SitesBLAST
Comparing WP_028488718.1 NCBI__GCF_000621325.1:WP_028488718.1 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)
33% identity, 90% coverage: 20:377/400 of query aligns to 12:377/377 of 1vjoA
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
31% identity, 94% coverage: 3:379/400 of query aligns to 2:383/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ P79), A78 (≠ G80), H79 (≠ S81), W104 (≠ F106), S154 (≠ T156), D179 (= D182), V181 (= V184), Q204 (= Q207), K205 (= K208), Y256 (= Y256), T259 (= T259)
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)
32% identity, 94% coverage: 3:379/400 of query aligns to 2:383/396 of Q7PRG3
- SAH 77:79 (≠ PGS 79:81) binding in other chain
- S154 (≠ T156) binding in other chain
- Q204 (= Q207) binding in other chain
- K205 (= K208) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y256) binding
- T259 (= T259) binding
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
32% identity, 94% coverage: 3:379/400 of query aligns to 1:382/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ P79), A77 (≠ G80), H78 (≠ S81), W103 (≠ F106), S153 (≠ T156), D178 (= D182), V180 (= V184), Q203 (= Q207), K204 (= K208), Y255 (= Y256), T258 (= T259)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
32% identity, 94% coverage: 4:379/400 of query aligns to 1:381/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G28), S41 (≠ N45), N42 (≠ H46), S152 (≠ T156), Y254 (= Y256), Q342 (≠ S343), L345 (≠ F346), R354 (= R352)
- binding pyridoxal-5'-phosphate: S75 (≠ P79), A76 (≠ G80), H77 (≠ S81), W102 (≠ F106), S152 (≠ T156), D177 (= D182), V179 (= V184), K203 (= K208), Y254 (= Y256), T257 (= T259)
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)
31% identity, 94% coverage: 3:379/400 of query aligns to 2:383/400 of Q0IG34
- SAH 77:79 (≠ PGS 79:81) binding in other chain
- S154 (≠ T156) binding in other chain
- Q204 (= Q207) binding in other chain
- K205 (= K208) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y256) binding
- T259 (= T259) binding
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
32% identity, 94% coverage: 4:377/400 of query aligns to 7:383/388 of 3kgwB
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
32% identity, 94% coverage: 4:377/400 of query aligns to 3:378/383 of 3kgxA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
29% identity, 97% coverage: 1:389/400 of query aligns to 1:393/393 of Q3LSM4
- SGH 78:80 (≠ PGS 79:81) binding in other chain
- S155 (≠ T156) binding ; binding
- Q205 (= Q207) binding in other chain
- K206 (= K208) modified: N6-(pyridoxal phosphate)lysine
- Y257 (= Y256) binding
- T260 (= T259) binding
- R356 (= R352) binding
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
29% identity, 95% coverage: 1:378/400 of query aligns to 1:382/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
29% identity, 95% coverage: 1:378/400 of query aligns to 1:382/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
29% identity, 95% coverage: 1:378/400 of query aligns to 1:382/385 of 2hufA
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
30% identity, 94% coverage: 4:377/400 of query aligns to 2:380/384 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, 94% coverage: 4:377/400 of query aligns to 2:380/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ P79), G77 (= G80), H78 (≠ S81), W103 (≠ F106), S153 (≠ T156), D178 (= D182), V180 (= V184), Q203 (= Q207), K204 (= K208), Y255 (= Y256), T258 (= T259)
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, 94% coverage: 4:377/400 of query aligns to 7:385/392 of P21549
- T9 (≠ P6) to N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
- P11 (= P8) to 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
- R36 (≠ K35) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ N40) 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 (≠ N45) 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 (= G80) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F106) 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 (≠ M110) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A148) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ T150) 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 (= G154) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T156) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (≠ T159) 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 (= L165) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ A169) 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 (≠ A172) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D182) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ T186) 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 (≠ A201) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ T204) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K208) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S217) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R233) 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 (≠ A244) 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 (vs. gap) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ V275) to T: in dbSNP:rs140992177
- A280 (≠ C276) to V: in dbSNP:rs73106685
- V326 (= V321) to I: in dbSNP:rs115057148
- I340 (≠ S335) 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
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
30% identity, 94% coverage: 4:377/400 of query aligns to 4:380/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (≠ A27), G26 (= G28), L346 (≠ F346), R355 (= R352)
- binding pyridoxal-5'-phosphate: S78 (≠ P79), G79 (= G80), H80 (≠ S81), W105 (≠ F106), S153 (≠ T156), D178 (= D182), V180 (= V184), K204 (= K208)
Sites not aligning to the query:
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
30% identity, 94% coverage: 4:377/400 of query aligns to 4:382/387 of 1j04A
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
34% identity, 86% coverage: 22:366/400 of query aligns to 1:342/352 of 2yrrA
2yriA Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine
34% identity, 86% coverage: 22:366/400 of query aligns to 1:342/352 of 2yriA
- binding (s,e)-3-hydroxy-2-((3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)methyleneamino)-2-methylpropanoic acid: G7 (= G28), S60 (≠ P79), G61 (= G80), S62 (= S81), F85 (= F106), T135 (= T156), D160 (= D182), V162 (= V184), K186 (= K208), R326 (= R352)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y229 (= Y256), T232 (= T259)
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
29% identity, 87% coverage: 24:372/400 of query aligns to 10:361/387 of 3islA
Query Sequence
>WP_028488718.1 NCBI__GCF_000621325.1:WP_028488718.1
MNELLPPPSIVPLEHILPDEPLLMMGAGPVPIPQKVAAANSIVINHLGETMNRVIEQVKD
MGRYVFQTDSSHVMGVSGPGSAAMEMAVANLVLPGERVLCITNGYFSLRMAEIVRRVRAE
PTILEMPHNESADLALVERALKQGQFHAVTLVQGETSNTVCNKNLDQIAKLAKRYGCLVI
VDAVCTLSTMPLAMDNWQVDAIITGGQKGLSSIPGVSLLAFSESAWSKKIARREELPFHW
CLDAQLADKFWNQKSYHYTAPVSGILALHEALRLVCEETLPQRFERHLRCSEALQAGIET
MGLKMLVEKQHRLNSVVGIIVPDHVSADVVRAHMSKVHKVEISGAFGLNILRIGQMGEQS
RAYNLFRTLHALGSSMRAAGASLDLPAGMAEMERVLSGEG
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