SitesBLAST
Comparing WP_028990417.1 NCBI__GCF_000423825.1:WP_028990417.1 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)
47% identity, 92% coverage: 9:371/394 of query aligns to 17:376/377 of 1vjoA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
43% identity, 96% coverage: 9:387/394 of query aligns to 6:381/387 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)
42% identity, 96% coverage: 9:387/394 of query aligns to 10:403/416 of O32148
- Q37 (≠ H36) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K198) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ Y248) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
41% identity, 92% coverage: 9:371/394 of query aligns to 21:382/388 of 3kgwB
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
41% identity, 92% coverage: 9:371/394 of query aligns to 17:377/383 of 3kgxA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
39% identity, 94% coverage: 9:379/394 of query aligns to 18:388/393 of Q3LSM4
- SGH 78:80 (≠ PGS 69:71) binding in other chain
- S155 (≠ T147) binding ; binding
- Q205 (= Q197) binding in other chain
- K206 (= K198) modified: N6-(pyridoxal phosphate)lysine
- Y257 (= Y248) binding
- T260 (= T251) binding
- R356 (= R347) binding
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
39% identity, 93% coverage: 9:375/394 of query aligns to 18:384/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
39% identity, 93% coverage: 9:375/394 of query aligns to 18:384/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
39% identity, 93% coverage: 9:375/394 of query aligns to 18:384/385 of 2hufA
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
39% identity, 89% coverage: 9:360/394 of query aligns to 18:370/387 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, 89% coverage: 9:360/394 of query aligns to 21:373/392 of P21549
- R36 (= R24) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M29) 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 (= G35) 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 (= G70) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F96) 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 (≠ M100) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (= L139) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ A141) 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 (≠ A145) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T147) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G150) 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 (≠ A155) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ V159) 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 (≠ A162) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D172) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S176) 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 (≠ A191) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (= S194) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K198) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S207) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R222) 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 (≠ L233) 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 (≠ S242) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ L267) to T: in dbSNP:rs140992177
- A280 (≠ Q268) to V: in dbSNP:rs73106685
- V326 (≠ I313) to I: in dbSNP:rs115057148
- I340 (≠ L327) 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, 89% coverage: 9:360/394 of query aligns to 16:368/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ P69), G77 (= G70), H78 (≠ S71), W103 (≠ F96), S153 (≠ T147), D178 (= D172), V180 (= V174), Q203 (= Q197), K204 (= K198), Y255 (= Y248), T258 (= T251)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
39% identity, 89% coverage: 9:360/394 of query aligns to 16:368/384 of 6rv0A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
40% identity, 89% coverage: 9:360/394 of query aligns to 18:368/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P16), G26 (= G17), L346 (= L338), R355 (= R347)
- binding pyridoxal-5'-phosphate: S78 (≠ P69), G79 (= G70), H80 (≠ S71), W105 (≠ F96), S153 (≠ T147), D178 (= D172), V180 (= V174), K204 (= K198)
Sites not aligning to the query:
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
38% identity, 92% coverage: 9:372/394 of query aligns to 15:379/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G17), S41 (≠ G35), N42 (≠ H36), S152 (≠ T147), Y254 (= Y248), Q342 (≠ G335), L345 (= L338), R354 (= R347)
- binding pyridoxal-5'-phosphate: S75 (≠ P69), A76 (≠ G70), H77 (≠ S71), W102 (≠ F96), S152 (≠ T147), D177 (= D172), V179 (= V174), K203 (= K198), Y254 (= Y248), T257 (= T251)
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
38% identity, 92% coverage: 9:372/394 of query aligns to 16:380/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ P69), A77 (≠ G70), H78 (≠ S71), W103 (≠ F96), S153 (≠ T147), D178 (= D172), V180 (= V174), Q203 (= Q197), K204 (= K198), Y255 (= Y248), T258 (= T251)
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)
38% identity, 92% coverage: 9:371/394 of query aligns to 17:380/396 of Q7PRG3
- SAH 77:79 (≠ PGS 69:71) binding in other chain
- S154 (≠ T147) binding in other chain
- Q204 (= Q197) binding in other chain
- K205 (= K198) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y248) binding
- T259 (= T251) binding
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
36% identity, 92% coverage: 9:371/394 of query aligns to 17:380/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ P69), A78 (≠ G70), H79 (≠ S71), W104 (≠ F96), S154 (≠ T147), D179 (= D172), V181 (= V174), Q204 (= Q197), K205 (= K198), Y256 (= Y248), T259 (= T251)
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, 92% coverage: 9:371/394 of query aligns to 17:380/400 of Q0IG34
- SAH 77:79 (≠ PGS 69:71) binding in other chain
- S154 (≠ T147) binding in other chain
- Q204 (= Q197) binding in other chain
- K205 (= K198) modified: N6-(pyridoxal phosphate)lysine
- Y256 (= Y248) binding
- T259 (= T251) binding
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
32% identity, 98% coverage: 4:391/394 of query aligns to 2:389/400 of 6pk3B
Query Sequence
>WP_028990417.1 NCBI__GCF_000423825.1:WP_028990417.1
MRTHSFHPPVRTLMGPGPSDVNPRVLEAMSRPTIGHLDPVFVDMMEELKSLLQYAFQTGN
QLTMPVSGPGSAGMETCFVNLVEPGDKVIVCQNGVFGGRMKENVERCGGTAVMVEDAWGS
AVDPQKLKDALQAHPDAKLVAFVHAETSTGAQSDAKALVEIAHRHDCLVIVDTVTSLGGT
PVKVDEWGIDAVYSGTQKCLSCTPGLSPVSFSERAMERIKHRKTKVQSWFMDLNLVMGYW
GSGAKRAYHHTAPINALYGLHEALVILQEEGLENAWARHAHAHRALLAGIEAMGLKFVVK
EDERLPQLNAVGIPEGVDDAAVRAQLLQDYNLEIGAGLGPMAGKIWRIGLMGYGANPKNV
LFCLGALEDVLSRMRAPIERGAALPAAHAALGAA
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