SitesBLAST
Comparing WP_012282232.1 NCBI__GCF_000019165.1:WP_012282232.1 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)
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
37% identity, 99% coverage: 4:387/387 of query aligns to 8:396/400 of 6pk3B
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)
37% identity, 99% coverage: 4:387/387 of query aligns to 9:397/401 of Q56YA5
- TGT 68:70 (≠ SGT 62:64) binding
- T148 (= T142) binding
- QK 200:201 (= QK 192:193) binding
- K201 (= K193) binding
- P251 (= P242) mutation to L: Abolishes aminotransferase activity.
- R347 (= R337) binding
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
37% identity, 99% coverage: 4:387/387 of query aligns to 7:395/399 of 6pk1A
2dr1A Crystal structure of the ph1308 protein from pyrococcus horikoshii ot3
35% identity, 92% coverage: 7:363/387 of query aligns to 19:375/381 of 2dr1A
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
33% identity, 96% coverage: 7:379/387 of query aligns to 10:384/387 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)
32% identity, 96% coverage: 7:379/387 of query aligns to 14:406/416 of O32148
- Q37 (≠ H30) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K193) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ T238) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
Q988B8 Pyridoxamine--pyruvate transaminase; Pyridoxamine-pyruvate aminotransferase; EC 2.6.1.30 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see 2 papers)
31% identity, 96% coverage: 11:380/387 of query aligns to 17:389/393 of Q988B8
- E68 (≠ S62) binding ; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
- Y95 (≠ F89) binding
- T146 (= T142) binding
- K197 (= K193) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
- C198 (≠ G194) mutation to A: No effect on enzyme activity.
- R336 (≠ Q328) mutation to A: Strongly decreased affinity for pyruvate.
- R345 (= R337) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
2z9xA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxyl-l-alanine (see paper)
31% identity, 96% coverage: 11:380/387 of query aligns to 16:388/392 of 2z9xA
2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
31% identity, 96% coverage: 11:380/387 of query aligns to 16:388/392 of 2z9wA
2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
31% identity, 96% coverage: 11:380/387 of query aligns to 16:388/392 of 2z9vA
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
32% identity, 87% coverage: 7:342/387 of query aligns to 22:361/393 of Q3LSM4
- SGH 78:80 (≠ SGT 62:64) binding in other chain
- S155 (≠ T142) binding ; binding
- Q205 (= Q192) binding in other chain
- K206 (= K193) modified: N6-(pyridoxal phosphate)lysine
- Y257 (vs. gap) binding
- T260 (= T241) binding
- R356 (= R337) binding
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
32% identity, 87% coverage: 7:342/387 of query aligns to 22:361/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
32% identity, 87% coverage: 7:342/387 of query aligns to 22:361/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
32% identity, 87% coverage: 7:342/387 of query aligns to 22:361/385 of 2hufA
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
31% identity, 92% coverage: 7:361/387 of query aligns to 21:377/377 of 1vjoA
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
32% identity, 87% coverage: 7:343/387 of query aligns to 21:359/383 of 3kgxA
Sites not aligning to the query:
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
32% identity, 87% coverage: 7:343/387 of query aligns to 25:364/388 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)
33% identity, 88% coverage: 4:342/387 of query aligns to 22:365/392 of P21549
- R36 (= R18) to C: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ L23) 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 (≠ N29) 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 (= G63) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F89) 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 (≠ F93) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (= L136) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (vs. gap) 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 (≠ N140) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T142) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (= G145) 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 (= L150) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (≠ S154) 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 (≠ R157) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D167) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ G171) 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 (≠ V186) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ T189) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K193) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ A202) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ K216) 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 (≠ F257) to T: in dbSNP:rs140992177
- A280 (≠ R258) to V: in dbSNP:rs73106685
- V326 (≠ A303) to I: in dbSNP:rs115057148
- I340 (≠ R317) 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)
33% identity, 88% coverage: 4:342/387 of query aligns to 17:360/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (= S62), G77 (= G63), H78 (≠ T64), W103 (≠ F89), S153 (≠ T142), D178 (= D167), V180 (= V169), Q203 (= Q192), K204 (= K193), Y255 (vs. gap), T258 (≠ V240)
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
33% identity, 88% coverage: 4:342/387 of query aligns to 19:362/387 of 1j04A
Query Sequence
>WP_012282232.1 NCBI__GCF_000019165.1:WP_012282232.1
MFEKEYLMLPGPTPVPPRLLRALSEPLINHRGPSFKRLIDEVTEGIRYAYQTKNDVLILP
SSGTGGMEAAIVNFLSPGDKVLALSIGAFGDRFATIAQTYGCIVDKVDFEWGTAVDLNVV
KAKLAADVNKEYKAILVTHNETSTGVCNDLKGLSEIRGDHPALILVDSVSGLGVMEVKTD
EWGLDVIVTAAQKGFMIPPGVAFVSVSPRAWAAYEKSTAPKFYWDLGSAKKFLEKGQTPV
TPAIPQLTGLREALQLFREKGREAVFAKQRYLRDITRAGVKALGLKLLADDAVASAAVTA
VWAPEGIEAKAINKRMREAHNVVLAGGQKKLENKIFRIGHLGYGQHLDVLATVAALEMTL
KELGYPVELGAGVKAAQEVIMSRKGLL
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