SitesBLAST
Comparing WP_004042827.1 NCBI__GCF_000337315.1:WP_004042827.1 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)
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
48% identity, 94% coverage: 1:357/378 of query aligns to 22:377/377 of 1vjoA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
43% identity, 100% coverage: 1:377/378 of query aligns to 11:383/387 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)
41% identity, 100% coverage: 1:377/378 of query aligns to 15:405/416 of O32148
- Q37 (≠ H23) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K185) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ Y233) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
41% identity, 94% coverage: 1:357/378 of query aligns to 22:378/383 of 3kgxA
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
41% identity, 94% coverage: 1:357/378 of query aligns to 26:383/388 of 3kgwB
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
39% identity, 94% coverage: 1:357/378 of query aligns to 23:382/387 of 1j04A
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)
39% identity, 94% coverage: 1:357/378 of query aligns to 26:385/392 of P21549
- R36 (= R11) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M16) 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 (= G22) 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 (= G57) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F83) 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 (≠ M87) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ V125) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ G127) 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 (≠ A131) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T133) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G136) 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 (≠ V142) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ T146) 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 (≠ A149) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D159) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S163) 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 (≠ V178) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S181) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K185) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S194) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R209) 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 (≠ L220) 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 (≠ D229) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ V252) to T: in dbSNP:rs140992177
- A280 (= A253) to V: in dbSNP:rs73106685
- V326 (= V298) to I: in dbSNP:rs115057148
- I340 (≠ L312) 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
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)
39% identity, 94% coverage: 1:357/378 of query aligns to 21:380/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ T56), G77 (= G57), H78 (≠ S58), W103 (≠ F83), S153 (≠ T133), D178 (= D159), V180 (= V161), Q203 (= Q184), K204 (= K185), Y255 (= Y233), T258 (= T236)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
39% identity, 94% coverage: 1:357/378 of query aligns to 21:380/384 of 6rv0A
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
37% identity, 96% coverage: 1:362/378 of query aligns to 22:386/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ T56), A78 (≠ G57), H79 (≠ S58), W104 (≠ F83), S154 (≠ T133), D179 (= D159), V181 (= V161), Q204 (= Q184), K205 (= K185), Y256 (= Y233), T259 (= T236)
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)
37% identity, 96% coverage: 1:362/378 of query aligns to 22:386/400 of Q0IG34
- SAH 77:79 (≠ TGS 56:58) binding in other chain
- S154 (≠ T133) binding in other chain
- Q204 (= Q184) binding in other chain
- K205 (= K185) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y233) binding pyridoxal 5'-phosphate
- T259 (= T236) binding pyridoxal 5'-phosphate
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
39% identity, 94% coverage: 1:357/378 of query aligns to 23:380/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P3), G26 (= G4), L346 (= L323), R355 (= R332)
- binding pyridoxal-5'-phosphate: S78 (≠ T56), G79 (= G57), H80 (≠ S58), W105 (≠ F83), S153 (≠ T133), D178 (= D159), V180 (= V161), K204 (= K185)
Sites not aligning to the query:
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
39% identity, 96% coverage: 1:364/378 of query aligns to 23:388/393 of Q3LSM4
- SGH 78:80 (≠ TGS 56:58) binding in other chain
- S155 (≠ T133) binding glyoxylate; binding L-alanine
- Q205 (= Q184) binding in other chain
- K206 (= K185) modified: N6-(pyridoxal phosphate)lysine
- Y257 (= Y233) binding pyridoxal 5'-phosphate
- T260 (= T236) binding pyridoxal 5'-phosphate
- R356 (= R332) binding glyoxylate
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)
37% identity, 96% coverage: 1:362/378 of query aligns to 22:386/396 of Q7PRG3
- SAH 77:79 (≠ TGS 56:58) binding in other chain
- S154 (≠ T133) binding in other chain
- Q204 (= Q184) binding in other chain
- K205 (= K185) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y233) binding pyridoxal 5'-phosphate
- T259 (= T236) binding pyridoxal 5'-phosphate
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
39% identity, 95% coverage: 1:358/378 of query aligns to 23:382/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
39% identity, 95% coverage: 1:358/378 of query aligns to 23:382/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
39% identity, 95% coverage: 1:358/378 of query aligns to 23:382/385 of 2hufA
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
37% identity, 96% coverage: 1:362/378 of query aligns to 20:384/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G4), S41 (≠ G22), N42 (≠ H23), S152 (≠ T133), Y254 (= Y233), Q342 (≠ A320), L345 (= L323), R354 (= R332)
- binding pyridoxal-5'-phosphate: S75 (≠ T56), A76 (≠ G57), H77 (≠ S58), W102 (≠ F83), S152 (≠ T133), D177 (= D159), V179 (= V161), K203 (= K185), Y254 (= Y233), T257 (= T236)
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
37% identity, 96% coverage: 1:362/378 of query aligns to 21:385/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ T56), A77 (≠ G57), H78 (≠ S58), W103 (≠ F83), S153 (≠ T133), D178 (= D159), V180 (= V161), Q203 (= Q184), K204 (= K185), Y255 (= Y233), T258 (= T236)
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
36% identity, 94% coverage: 1:356/378 of query aligns to 4:350/352 of 2yrrA
Query Sequence
>WP_004042827.1 NCBI__GCF_000337315.1:WP_004042827.1
MGPGPSDVHPRVLRAMSTPLVGHLDPSFIEVMNEVQELMRYTFRTDNKWTIPVSGTGSAS
MEAAIGNLVEPGDTMLVPTNGYFGGRMESMAERAGGEVVHVDAPWGEPLDSADVQDAFDE
HQPDVFGFVHAETSTGVKQPSVPELTSIAHDHDALVVADTVTSLGGVELEADDWGIDVAY
SGPQKCLSCPPGASPLTLNDRAMDKVLSREEPTRSWYLDLSLLEGYWGDDRSYHHTAPIT
NVYAIREALRLVAEEGIEERWARHRRVAGALKAGVEAMGLGLNPEDEYWLPSLNAVLVPD
GVDAGAAIDYVLDHYDLEIAGGLGALAGDIFRVGCMGHSARPENVSFLLTALGEALEAQG
ADVDPEAGFAAMREALNQ
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