SitesBLAST
Comparing WP_083818485.1 NCBI__GCF_000223395.1:WP_083818485.1 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)
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
37% identity, 99% coverage: 5:365/366 of query aligns to 19:377/381 of 2dr1A
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
33% identity, 93% coverage: 4:342/366 of query aligns to 20:357/377 of 1vjoA
Q56YA5 Serine--glyoxylate aminotransferase; Alanine--glyoxylate aminotransferase; AGT; Asparagine aminotransferase; Serine--pyruvate aminotransferase; EC 2.6.1.45; EC 2.6.1.44; EC 2.6.1.-; EC 2.6.1.51 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
33% identity, 93% coverage: 5:345/366 of query aligns to 12:355/401 of Q56YA5
- TGT 68:70 (≠ SGT 61:63) binding pyridoxal 5'-phosphate
- T148 (= T138) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 189:190) binding pyridoxal 5'-phosphate
- K201 (= K190) binding 3-hydroxypyruvate
- P251 (= P242) mutation to L: Abolishes aminotransferase activity.
- R347 (= R337) binding 3-hydroxypyruvate
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
33% identity, 93% coverage: 5:345/366 of query aligns to 11:354/400 of 6pk3B
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
33% identity, 93% coverage: 5:345/366 of query aligns to 10:353/399 of 6pk1A
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
33% identity, 98% coverage: 5:363/366 of query aligns to 3:347/348 of 1iugA
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
29% identity, 99% coverage: 2:365/366 of query aligns to 22:387/388 of 3kgwB
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)
29% identity, 98% coverage: 2:358/366 of query aligns to 17:380/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S61), G77 (= G62), H78 (≠ T63), W103 (≠ F88), S153 (≠ T138), D178 (= D164), V180 (= V166), Q203 (= Q189), K204 (= K190), Y255 (vs. gap), T258 (= T241)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
29% identity, 98% coverage: 2:358/366 of query aligns to 17:380/384 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)
29% identity, 98% coverage: 2:358/366 of query aligns to 22:385/392 of P21549
- R36 (= R16) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ L21) 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 (≠ S27) 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 (= G62) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F88) 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 (= A92) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ A130) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (= F132) 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 (≠ N136) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T138) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G141) 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 (= L147) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ A151) 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 (≠ V154) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D164) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ G168) 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 (≠ V183) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ T186) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K190) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ G199) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ S215) 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 (≠ L226) 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 (≠ K235) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (= I257) to T: in dbSNP:rs140992177
- A280 (≠ E258) to V: in dbSNP:rs73106685
- V326 (≠ L304) to I: in dbSNP:rs115057148
- I340 (≠ A318) 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
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
29% identity, 99% coverage: 2:365/366 of query aligns to 18:382/383 of 3kgxA
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
29% identity, 93% coverage: 4:342/366 of query aligns to 20:361/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (= S61), A78 (≠ G62), H79 (≠ T63), W104 (≠ F88), S154 (≠ T138), D179 (= D164), V181 (= V166), Q204 (= Q189), K205 (= K190), Y256 (≠ T238), T259 (= T241)
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
28% identity, 92% coverage: 5:342/366 of query aligns to 10:346/387 of 3islA
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
29% identity, 98% coverage: 2:358/366 of query aligns to 19:382/387 of 1j04A
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)
29% identity, 93% coverage: 4:342/366 of query aligns to 20:361/396 of Q7PRG3
- SAH 77:79 (≠ SGT 61:63) binding in other chain
- S154 (≠ T138) binding in other chain
- Q204 (= Q189) binding in other chain
- K205 (= K190) modified: N6-(pyridoxal phosphate)lysine
- Y256 (vs. gap) binding pyridoxal 5'-phosphate
- T259 (= T241) binding pyridoxal 5'-phosphate
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
29% identity, 93% coverage: 4:342/366 of query aligns to 18:359/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G9), S41 (= S27), N42 (≠ H28), S152 (≠ T138), Y254 (vs. gap), Q342 (≠ A325), L345 (≠ M328), R354 (= R337)
- binding pyridoxal-5'-phosphate: S75 (= S61), A76 (≠ G62), H77 (≠ T63), W102 (≠ F88), S152 (≠ T138), D177 (= D164), V179 (= V166), K203 (= K190), Y254 (vs. gap), T257 (= T241)
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
29% identity, 93% coverage: 4:342/366 of query aligns to 19:360/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (= S61), A77 (≠ G62), H78 (≠ T63), W103 (≠ F88), S153 (≠ T138), D178 (= D164), V180 (= V166), Q203 (= Q189), K204 (= K190), Y255 (vs. gap), T258 (= T241)
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
29% identity, 98% coverage: 2:358/366 of query aligns to 19:380/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P8), G26 (= G9), L346 (≠ M328), R355 (= R337)
- binding pyridoxal-5'-phosphate: S78 (= S61), G79 (= G62), H80 (≠ T63), W105 (≠ F88), S153 (≠ T138), D178 (= D164), V180 (= V166), K204 (= K190)
Sites not aligning to the query:
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)
29% identity, 93% coverage: 4:342/366 of query aligns to 20:361/400 of Q0IG34
- SAH 77:79 (≠ SGT 61:63) binding in other chain
- S154 (≠ T138) binding in other chain
- Q204 (= Q189) binding in other chain
- K205 (= K190) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ T238) binding pyridoxal 5'-phosphate
- T259 (= T241) binding pyridoxal 5'-phosphate
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)
28% identity, 92% coverage: 5:342/366 of query aligns to 14:368/416 of O32148
- Q37 (≠ H28) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K190) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ T238) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
Query Sequence
>WP_083818485.1 NCBI__GCF_000223395.1:WP_083818485.1
MTMVLLTPGPVEIHERVLKALSEGIASHRSETYRNWHCEAVERLKRISGLRDGSVYLIPG
SGTTAVDAMIYSVLAPGEKVLAYIVGEFGRRAVNTMKARGLNVRLLEEPWGKAIRIERLK
EALEEDSYDAVFIVHNETSTGVANRTLREAAELVHKHGAILLVDSVSGFAGERLYMDDWG
VDVVATATQKCLAAPPGLGIVMVKSDVVERIEKVSKESPPPPSINLSLYEKFLAKCETPF
TPPVNVVRALVEALRLIEEEGGIEARYREQEMRASRFYSVIDAAGLDTLAEKSARSYTVA
AVRLPEGVRAPEVKKRMAELGFEIAGGMGEYREKVVRVGLMGAINADIVEAAARSLVEII
QELSRG
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