SitesBLAST
Comparing Synpcc7942_2160 FitnessBrowser__SynE:Synpcc7942_2160 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)
74% identity, 98% coverage: 7:381/384 of query aligns to 2:376/377 of 1vjoA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
44% identity, 95% coverage: 17:381/384 of query aligns to 13:380/393 of Q3LSM4
- SGH 78:80 (≠ TGS 82:84) binding in other chain
- S155 (≠ T159) binding ; binding
- Q205 (= Q209) binding in other chain
- K206 (= K210) modified: N6-(pyridoxal phosphate)lysine
- Y257 (= Y258) binding
- T260 (= T261) binding
- R356 (= R357) binding
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
44% identity, 95% coverage: 17:381/384 of query aligns to 13:380/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
44% identity, 95% coverage: 17:381/384 of query aligns to 13:380/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
44% identity, 95% coverage: 17:381/384 of query aligns to 13:380/385 of 2hufA
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
45% identity, 95% coverage: 17:381/384 of query aligns to 12:377/383 of 3kgxA
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
45% identity, 95% coverage: 17:381/384 of query aligns to 16:382/388 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)
44% identity, 96% coverage: 13:381/384 of query aligns to 12:384/392 of P21549
- R36 (≠ A37) 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 (≠ I42) 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 (= G48) 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 (= G83) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F109) 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 (≠ L113) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ I151) 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 (≠ A153) 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 (≠ A157) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T159) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G162) 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 (= L167) 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 (= G171) 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 (= C174) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D184) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S188) 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 (≠ L203) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S206) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K210) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S219) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R234) 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 (≠ M245) 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 (≠ S254) 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 (= I277) to T: in dbSNP:rs140992177
- A280 (= A278) to V: in dbSNP:rs73106685
- V326 (≠ I323) to I: in dbSNP:rs115057148
- I340 (≠ L337) 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)
44% identity, 96% coverage: 13:381/384 of query aligns to 7:379/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ T82), G77 (= G83), H78 (≠ S84), W103 (≠ F109), S153 (≠ T159), D178 (= D184), V180 (= V186), Q203 (= Q209), K204 (= K210), Y255 (= Y258), T258 (= T261)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
44% identity, 96% coverage: 13:381/384 of query aligns to 7:379/384 of 6rv0A
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
44% identity, 96% coverage: 13:381/384 of query aligns to 9:381/387 of 1j04A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
44% identity, 96% coverage: 13:381/384 of query aligns to 9:379/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P29), G26 (= G30), L346 (= L348), R355 (= R357)
- binding pyridoxal-5'-phosphate: S78 (≠ T82), G79 (= G83), H80 (≠ S84), W105 (≠ F109), S153 (≠ T159), D178 (= D184), V180 (= V186), K204 (= K210)
Sites not aligning to the query:
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
40% identity, 95% coverage: 18:381/384 of query aligns to 13:380/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ T82), A78 (≠ G83), H79 (≠ S84), W104 (≠ F109), S154 (≠ T159), D179 (= D184), V181 (= V186), Q204 (= Q209), K205 (= K210), Y256 (= Y258), T259 (= T261)
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)
40% identity, 95% coverage: 18:381/384 of query aligns to 13:380/400 of Q0IG34
- SAH 77:79 (≠ TGS 82:84) binding in other chain
- S154 (≠ T159) binding in other chain
- Q204 (= Q209) binding in other chain
- K205 (= K210) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y258) binding
- T259 (= T261) binding
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
43% identity, 93% coverage: 17:374/384 of query aligns to 10:371/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G30), S41 (≠ G48), N42 (≠ H49), S152 (≠ T159), Y254 (= Y258), Q342 (≠ G345), L345 (= L348), R354 (= R357)
- binding pyridoxal-5'-phosphate: S75 (≠ T82), A76 (≠ G83), H77 (≠ S84), W102 (≠ F109), S152 (≠ T159), D177 (= D184), V179 (= V186), K203 (= K210), Y254 (= Y258), T257 (= T261)
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
43% identity, 93% coverage: 17:374/384 of query aligns to 11:372/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ T82), A77 (≠ G83), H78 (≠ S84), W103 (≠ F109), S153 (≠ T159), D178 (= D184), V180 (= V186), Q203 (= Q209), K204 (= K210), Y255 (= Y258), T258 (= T261)
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)
43% identity, 93% coverage: 17:374/384 of query aligns to 12:373/396 of Q7PRG3
- SAH 77:79 (≠ TGS 82:84) binding in other chain
- S154 (≠ T159) binding in other chain
- Q204 (= Q209) binding in other chain
- K205 (= K210) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y258) binding
- T259 (= T261) binding
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
40% identity, 94% coverage: 22:383/384 of query aligns to 6:367/387 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)
39% identity, 94% coverage: 22:383/384 of query aligns to 10:389/416 of O32148
- Q37 (≠ H49) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K210) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ Y258) 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
37% identity, 92% coverage: 25:377/384 of query aligns to 2:346/352 of 2yrrA
Query Sequence
>Synpcc7942_2160 FitnessBrowser__SynE:Synpcc7942_2160
MTVTLPSVSEKHRVRLQPLELPERLLLGPGPSNAHPAVLEAISRPPIGHLDPKFLELMTE
VQGLLRYIWQTDNRLTIPVSGTGSAAMEATIANSVEPGDVVLVGVMGYFGNRLVDMAGRY
GADVRTIHKPWGDVFSLAELRQALEEHRPQILALVHAETSTGAEQPLAGVGDLCREFDCL
LLIDTVTSLGAVPTLLDEWGVDLAYSCSQKGLSCPPGVSPFTMGPRAEEKLARRKGKVAN
WYLDMSLLNQYWGSDRVYHHTAPVNMNFGIREALRLIADEGIETVWKRHRDNAEYLWAGL
EDLGLTCHVPVENRLPTLTTVRIPEGVDGKAVSRQLLDEHGIEMGGGLGELAGKVWRIGL
MGYNSRRENVDRLLSILADVLPRS
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