SitesBLAST
Comparing WP_012676496.1 NCBI__GCF_000021565.1:WP_012676496.1 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
35% identity, 92% coverage: 4:352/381 of query aligns to 16:368/381 of 2dr1A
6pk3B Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana (see paper)
34% identity, 97% coverage: 4:373/381 of query aligns to 8:386/400 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)
34% identity, 97% coverage: 4:373/381 of query aligns to 9:387/401 of Q56YA5
- TGT 68:70 (≠ SGT 62:64) binding pyridoxal 5'-phosphate
- T148 (= T140) binding pyridoxal 5'-phosphate
- QK 200:201 (= QK 191:192) binding pyridoxal 5'-phosphate
- K201 (= K192) binding 3-hydroxypyruvate
- P251 (= P241) mutation to L: Abolishes aminotransferase activity.
- R347 (= R333) binding 3-hydroxypyruvate
6pk1A Alanine-glyoxylate aminotransferase 1 (agt1) from arabidopsis thaliana in presence of serine (see paper)
34% identity, 97% coverage: 4:373/381 of query aligns to 7:385/399 of 6pk1A
1iugA The crystal structure of aspartate aminotransferase which belongs to subgroup iv from thermus thermophilus (see paper)
36% identity, 90% coverage: 7:348/381 of query aligns to 3:336/348 of 1iugA
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
33% identity, 97% coverage: 7:375/381 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, 98% coverage: 7:381/381 of query aligns to 14:411/416 of O32148
- Q37 (≠ H30) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K192) modified: N6-(pyridoxal phosphate)lysine
- N264 (≠ T237) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
31% identity, 92% coverage: 7:357/381 of query aligns to 21:377/377 of 1vjoA
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)
26% identity, 97% coverage: 8:376/381 of query aligns to 14:389/393 of Q988B8
- E68 (≠ S62) binding pyridoxal 5'-phosphate; mutation E->A,G: Low but detectable pyridoxamine--pyruvate transaminase activity.
- Y95 (≠ F89) binding pyridoxal 5'-phosphate
- T146 (= T140) binding pyridoxal 5'-phosphate
- K197 (= K192) modified: N6-(pyridoxal phosphate)lysine; mutation to L: Loss of function.
- C198 (≠ A193) mutation to A: No effect on enzyme activity.
- R336 (≠ Q324) mutation to A: Strongly decreased affinity for pyruvate.
- R345 (= R333) binding pyridoxal 5'-phosphate
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)
26% identity, 97% coverage: 8:376/381 of query aligns to 13:388/392 of 2z9xA
2z9wA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxal (see paper)
26% identity, 97% coverage: 8:376/381 of query aligns to 13:388/392 of 2z9wA
2z9vA Crystal structure of pyridoxamine-pyruvate aminotransferase complexed with pyridoxamine (see paper)
26% identity, 97% coverage: 8:376/381 of query aligns to 13:388/392 of 2z9vA
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
31% identity, 87% coverage: 7:338/381 of query aligns to 3:331/352 of 2yrrA
2yriA Crystal structure of alanine-pyruvate aminotransferase with 2- methylserine
31% identity, 87% coverage: 7:338/381 of query aligns to 3:331/352 of 2yriA
- binding (s,e)-3-hydroxy-2-((3-hydroxy-2-methyl-5-(phosphonooxymethyl)pyridin-4-yl)methyleneamino)-2-methylpropanoic acid: G7 (= G11), S60 (≠ T64), G61 (= G65), S62 (≠ A66), F85 (= F89), T135 (= T140), D160 (= D166), V162 (≠ I168), K186 (= K192), R326 (= R333)
- binding 4'-deoxy-4'-aminopyridoxal-5'-phosphate: Y229 (≠ T237), T232 (= T240)
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
29% identity, 88% coverage: 4:338/381 of query aligns to 17:360/384 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, 88% coverage: 4:338/381 of query aligns to 22:365/392 of P21549
- R36 (≠ Q18) 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 (≠ H29) 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 (≠ W93) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (≠ K131) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (= F134) 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 (≠ S138) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T140) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (≠ T143) 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 (≠ V148) to P: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (= G152) 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 (≠ A155) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D166) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (= S170) 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 (≠ V185) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ T188) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K192) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (= S201) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (≠ K215) 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 (≠ V225) 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 (≠ A229) to R: in HP1; associated in cis with L-11 and M-340; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (= I256) to T: in dbSNP:rs140992177
- A280 (≠ L257) to V: in dbSNP:rs73106685
- V326 (≠ S300) to I: in dbSNP:rs115057148
- I340 (≠ L314) 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)
29% identity, 88% coverage: 4:338/381 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 (≠ T140), D178 (= D166), V180 (≠ I168), Q203 (= Q191), K204 (= K192), Y255 (≠ Q236), T258 (≠ Y239)
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
28% identity, 90% coverage: 7:350/381 of query aligns to 21:370/383 of 3kgxA
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
29% identity, 88% coverage: 4:338/381 of query aligns to 19:360/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P10), G26 (= G11), L346 (≠ Q324), R355 (= R333)
- binding pyridoxal-5'-phosphate: S78 (= S62), G79 (= G63), H80 (≠ T64), W105 (≠ F89), S153 (≠ T140), D178 (= D166), V180 (≠ I168), K204 (= K192)
Sites not aligning to the query:
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
29% identity, 88% coverage: 4:338/381 of query aligns to 19:362/387 of 1j04A
Query Sequence
>WP_012676496.1 NCBI__GCF_000021565.1:WP_012676496.1
MFIKERLFTPGPVPLPPQVIKALGQQIIHHRTPEFTQIFLEARENLQKLLKTERDVIMFA
SSGTGAMEASVANFFRKGDRVLIINAGKFGQRWKELASVYQLKIVDYEIEWGKTYDKERI
LQIISEFPDIKGIFVQHSETSTTTYHDVKYLGDIAKKLDDCLLVVDGITSVGVYQVYPEE
LGIDVLVTGSQKALMLPPGLSVLYFSEKAEERASKSDMPRYYFDVLKEAKKQSKGQTAYT
PAINLIIALNESLKLILGEGLDNLEERHRIMAEATREAVKEIGLKLLSESPSNSATGVYS
PAGIDADQLRKELLKLGFRVAGGQDHLKGKIFRIAHMGYFDFMDVVQVIAGLEMALKRIG
YEIEIGKGVRKAQEVILENLG
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