SitesBLAST
Comparing 7023122 FitnessBrowser__ANA3:7023122 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, 97% coverage: 13:376/377 of query aligns to 17:376/377 of 1vjoA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
38% identity, 97% coverage: 13:376/377 of query aligns to 6:365/387 of 3islA
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)
40% identity, 97% coverage: 13:377/377 of query aligns to 21:385/392 of P21549
- R36 (≠ E28) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ Q33) to E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; 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 (= G39) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; 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 (= G74) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F100) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs180177197
- A112 (≠ M104) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ F143) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ A145) to I: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein destabilization; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; mitochondrial mistargeting; dbSNP:rs121908524
- G156 (≠ A149) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T151) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G154) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; 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; when associated with L-11 and M-340 on the minor AGXT allele; 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 (≠ A159) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ C163) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in mitochondrial mistargeting; slight 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; dbSNP:rs121908529
- C173 (≠ A166) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D176) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S180) 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 (≠ A195) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S198) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K202) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S211) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R226) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908526; to H: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908527
- I244 (≠ Q237) to T: in HP1; prevalent mutation in the Canary islands; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; partial mitochondrial mistargeting; dbSNP:rs121908525
- C253 (≠ S246) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ L272) to T: in dbSNP:rs140992177
- A280 (= A273) to V: in dbSNP:rs73106685
- V326 (≠ I318) to I: in dbSNP:rs115057148
- I340 (≠ L332) to M: associated with hyperoxaluria; dbSNP:rs4426527
Sites not aligning to the query:
- 9 T → N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
- 11 P → L: reduction of specific alanine--glyoxylate aminotransferase activity in vitro; causes mitochondrial mistargeting when associated with R-170; 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)
40% identity, 97% coverage: 13:377/377 of query aligns to 16:380/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ P73), G77 (= G74), H78 (≠ S75), W103 (≠ F100), S153 (≠ T151), D178 (= D176), V180 (= V178), Q203 (= Q201), K204 (= K202), Y255 (= Y253), T258 (= T256)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
40% identity, 97% coverage: 13:377/377 of query aligns to 16:380/384 of 6rv0A
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
40% identity, 97% coverage: 13:377/377 of query aligns to 18:382/387 of 1j04A
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
39% identity, 97% coverage: 13:377/377 of query aligns to 21:383/388 of 3kgwB
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
39% identity, 97% coverage: 13:377/377 of query aligns to 17:378/383 of 3kgxA
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
40% identity, 97% coverage: 13:377/377 of query aligns to 18:380/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P20), G26 (= G21), L346 (= L343), R355 (= R352)
- binding pyridoxal-5'-phosphate: S78 (≠ P73), G79 (= G74), H80 (≠ S75), W105 (≠ F100), S153 (≠ T151), D178 (= D176), V180 (= V178), K204 (= K202)
Sites not aligning to the query:
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)
36% identity, 97% coverage: 13:376/377 of query aligns to 10:387/416 of O32148
- Q37 (≠ H40) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K202) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ Y253) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
40% identity, 97% coverage: 13:376/377 of query aligns to 18:380/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
40% identity, 97% coverage: 13:376/377 of query aligns to 18:380/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
40% identity, 97% coverage: 13:376/377 of query aligns to 18:380/385 of 2hufA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
40% identity, 97% coverage: 13:376/377 of query aligns to 18:380/393 of Q3LSM4
- SGH 78:80 (≠ PGS 73:75) binding in other chain
- S155 (≠ T151) binding ; binding
- Q205 (= Q201) binding in other chain
- K206 (= K202) modified: N6-(pyridoxal phosphate)lysine
- Y257 (= Y253) binding
- T260 (= T256) binding
- R356 (= R352) binding
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, 99% coverage: 5:377/377 of query aligns to 6:381/396 of Q7PRG3
- SAH 77:79 (≠ PGS 73:75) binding in other chain
- S154 (≠ T151) binding in other chain
- Q204 (= Q201) binding in other chain
- K205 (= K202) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y253) binding
- T259 (= T256) binding
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
37% identity, 99% coverage: 5:377/377 of query aligns to 5:380/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ P73), A77 (≠ G74), H78 (≠ S75), W103 (≠ F100), S153 (≠ T151), D178 (= D176), V180 (= V178), Q203 (= Q201), K204 (= K202), Y255 (= Y253), T258 (= T256)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
37% identity, 99% coverage: 5:377/377 of query aligns to 4:379/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G21), S41 (≠ G39), N42 (≠ H40), S152 (≠ T151), Y254 (= Y253), Q342 (≠ G340), L345 (= L343), R354 (= R352)
- binding pyridoxal-5'-phosphate: S75 (≠ P73), A76 (≠ G74), H77 (≠ S75), W102 (≠ F100), S152 (≠ T151), D177 (= D176), V179 (= V178), K203 (= K202), Y254 (= Y253), T257 (= T256)
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
36% identity, 97% coverage: 13:377/377 of query aligns to 17:381/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ P73), A78 (≠ G74), H79 (≠ S75), W104 (≠ F100), S154 (≠ T151), D179 (= D176), V181 (= V178), Q204 (= Q201), K205 (= K202), Y256 (= Y253), T259 (= T256)
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)
36% identity, 97% coverage: 13:376/377 of query aligns to 17:380/400 of Q0IG34
- SAH 77:79 (≠ PGS 73:75) binding in other chain
- S154 (≠ T151) binding in other chain
- Q204 (= Q201) binding in other chain
- K205 (= K202) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y253) binding
- T259 (= T256) binding
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
36% identity, 96% coverage: 16:376/377 of query aligns to 2:350/352 of 2yrrA
Query Sequence
>7023122 FitnessBrowser__ANA3:7023122
MLPAPHFSAFNPPRRILMGPGPSDVYPEVLAAQARPTVGHLDPLFVGMMDELKSLIQYAF
QTKNEMTMAVSAPGSAGMETCFVNLVEPGEKVIVCRNGVFGERMRQNVERVGAIAVLVDN
EWGTPVDAAAVEAALKANPDAKFLAFVHAETSTGALSDAKTLCALAKQYGCLSIVDAVTS
LGGVELRVDEWGIDAIYSGSQKCLSCVPGLSPVSFSPNAVEKLKNRKTPVQSWFLDQSLV
MAYWTSAGGKRSYHHTAPVNALYALHESLRLLAEEGLENAWKRHQDMHLVLRAGLEKLGL
KFVVAEASRLPQLNAIYIPEGVDDAAVRARLLKDYNLEIGAGLGALAGKAWRIGLMGFGA
RRENVALCLRALEEVLN
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