SitesBLAST
Comparing WP_012818166.1 NCBI__GCF_000024605.1:WP_012818166.1 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)
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
36% identity, 98% coverage: 6:380/383 of query aligns to 9:391/399 of 6pk1A
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
36% identity, 98% coverage: 6:380/383 of query aligns to 10:392/400 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, 98% coverage: 6:380/383 of query aligns to 11:393/401 of Q56YA5
- TGT 68:70 (≠ SGT 62:64) binding
- T148 (= T139) binding
- QK 200:201 (= QK 189:190) binding
- K201 (= K190) binding
- P251 (= P239) mutation to L: Abolishes aminotransferase activity.
- R347 (= R334) binding
2z9xA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxyl-l-alanine (see paper)
37% identity, 96% coverage: 11:377/383 of query aligns to 16:388/392 of 2z9xA
2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
37% identity, 96% coverage: 11:377/383 of query aligns to 16:388/392 of 2z9wA
2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
37% identity, 96% coverage: 11:377/383 of query aligns to 16:388/392 of 2z9vA
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)
37% identity, 96% coverage: 11:377/383 of query aligns to 17:389/393 of Q988B8
- E68 (≠ S62) binding ; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
- Y95 (≠ F89) binding
- T146 (= T139) binding
- K197 (= K190) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
- C198 (≠ A191) 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
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
37% identity, 92% coverage: 1:353/383 of query aligns to 13:368/381 of 2dr1A
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
33% identity, 96% coverage: 7:373/383 of query aligns to 10:381/387 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)
32% identity, 98% coverage: 7:383/383 of query aligns to 14:413/416 of O32148
- Q37 (≠ H30) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K190) modified: N6-(pyridoxal phosphate)lysine
- N264 (= N234) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
39% identity, 87% coverage: 7:339/383 of query aligns to 3:331/352 of 2yrrA
2yriA Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine
39% identity, 87% coverage: 7:339/383 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 (= S62), G61 (= G63), S62 (≠ T64), F85 (= F89), T135 (= T139), D160 (= D164), V162 (= V166), K186 (= K190), R326 (= R334)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y229 (≠ T235), T232 (= T238)
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
34% identity, 88% coverage: 5:340/383 of query aligns to 18:358/377 of 1vjoA
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
33% identity, 88% coverage: 5:340/383 of query aligns to 22:364/388 of 3kgwB
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, 87% coverage: 7:339/383 of query aligns to 25:365/392 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 (≠ M23) 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 (= G63) 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 (≠ F93) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ V131) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ L133) 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 (≠ N137) 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 (≠ 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 (= G151) 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 (= S168) 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 (≠ T186) 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 (≠ A199) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ N214) 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 (≠ L223) 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 (≠ A225) 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 (≠ L255) to V: in dbSNP:rs73106685
- V326 (≠ A300) to I: in dbSNP:rs115057148
- I340 (≠ A314) 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, 87% coverage: 7:339/383 of query aligns to 20:360/384 of 6rv0A
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
33% identity, 88% coverage: 5:340/383 of query aligns to 18:359/383 of 3kgxA
Sites not aligning to the query:
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, 87% coverage: 7:339/383 of query aligns to 20:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S62), G77 (= G63), H78 (≠ T64), W103 (≠ F89), S153 (≠ T139), D178 (= D164), V180 (= V166), Q203 (= Q189), K204 (= K190), Y255 (≠ K232), T258 (= T235)
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
33% identity, 87% coverage: 7:339/383 of query aligns to 22:362/387 of 1j04A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
33% identity, 87% coverage: 7:339/383 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 (= S62), G79 (= G63), H80 (≠ T64), W105 (≠ F89), S153 (≠ T139), D178 (= D164), V180 (= V166), K204 (= K190)
Sites not aligning to the query:
Query Sequence
>WP_012818166.1 NCBI__GCF_000024605.1:WP_012818166.1
MKKETRLFIPGPTPVPPAVAEAMARPLIGHRTEDFARLYARLEERLRVVLGTKNDIVILT
SSGTGGMEAAVANLVSPGDPVLALVTGKFGERFAELAKVYGGAVEVMEFGWGKAVDLEAV
EEKLKARRFKVVLATHNETSTTVVNDIRGLGELTRRYGALLVVDAVSSAGGMEIRMDDWG
VDVLVTASQKALMVPPGLAIVAASDAAWKAMEENKNPRYYLDLLAARKSKQKYNTPYTPA
VSLFVGLDRALDLILAEGLEKVYRKHRLLARAVRAAIRALGLKLMIPDEYASPVVTGVWA
PEGIEVDRLRKEIASRYGVLLAGGQGPLKGKIFRISHMGYVDAVDILGALGALELGLYRF
GFKFKLGEGLAQAQAVLAEEGEE
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