SitesBLAST
Comparing H281DRAFT_04750 FitnessBrowser__Burk376:H281DRAFT_04750 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
32% identity, 87% coverage: 28:383/407 of query aligns to 12:376/377 of 1vjoA
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
33% identity, 87% coverage: 27:379/407 of query aligns to 12:376/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
33% identity, 87% coverage: 27:379/407 of query aligns to 12:376/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
33% identity, 87% coverage: 27:379/407 of query aligns to 12:376/385 of 2hufA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
33% identity, 87% coverage: 27:379/407 of query aligns to 12:376/393 of Q3LSM4
- SGH 78:80 (≠ PGS 87:89) binding in other chain
- S155 (≠ T164) binding ; binding
- Q205 (= Q215) binding in other chain
- K206 (= K216) modified: N6-(pyridoxal phosphate)lysine
- Y257 (= Y263) binding
- T260 (= T266) binding
- R356 (= R359) binding
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)
32% identity, 86% coverage: 31:379/407 of query aligns to 19:375/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ P87), G77 (= G88), H78 (≠ S89), W103 (≠ F114), S153 (≠ T164), D178 (= D190), V180 (= V192), Q203 (= Q215), K204 (= K216), Y255 (= Y263), T258 (= T266)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
32% identity, 86% coverage: 31:379/407 of query aligns to 19:375/384 of 6rv0A
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)
32% identity, 86% coverage: 31:379/407 of query aligns to 24:380/392 of P21549
- R36 (≠ A43) 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 (≠ N48) 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 (≠ N53) 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 (= G88) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F114) 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 (≠ M118) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ I156) 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 (≠ T158) 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 (= G162) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T164) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (≠ T167) 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 (= L173) 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 (≠ A177) 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 (≠ A180) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D190) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ T194) 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 (≠ A209) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ T212) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K216) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S225) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R240) 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 (≠ A251) 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 (vs. gap) 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 (≠ V282) to T: in dbSNP:rs140992177
- A280 (≠ C283) to V: in dbSNP:rs73106685
- V326 (= V328) to I: in dbSNP:rs115057148
- I340 (≠ S342) 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
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
32% identity, 86% coverage: 31:379/407 of query aligns to 21:377/387 of 1j04A
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
31% identity, 90% coverage: 13:379/407 of query aligns to 4:373/383 of 3kgxA
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)
33% identity, 84% coverage: 24:365/407 of query aligns to 15:362/396 of Q7PRG3
- SAH 77:79 (≠ PGS 87:89) binding in other chain
- S154 (≠ T164) binding in other chain
- Q204 (= Q215) binding in other chain
- K205 (= K216) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y263) binding
- T259 (= T266) binding
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
33% identity, 84% coverage: 24:365/407 of query aligns to 13:360/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G36), S41 (≠ N53), N42 (≠ H54), S152 (≠ T164), Y254 (= Y263), Q342 (≠ S350), L345 (≠ F353), R354 (= R359)
- binding pyridoxal-5'-phosphate: S75 (≠ P87), A76 (≠ G88), H77 (≠ S89), W102 (≠ F114), S152 (≠ T164), D177 (= D190), V179 (= V192), K203 (= K216), Y254 (= Y263), T257 (= T266)
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
33% identity, 84% coverage: 24:365/407 of query aligns to 14:361/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ P87), A77 (≠ G88), H78 (≠ S89), W103 (≠ F114), S153 (≠ T164), D178 (= D190), V180 (= V192), Q203 (= Q215), K204 (= K216), Y255 (= Y263), T258 (= T266)
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
31% identity, 90% coverage: 13:379/407 of query aligns to 8:378/388 of 3kgwB
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
33% identity, 86% coverage: 32:379/407 of query aligns to 10:361/387 of 3islA
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
31% identity, 86% coverage: 31:379/407 of query aligns to 21:375/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (≠ A35), G26 (= G36), L346 (≠ F353), R355 (= R359)
- binding pyridoxal-5'-phosphate: S78 (≠ P87), G79 (= G88), H80 (≠ S89), W105 (≠ F114), S153 (≠ T164), D178 (= D190), V180 (= V192), K204 (= K216)
Sites not aligning to the query:
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
31% identity, 88% coverage: 24:383/407 of query aligns to 15:380/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ P87), A78 (≠ G88), H79 (≠ S89), W104 (≠ F114), S154 (≠ T164), D179 (= D190), V181 (= V192), Q204 (= Q215), K205 (= K216), Y256 (= Y263), T259 (= T266)
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)
30% identity, 88% coverage: 24:383/407 of query aligns to 15:380/400 of Q0IG34
- SAH 77:79 (≠ PGS 87:89) binding in other chain
- S154 (≠ T164) binding in other chain
- Q204 (= Q215) binding in other chain
- K205 (= K216) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y263) binding
- T259 (= T266) binding
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)
32% identity, 86% coverage: 32:379/407 of query aligns to 14:383/416 of O32148
- Q37 (≠ H54) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K216) modified: N6-(pyridoxal phosphate)lysine
- N264 (vs. gap) 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
34% identity, 87% coverage: 30:383/407 of query aligns to 1:350/352 of 2yrrA
Query Sequence
>H281DRAFT_04750 FitnessBrowser__Burk376:H281DRAFT_04750
MPTSSSNVASTAVPCPVVESLDAILPEEPLLMMGAGPVPIPAAVAKANTIVINHLGATMV
KVIGQVKTMARYVFQTNSKWVLGVAGPGSAAMEMAISNLAWEGTRVLSIKNGFFSGRMAE
MGRRVGARVTELEVADRTVASLDEIAEAIRRERPEIVTVVQGETSNTVWNYQLKDIAALA
KAAGALVIVDAVCTLSTMPLAMDAWGIDAVITGGQKGLSSIPGVSLIAFSDAAWERVKGR
TAPNAHWCLDASLAENFWHNAGYHYTAPVSGVLALHEALRLVCAETLEKRFARHLKCSVA
LQEGVTALGLQLYAPVACRLNSVVGIEVPAGLSPGDVCAHISRQHQVEISGSFGLPIVRI
GQMGEQCREHNLFRTLHALGRTMVDLGVKVDLPAGVAALERGLSEGK
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