SitesBLAST
Comparing WP_012386429.1 NCBI__GCF_000019845.1:WP_012386429.1 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)
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)
46% identity, 94% coverage: 6:381/398 of query aligns to 8:385/401 of Q56YA5
- TGT 68:70 (≠ SGT 65:67) binding pyridoxal 5'-phosphate
- T148 (= T145) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 197:198) binding pyridoxal 5'-phosphate
- K201 (= K198) binding 3-hydroxypyruvate
- P251 (= P247) mutation to L: Abolishes aminotransferase activity.
- R347 (= R343) binding 3-hydroxypyruvate
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
46% identity, 94% coverage: 6:381/398 of query aligns to 6:383/399 of 6pk1A
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
46% identity, 94% coverage: 6:381/398 of query aligns to 7:384/400 of 6pk3B
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
30% identity, 93% coverage: 10:381/398 of query aligns to 10:380/387 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)
30% identity, 93% coverage: 10:381/398 of query aligns to 14:402/416 of O32148
- Q37 (≠ H33) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K198) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ F243) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
32% identity, 84% coverage: 13:348/398 of query aligns to 24:357/377 of 1vjoA
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
31% identity, 86% coverage: 7:348/398 of query aligns to 16:354/381 of 2dr1A
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
31% identity, 86% coverage: 9:349/398 of query aligns to 21:362/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
31% identity, 86% coverage: 9:349/398 of query aligns to 21:362/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
31% identity, 86% coverage: 9:349/398 of query aligns to 21:362/385 of 2hufA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
31% identity, 86% coverage: 9:349/398 of query aligns to 21:362/393 of Q3LSM4
- SGH 78:80 (≠ SGT 65:67) binding in other chain
- S155 (≠ T145) binding glyoxylate; binding L-alanine
- Q205 (= Q197) binding in other chain
- K206 (= K198) modified: N6-(pyridoxal phosphate)lysine
- Y257 (≠ F243) binding pyridoxal 5'-phosphate
- T260 (= T246) binding pyridoxal 5'-phosphate
- R356 (= R343) binding glyoxylate
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
30% identity, 85% coverage: 13:351/398 of query aligns to 25:364/387 of 1j04A
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
30% identity, 85% coverage: 13:351/398 of query aligns to 23:362/384 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, 85% coverage: 13:351/398 of query aligns to 23:362/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S65), G77 (= G66), H78 (≠ T67), W103 (≠ F92), S153 (≠ T145), D178 (= D172), V180 (≠ I174), Q203 (= Q197), K204 (= K198), Y255 (≠ F243), T258 (= T246)
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, 85% coverage: 13:351/398 of query aligns to 28:367/392 of P21549
- R36 (= R21) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ L26) 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 (≠ D32) 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 (= G66) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F92) 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 (≠ W96) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A137) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ M139) 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 (≠ N143) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T145) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G148) 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 (≠ I153) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ R157) 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 (≠ I160) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D172) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S176) 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 (≠ V191) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S194) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K198) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ G207) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ S219) 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 (≠ W231) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ L262) to T: in dbSNP:rs140992177
- A280 (≠ L263) to V: in dbSNP:rs73106685
- V326 (≠ M309) to I: in dbSNP:rs115057148
- I340 (≠ L323) 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
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
30% identity, 85% coverage: 13:351/398 of query aligns to 25:362/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P13), G26 (= G14), L346 (= L334), R355 (= R343)
- binding pyridoxal-5'-phosphate: S78 (= S65), G79 (= G66), H80 (≠ T67), W105 (= W96), S153 (≠ T145), D178 (= D172), V180 (≠ I174), K204 (= K198)
Sites not aligning to the query:
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)
29% identity, 87% coverage: 13:357/398 of query aligns to 24:370/400 of Q0IG34
- SAH 77:79 (≠ SSG 64:66) binding in other chain
- S154 (≠ T145) binding in other chain
- Q204 (= Q197) binding in other chain
- K205 (= K198) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding pyridoxal 5'-phosphate
- T259 (= T246) binding pyridoxal 5'-phosphate
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
29% identity, 87% coverage: 13:357/398 of query aligns to 24:370/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (= S64), A78 (≠ S65), H79 (≠ G66), W104 (≠ F92), S154 (≠ T145), D179 (= D172), V181 (≠ I174), Q204 (= Q197), K205 (= K198), Y256 (vs. gap), T259 (= T246)
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
30% identity, 84% coverage: 13:348/398 of query aligns to 24:358/383 of 3kgxA
Sites not aligning to the query:
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
30% identity, 84% coverage: 13:348/398 of query aligns to 28:363/388 of 3kgwB
Query Sequence
>WP_012386429.1 NCBI__GCF_000019845.1:WP_012386429.1
MTTQQGRHFLQIPGPSPVPERILRALSMQVIDHRGPEFGALGREVLAGCQTIFKTSGPVV
IYPSSGTGAWEAAIVNTLSPGDKVLMVETGHFATLWRKMAGRWGLDVDFLAGDWRHGADP
AAIEAKLAEDKPKSIKAVMVVHNETSTGVISRIAEIRKAIDKANHPALLMVDTISSLGSA
DYRHEEWGVDVTVSCSQKGLMLPPGLGFTAISDKALAASKTNKMPRSYWDWEEMLKPNAN
GFFPYTPATNLLYGLREAIKILLEEGLDTVFARHQHLAAATRAAVRAWGLEILCLEPAEY
SPVLTAILMPQGHDADQFRALVLEKYNMSLGAGLTNLAGKVFRIGHLGECNELTLIGTLG
GVEMGLAAAGVPHKAGGVLAAMQALGDLNTAVSQLAAE
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