SitesBLAST
Comparing CCNA_02687 FitnessBrowser__Caulo:CCNA_02687 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)
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)
53% identity, 94% coverage: 26:425/426 of query aligns to 6:407/416 of O32148
- Q37 (= Q57) mutation to H: 5-fold decrease in transamination activity.
- K198 (= K218) modified: N6-(pyridoxal phosphate)lysine
- N264 (= N282) mutation to S: 9-fold decrease in transamination activity.; mutation to Y: Loss of transamination activity.
3islA Crystal structure of ureidoglycine-glyoxylate aminotransferase (pucg) from bacillus subtilis
52% identity, 94% coverage: 26:425/426 of query aligns to 2:385/387 of 3islA
1vjoA Crystal structure of alanine--glyoxylate aminotransferase (alr1004) from nostoc sp. At 1.70 a resolution (see paper)
37% identity, 89% coverage: 27:406/426 of query aligns to 14:377/377 of 1vjoA
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)
35% identity, 90% coverage: 25:406/426 of query aligns to 12:381/396 of Q7PRG3
- SAH 77:79 (≠ TSR 90:92) binding in other chain
- S154 (≠ T167) binding in other chain
- Q204 (= Q217) binding in other chain
- K205 (= K218) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ N282) binding
- T259 (= T285) binding
2ch1A Structure of anopheles gambiae 3-hydroxykynurenine transaminase (see paper)
35% identity, 90% coverage: 25:406/426 of query aligns to 11:380/388 of 2ch1A
- binding pyridoxal-5'-phosphate: S76 (≠ T90), A77 (≠ S91), H78 (≠ R92), W103 (≠ F117), S153 (≠ T167), D178 (= D192), V180 (≠ T194), Q203 (= Q217), K204 (= K218), Y255 (≠ N282), T258 (= T285)
2ch2A Structure of the anopheles gambiae 3-hydroxykynurenine transaminase in complex with inhibitor (see paper)
35% identity, 90% coverage: 25:406/426 of query aligns to 10:379/387 of 2ch2A
- binding 4-(2-aminophenyl)-4-oxobutanoic acid: G23 (= G38), S41 (≠ G56), N42 (≠ Q57), S152 (≠ T167), Y254 (≠ N282), Q342 (≠ G369), L345 (≠ F372), R354 (= R381)
- binding pyridoxal-5'-phosphate: S75 (≠ T90), A76 (≠ S91), H77 (≠ R92), W102 (≠ F117), S152 (≠ T167), D177 (= D192), V179 (≠ T194), K203 (= K218), Y254 (≠ N282), T257 (= T285)
Q3LSM4 Alanine--glyoxylate aminotransferase; EC 2.6.1.44 from Aedes aegypti (Yellowfever mosquito) (Culex aegypti) (see paper)
34% identity, 88% coverage: 30:402/426 of query aligns to 18:377/393 of Q3LSM4
- SGH 78:80 (≠ TSR 90:92) binding in other chain
- S155 (≠ T167) binding ; binding
- Q205 (= Q217) binding in other chain
- K206 (= K218) modified: N6-(pyridoxal phosphate)lysine
- Y257 (≠ N282) binding
- T260 (= T285) binding
- R356 (= R381) binding
2huuA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with alanine (see paper)
34% identity, 88% coverage: 30:402/426 of query aligns to 18:377/385 of 2huuA
2huiA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase in complex with glyoxylic acid (see paper)
34% identity, 88% coverage: 30:402/426 of query aligns to 18:377/385 of 2huiA
2hufA Crystal structure of aedes aegypti alanine glyoxylate aminotransferase (see paper)
34% identity, 88% coverage: 30:402/426 of query aligns to 18:377/385 of 2hufA
6mfbD Crystal structure of 3-hydroxykynurenine transaminase from aedes aegypti
35% identity, 88% coverage: 30:406/426 of query aligns to 17:381/386 of 6mfbD
- binding pyridoxal-5'-phosphate: S77 (≠ T90), A78 (≠ S91), H79 (≠ R92), W104 (≠ F117), S154 (≠ T167), D179 (= D192), V181 (≠ T194), Q204 (= Q217), K205 (= K218), Y256 (≠ N282), T259 (= T285)
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, 90% coverage: 24:406/426 of query aligns to 15:385/392 of P21549
- R36 (= R45) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177157
- G41 (≠ M50) to E: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177168; to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; 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 (= G56) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; 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 (≠ S91) to E: in HP1; abolishes alanine--glyoxylate aminotransferase activity by interfering with pyridoxal phosphate binding; dbSNP:rs121908522
- W108 (≠ F117) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs180177197
- A112 (≠ L121) to D: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs796052061
- L150 (= L159) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177222
- F152 (≠ A161) to I: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in protein destabilization; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; mitochondrial mistargeting; dbSNP:rs121908524
- G156 (= G165) to R: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; dbSNP:rs121908530
- S158 (≠ T167) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177225
- G161 (≠ T170) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; 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; when associated with L-11 and M-340 on the minor AGXT allele; 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 (= L175) to P: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177230
- G170 (= G179) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in mitochondrial mistargeting; slight 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; dbSNP:rs121908529
- C173 (= C182) to Y: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; decreased protein stability; causes protein aggregation; dbSNP:rs180177231
- D183 (= D192) to N: in HP1; loss of alanine--glyoxylate aminotransferase activity; no loss of dimerization; no effect on protein stability; dbSNP:rs180177236
- S187 (≠ T196) 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 (= I211) to N: in HP1; uncertain significance; dbSNP:rs536352238
- S205 (≠ A214) to P: in HP1; loss of alanine--glyoxylate aminotransferase activity; decreased protein stability; dbSNP:rs121908520
- K209 (= K218) mutation to R: Affects pyridoxal phosphate binding; loss of alanine--glyoxylate aminotransferase activity.
- S218 (≠ A227) to L: in HP1; loss of alanine--glyoxylate aminotransferase activity; loss of dimerization; no effect on protein stability; dbSNP:rs180177253
- R233 (= R242) to C: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908526; to H: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs121908527
- I244 (≠ L269) to T: in HP1; prevalent mutation in the Canary islands; when associated with L-11 and M-340 on the minor AGXT allele; results in protein misfolding; decreased alanine--glyoxylate aminotransferase activity; no loss of dimerization; partial mitochondrial mistargeting; dbSNP:rs121908525
- C253 (vs. gap) to R: in HP1; when associated with L-11 and M-340 on the minor AGXT allele; results in loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs180177264
- I279 (≠ V301) to T: in dbSNP:rs140992177
- A280 (≠ L302) to V: in dbSNP:rs73106685
- V326 (= V347) to I: in dbSNP:rs115057148
- I340 (≠ R361) to M: associated with hyperoxaluria; dbSNP:rs4426527
Sites not aligning to the query:
- 9 T → N: no loss of alanine--glyoxylate aminotransferase activity; dbSNP:rs115014558
- 11 P → L: reduction of specific alanine--glyoxylate aminotransferase activity in vitro; causes mitochondrial mistargeting when associated with R-170; dbSNP:rs34116584
6rv0A Human alanine:glyoxylate aminotransferase major allele (agt-ma); with pmp in the active site (see paper)
33% identity, 90% coverage: 24:406/426 of query aligns to 10:380/384 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)
33% identity, 90% coverage: 24:406/426 of query aligns to 10:380/385 of 5hhyA
- binding (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate: S76 (≠ T90), G77 (≠ S91), H78 (≠ R92), W103 (≠ F117), S153 (≠ T167), D178 (= D192), V180 (≠ T194), Q203 (= Q217), K204 (= K218), Y255 (≠ N282), T258 (= T285)
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)
35% identity, 88% coverage: 30:406/426 of query aligns to 17:381/400 of Q0IG34
- SAH 77:79 (≠ TSR 90:92) binding in other chain
- S154 (≠ T167) binding in other chain
- Q204 (= Q217) binding in other chain
- K205 (= K218) modified: N6-(pyridoxal phosphate)lysine
- Y256 (≠ N282) binding
- T259 (= T285) binding
1j04A Structural mechanism of enzyme mistargeting in hereditary kidney stone disease in vitro (see paper)
33% identity, 90% coverage: 24:406/426 of query aligns to 12:382/387 of 1j04A
1h0cA The crystal structure of human alanine:glyoxylate aminotransferase (see paper)
33% identity, 90% coverage: 24:406/426 of query aligns to 12:380/385 of 1h0cA
- binding (aminooxy)acetic acid: P25 (= P37), G26 (= G38), L346 (≠ F372), R355 (= R381)
- binding pyridoxal-5'-phosphate: S78 (≠ T90), G79 (≠ S91), H80 (≠ R92), W105 (≠ F117), S153 (≠ T167), D178 (= D192), V180 (≠ T194), K204 (= K218)
Sites not aligning to the query:
3kgwB Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.65 a resolution
32% identity, 89% coverage: 27:406/426 of query aligns to 18:383/388 of 3kgwB
3kgxA Crystal structure of putative aminotransferase (aah25799.1) from mus musculus at 1.80 a resolution
32% identity, 89% coverage: 27:406/426 of query aligns to 14:378/383 of 3kgxA
2yrrA Hypothetical alanine aminotransferase (tth0173) from thermus thermophilus hb8
32% identity, 88% coverage: 33:405/426 of query aligns to 2:350/352 of 2yrrA
Query Sequence
>CCNA_02687 FitnessBrowser__Caulo:CCNA_02687
MRAAGGPRRTHSDHRQDHAMTDTFNELDHPARLLMGPGPINVHPRVLRAMSVQLLGQFDP
EFTGYMNEVMALYRGVFQTQNRWTFTIDGTSRAGIEAALVSTLQPGDDVVVVNAGRFGLL
LAEIAERCDAKVTFVEASWGAVVDPQAVEDAVKRVKPRLVACVHGDTSTTMAQPLGEIGA
ICRAHGALMYVDATATLSGMDVPVDAWGADIVTAGLQKCLGGPSGSAPITISDQAAEHIF
SRRHVEKGLAGTGGAAGAGRRIASNYFDLAMIMDYWSEKRLNHHTECAPMLFAARECARL
VLEEGLPARFDRHAQAGAAMTAGLEAMGLSIYGDKAHKMTNVTGIWVPKGVDYDRVKARM
RTDFEIEIGSAFGPLTGKIWRIGTMGVNARKHAVLQTLAAFEAVLRWEGFSAPAGAGVDA
AAKVYG
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