SitesBLAST
Comparing 6937743 FitnessBrowser__SB2B:6937743 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)
6rz0A Crystal structure of escherichia coli glyoxalase ii
45% identity, 100% coverage: 2:258/258 of query aligns to 1:251/251 of 6rz0A
- active site: H53 (= H54), H55 (= H56), D57 (= D58), H58 (= H59), H110 (= H115), D127 (= D132), H165 (= H170)
- binding zinc ion: H53 (= H54), H55 (= H56), D57 (= D58), H58 (= H59), H110 (= H115), D127 (= D132), D127 (= D132), H165 (= H170)
Q9SID3 Hydroxyacylglutathione hydrolase 2, mitochondrial; Glyoxalase II; Glx II; EC 3.1.2.6 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
41% identity, 100% coverage: 2:258/258 of query aligns to 71:324/324 of Q9SID3
- H124 (= H54) binding Zn(2+)
- H126 (= H56) binding Zn(2+)
- D128 (= D58) binding Fe cation
- H129 (= H59) binding Fe cation
- H182 (= H115) binding Zn(2+)
- D201 (= D132) binding Fe cation; binding Zn(2+)
- H239 (= H170) binding Fe cation
2q42A Ensemble refinement of the protein crystal structure of glyoxalase ii from arabidopsis thaliana gene at2g31350 (see paper)
41% identity, 100% coverage: 2:258/258 of query aligns to 1:254/254 of 2q42A
- active site: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H112 (= H115), D131 (= D132), H169 (= H170)
- binding fe (iii) ion: H54 (= H54), D58 (= D58), H59 (= H59), D131 (= D132), H169 (= H170)
- binding zinc ion: H54 (= H54), H56 (= H56), H112 (= H115), D131 (= D132)
8ewoA Crystal structure of putative glyoxylase ii from pseudomonas aeruginosa
45% identity, 100% coverage: 1:258/258 of query aligns to 2:259/259 of 8ewoA
2qedA Crystal structure of salmonella thyphimurium lt2 glyoxalase ii (see paper)
42% identity, 100% coverage: 2:258/258 of query aligns to 2:252/252 of 2qedA
- active site: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H111 (= H115), D128 (= D132), H166 (= H170)
- binding fe (iii) ion: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H59 (= H59), H111 (= H115), D128 (= D132), D128 (= D132), H166 (= H170)
Q8ZRM2 Hydroxyacylglutathione hydrolase; Glyoxalase II; Glx II; EC 3.1.2.6 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
42% identity, 100% coverage: 2:258/258 of query aligns to 1:251/251 of Q8ZRM2
- H53 (= H54) binding a divalent metal cation
- H55 (= H56) binding a divalent metal cation
- D57 (= D58) binding a divalent metal cation
- H58 (= H59) binding a divalent metal cation
- H110 (= H115) binding a divalent metal cation
- D127 (= D132) binding a divalent metal cation; binding a divalent metal cation
- H165 (= H170) binding a divalent metal cation
O24496 Hydroxyacylglutathione hydrolase cytoplasmic; Glyoxalase II; Glx II; EC 3.1.2.6 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
38% identity, 91% coverage: 2:237/258 of query aligns to 1:241/258 of O24496
- H54 (= H54) mutation to N: Binds normal amount of metal, but reduced enzyme activity.
- D58 (= D58) mutation to C: Binds normal amount of metal, but reduced enzyme activity.
- C142 (= C139) mutation to A: Increases the metal content and the enzyme activity.
- K144 (≠ R141) mutation to A: Binds normal amount of metal, but reduced enzyme activity.
- N180 (= N176) mutation to A: 70% reduction in enzyme activity.
- R227 (= R223) mutation to A: Decreases metal binding and enzyme stability.
Sites not aligning to the query:
- 250 R→W: Decreases the substrate affinity.
1qh5B Human glyoxalase ii with s-(n-hydroxy-n-bromophenylcarbamoyl) glutathione (see paper)
35% identity, 100% coverage: 2:258/258 of query aligns to 1:255/260 of 1qh5B
- active site: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H110 (= H115), D134 (= D132), H173 (= H170)
- binding s-(n-hydroxy-n-bromophenylcarbamoyl)glutathione: H56 (= H56), H110 (= H115), C141 (= C139), K143 (≠ R141), Y145 (≠ F143), H173 (= H170), Y175 (= Y172), R249 (= R252), K252 (= K255)
- binding zinc ion: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H110 (= H115), D134 (= D132), D134 (= D132), H173 (= H170)
1qh5A Human glyoxalase ii with s-(n-hydroxy-n-bromophenylcarbamoyl) glutathione (see paper)
35% identity, 100% coverage: 2:258/258 of query aligns to 1:255/260 of 1qh5A
- active site: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H110 (= H115), D134 (= D132), H173 (= H170)
- binding glutathione: D134 (= D132), C141 (= C139), K143 (≠ R141), H173 (= H170), Y175 (= Y172), R249 (= R252), K252 (= K255)
- binding zinc ion: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H110 (= H115), D134 (= D132), D134 (= D132), H173 (= H170)
1qh3A Human glyoxalase ii with cacodylate and acetate ions present in the active site (see paper)
35% identity, 100% coverage: 2:258/258 of query aligns to 1:255/260 of 1qh3A
- active site: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H110 (= H115), D134 (= D132), H173 (= H170)
- binding acetate ion: C141 (= C139), Y175 (= Y172), R249 (= R252), K252 (= K255)
- binding cacodylate ion: H56 (= H56), H110 (= H115), D134 (= D132), Y145 (≠ F143), H173 (= H170)
- binding manganese (ii) ion: H185 (≠ A182), H235 (≠ Q236), E251 (≠ W254)
- binding zinc ion: H54 (= H54), H56 (= H56), D58 (= D58), H59 (= H59), H110 (= H115), D134 (= D132), D134 (= D132), H173 (= H170)
Q16775 Hydroxyacylglutathione hydrolase, mitochondrial; Glyoxalase II; Glx II; EC 3.1.2.6 from Homo sapiens (Human) (see paper)
35% identity, 100% coverage: 2:258/258 of query aligns to 49:303/308 of Q16775
- H102 (= H54) binding Zn(2+)
- H104 (= H56) binding Zn(2+)
- D106 (= D58) binding Zn(2+)
- H107 (= H59) binding Zn(2+)
- H158 (= H115) binding Zn(2+)
- D182 (= D132) binding Zn(2+); binding Zn(2+)
- KFY 191:193 (≠ RLF 141:143) binding substrate
- H221 (= H170) binding Zn(2+)
- HEY 221:223 (= HEY 170:172) binding substrate
- RREK 297:300 (≠ RRWK 252:255) binding substrate
2p18A Crystal structure of the leishmania infantum glyoxalase ii (see paper)
28% identity, 86% coverage: 2:224/258 of query aligns to 13:259/283 of 2p18A
- active site: H68 (= H54), H70 (= H56), D72 (= D58), H73 (= H59), H129 (= H115), D154 (= D132), H200 (= H170)
- binding spermidine: I161 (≠ C139), Y202 (= Y172)
- binding zinc ion: H68 (= H54), H70 (= H56), D72 (= D58), H73 (= H59), H129 (= H115), D154 (= D132), D154 (= D132), H200 (= H170)
4ysbA Crystal structure of ethe1 from myxococcus xanthus (see paper)
38% identity, 57% coverage: 25:172/258 of query aligns to 26:172/225 of 4ysbA
Q9C8L4 Persulfide dioxygenase ETHE1 homolog, mitochondrial; Glyoxalase II; Glx II; Sulfur dioxygenase ETHE1; EC 1.13.11.18 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 59% coverage: 21:172/258 of query aligns to 75:234/294 of Q9C8L4
- H110 (= H54) binding Fe cation
- H166 (= H115) binding Fe cation
- D191 (= D132) binding Fe cation
7l0bA Crystal structure of hydroxyacyl glutathione hydrolase (glob) from staphylococcus aureus, apoenzyme (see paper)
30% identity, 58% coverage: 22:170/258 of query aligns to 22:185/202 of 7l0bA
2gcuA X-ray structure of gene product from arabidopsis thaliana at1g53580 (see paper)
32% identity, 59% coverage: 21:172/258 of query aligns to 26:185/244 of 2gcuA
3tp9A Crystal structure of alicyclobacillus acidocaldarius protein with beta-lactamase and rhodanese domains
31% identity, 57% coverage: 23:170/258 of query aligns to 26:198/473 of 3tp9A
4ad9A Crystal structure of human lactb2. (see paper)
31% identity, 59% coverage: 26:176/258 of query aligns to 43:205/288 of 4ad9A
Q53H82 Endoribonuclease LACTB2; Beta-lactamase-like protein 2; EC 3.1.27.- from Homo sapiens (Human) (see paper)
31% identity, 59% coverage: 26:176/258 of query aligns to 43:205/288 of Q53H82
- HWHRDH 77:82 (≠ HHHRDH 54:59) mutation Missing: Loss of endoribonuclease activity.
- D81 (= D58) mutation to A: Loss of endoribonuclease activity.
- R110 (≠ S76) mutation to A: Mildly decreases endoribonuclease activity. No effect on RNA-binding.
- N116 (≠ A82) mutation to A: Loss of endoribonuclease activity. No effect on RNA-binding.
- E118 (≠ T84) mutation to A: Loss of endoribonuclease activity. No effect on RNA-binding.
- D164 (= D132) mutation to A: Loss of endoribonuclease activity.
Sites not aligning to the query:
- 216:217 HR→AT: Loss of endoribonuclease activity. Strongly decreases RNA-binding.
- 220 R→T: Loss of endoribonuclease activity. Strongly decreases RNA-binding.
O95571 Persulfide dioxygenase ETHE1, mitochondrial; Ethylmalonic encephalopathy protein 1; Hepatoma subtracted clone one protein; Sulfur dioxygenase ETHE1; EC 1.13.11.18 from Homo sapiens (Human) (see 4 papers)
30% identity, 68% coverage: 25:200/258 of query aligns to 48:229/254 of O95571