), A77 (≠ G64), H78 (vs. gap), W103 (≠ F88), S153 (≠ T139), D178 (= D164), V180 (= V166), Q203 (= Q189), K204 (= K190), Y255 (vs. gap), T258 (vs. gap)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
27% identity, 90% coverage: 6:347/380 of query aligns to 19:368/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G10), S41 (≠ H28), N42 (≠ H29), S152 (≠ T139), Y254 (vs. gap), Q342 (≠ A321), L345 (≠ Q324), R354 (= R333)
- binding pyridoxal-5'-phosphate: S75 (≠ T63), A76 (≠ G64), H77 (vs. gap), W102 (≠ F88), S152 (≠ T139), D177 (= D164), V179 (= V166), K203 (= K190), Y254 (vs. gap), T257 (vs. gap)
Q0IG34 3-hydroxykynurenine transaminase; 3-hydroxykynurenine transaminase and alanine--glyoxylate aminotransferase; Ae-HKT/AGT; Alanine--glyoxylate aminotransferase; EC 2.6.1.63; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
28% identity, 91% coverage: 6:350/380 of query aligns to 21:370/400 of Q0IG34
- SAH 77:79 (≠ TG- 63:64) binding in other chain
- S154 (≠ T139) binding in other chain
- Q204 (= Q189) binding in other chain
- K205 (= K190) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ G235) binding pyridoxal 5'-phosphate
- T259 (= T238) binding pyridoxal 5'-phosphate
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
29% identity, 88% coverage: 6:338/380 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)
30% identity, 88% coverage: 6:338/380 of query aligns to 20:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S61), G77 (= G62), H78 (≠ T63), W103 (≠ F88), S153 (≠ T139), D178 (= D164), V180 (= V166), Q203 (= Q189), K204 (= K190), Y255 (≠ F237), T258 (= T238)
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)
29% identity, 88% coverage: 6:338/380 of query aligns to 25:365/392 of P21549
- R36 (= R17) 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 (≠ A131) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ Y133) 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 (≠ L137) 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 (= G142) 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 (≠ I147) 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 (≠ T154) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D164) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ A168) 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 (≠ V183) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S186) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K190) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ G199) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ S214) 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 (vs. gap) 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 (≠ Q230) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (= I254) to T: in dbSNP:rs140992177
- A280 (≠ D255) to V: in dbSNP:rs73106685
- V326 (≠ A299) to I: in dbSNP:rs115057148
- I340 (≠ K313) 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
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
29% identity, 88% coverage: 6:338/380 of query aligns to 22:362/387 of 1j04A
Query Sequence
>WP_013257548.1 NCBI__GCF_000143965.1:WP_013257548.1
MKKVSLLAPGPTPVPSRTLLAMAQPLIHHRSADFLEIFGKVRQGLKKVFQTENEVLTFCS
SGTGAMESSVANLLSPGDKAIAIRGGKFGERWTEILKAYGCQPVNLDVPWGQAVKPADVA
KLLADDPSIKAVYVQALETSTGVAHPIEELAKVTAKTDAVLVVDAVSALLAYDIPVDKWG
LDVVISGSQKAMMLPPGLGFVSIGPKALKLMESSKLPKFYFSWAKELKNQTQNKGAFTSP
VTLFMGLLDIFDYIDELGMQNIFAETGLKSKAFKAAMAALGLTLYSKECPSQALTAVEAP
AGVDAQAVVKWLKEKYGIFIAGGQDQAKGKIFRVAHMGHISEFDTLQGISAIEMALAGLG
YKFEMGAGVAAAQKVFGEAI
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