SitesBLAST
Comparing WP_012471375.1 NCBI__GCF_000020385.1:WP_012471375.1 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)
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
35% identity, 97% coverage: 4:349/355 of query aligns to 18:368/381 of 2dr1A
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
31% identity, 95% coverage: 5:342/355 of query aligns to 11:358/400 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)
31% identity, 95% coverage: 5:342/355 of query aligns to 12:359/401 of Q56YA5
- TGT 68:70 (≠ SAF 60:62) binding pyridoxal 5'-phosphate
- T148 (= T135) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 186:187) binding pyridoxal 5'-phosphate
- K201 (= K187) binding 3-hydroxypyruvate
- P251 (= P236) mutation to L: Abolishes aminotransferase activity.
- R347 (= R330) binding 3-hydroxypyruvate
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
31% identity, 95% coverage: 5:342/355 of query aligns to 10:357/399 of 6pk1A
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
30% identity, 97% coverage: 5:350/355 of query aligns to 3:347/352 of 2yrrA
2yriA Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine
30% identity, 97% coverage: 5:350/355 of query aligns to 3:347/352 of 2yriA
- binding (s,e)-3-hydroxy-2-((3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)methyleneamino)-2-methylpropanoic acid: G7 (= G9), S60 (≠ F62), G61 (= G63), S62 (≠ A64), F85 (= F85), T135 (= T135), D160 (= D161), V162 (= V163), K186 (= K187), R326 (= R330)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y229 (≠ T232), T232 (= T235)
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
29% identity, 94% coverage: 3:335/355 of query aligns to 19:357/377 of 1vjoA
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
27% identity, 93% coverage: 5:335/355 of query aligns to 3:326/348 of 1iugA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
29% identity, 98% coverage: 3:349/355 of query aligns to 20:373/393 of Q3LSM4
- SGH 78:80 (≠ SAF 60:62) binding in other chain
- S155 (≠ T135) binding glyoxylate; binding L-alanine
- Q205 (= Q186) binding in other chain
- K206 (= K187) modified: N6-(pyridoxal phosphate)lysine
- Y257 (vs. gap) binding pyridoxal 5'-phosphate
- T260 (= T235) binding pyridoxal 5'-phosphate
- R356 (= R330) binding glyoxylate
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
29% identity, 98% coverage: 3:349/355 of query aligns to 20:373/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
29% identity, 98% coverage: 3:349/355 of query aligns to 20:373/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
29% identity, 98% coverage: 3:349/355 of query aligns to 20:373/385 of 2hufA
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, 93% coverage: 5:335/355 of query aligns to 20:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S60), G77 (≠ A61), H78 (≠ F62), W103 (≠ F85), S153 (≠ T135), D178 (= D161), V180 (= V163), Q203 (= Q186), K204 (= K187), Y255 (vs. gap), T258 (≠ S234)
2bkwA Yeast alanine:glyoxylate aminotransferase yfl030w (see paper)
28% identity, 94% coverage: 2:335/355 of query aligns to 3:357/381 of 2bkwA
Sites not aligning to the query:
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)
30% identity, 93% coverage: 5:335/355 of query aligns to 25:365/392 of P21549
- R36 (≠ E16) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M21) 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 (= G27) 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 (≠ A61) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F85) 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 (≠ W89) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ S127) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ T129) 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 (≠ N133) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T135) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G138) 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 (= L143) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ A147) 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 (≠ M150) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D161) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S165) 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 (≠ C180) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ F183) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K187) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ A196) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ V211) 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 (≠ F220) 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 (≠ K229) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ F251) to T: in dbSNP:rs140992177
- A280 (≠ F252) to V: in dbSNP:rs73106685
- V326 (≠ N297) to I: in dbSNP:rs115057148
- I340 (≠ G311) 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)
30% identity, 93% coverage: 5:335/355 of query aligns to 20:360/384 of 6rv0A
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
30% identity, 93% coverage: 5:335/355 of query aligns to 22:362/387 of 1j04A
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
29% identity, 94% coverage: 3:335/355 of query aligns to 23:363/388 of 3kgwB
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
30% identity, 93% coverage: 5:335/355 of query aligns to 22:360/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P8), G26 (= G9), L346 (≠ Y321), R355 (= R330)
- binding pyridoxal-5'-phosphate: S78 (= S60), G79 (≠ A61), H80 (≠ F62), W105 (≠ F85), S153 (≠ T135), D178 (= D161), V180 (= V163), K204 (= K187)
Sites not aligning to the query:
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
26% identity, 94% coverage: 2:335/355 of query aligns to 7:346/387 of 3islA
Query Sequence
>WP_012471375.1 NCBI__GCF_000020385.1:WP_012471375.1
MVKKLFIPGPVNVAPEVFAAMSQPMIGHRMKEYAELHGRIKTSLKRLMMTESRVFLATSS
AFGAMEGALRNLVKGRCANFCNGAFSDKWHDVTLRCGKEADAVKVPWGQPITAELVDATL
ATGKYDSMTMIHNETSTGVLSPLAEIAAVMRNYPDVMFIVDTVSSMSAMPIGLDELGIDC
CIFGVQKAFALPPGLAIFTATEKALQRAQSVENRGYYFDFMEFAANDDKDNTPSTPCISL
IYGLDCQLQRFFAEGLEARWERHRVMAERTRSWVLERGFELFAPEGARSVTLTSVANSRG
VDLAAIKKQLGEKGYAFDDGYGKIKGKTFRIAHMGDLQPAELEEFLTVLDGELKG
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