SitesBLAST
Comparing 3608903 Dshi_2294 Pyrrolo-quinoline quinone (RefSeq) 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)
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
27% identity, 79% coverage: 143:749/769 of query aligns to 20:540/670 of 1kb0A
- active site: E185 (≠ V334), N263 (= N398), D308 (= D442)
- binding calcium ion: E185 (≠ V334), N263 (= N398), D308 (= D442)
- binding heme c: F113 (≠ W239), Q435 (= Q619)
- binding pyrroloquinoline quinone: E70 (≠ Q197), C116 (= C242), C117 (vs. gap), R122 (= R243), T167 (= T312), G182 (= G331), G183 (≠ M332), A184 (= A333), E185 (≠ V334), T243 (≠ N378), W245 (= W380), N263 (= N398), D308 (= D442), K335 (= K470), N394 (= N570), W395 (= W571), W479 (≠ F672)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C242), C117 (vs. gap), E185 (≠ V334), W267 (≠ D402), D308 (= D442), K335 (= K470), P389 (≠ Y565), Y390 (≠ F566), W440 (≠ A626)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 614, 615, 617, 620, 624, 628, 631, 632, 636, 637, 640, 641, 642, 643, 645
- binding pyrroloquinoline quinone: 543, 544
- binding tetrahydrofuran-2-carboxylic acid: 544
Q46444 Quinohemoprotein alcohol dehydrogenase; QH-ADH; Alcohol dehydrogenase (azurin); PQQ-containing alcohol dehydrogenase; PQQ-dependent ADH; Quinohaemoprotein ethanol dehydrogenase type I; QH-EDHI; EC 1.1.9.1 from Comamonas testosteroni (Pseudomonas testosteroni) (see 3 papers)
27% identity, 79% coverage: 143:749/769 of query aligns to 51:571/708 of Q46444
- E101 (≠ Q197) binding
- C147 (= C242) modified: Disulfide link with 148
- C148 (vs. gap) modified: Disulfide link with 147
- R153 (= R243) binding
- T198 (= T312) binding
- GA 214:215 (≠ MA 332:333) binding
- E216 (≠ V334) binding
- T274 (≠ N378) binding
- N294 (= N398) binding
- D339 (= D442) binding
- K366 (= K470) binding
- NW 425:426 (= NW 570:571) binding
Sites not aligning to the query:
- 1:31 signal peptide
- 575 binding
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 678 binding axial binding residue
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
26% identity, 84% coverage: 106:749/769 of query aligns to 2:567/718 of Q4W6G0
- C138 (≠ Y247) modified: Disulfide link with 139
- C139 (≠ Y248) modified: Disulfide link with 138
- R144 (= R253) binding
- T189 (= T312) binding
- GA 205:206 (≠ MA 332:333) binding
- E207 (≠ V334) binding
- T264 (≠ N378) binding
- N284 (= N398) binding
- D329 (= D442) binding
- K356 (= K470) binding
- W415 (≠ F566) binding
- DW 419:420 (≠ NW 570:571) binding
Sites not aligning to the query:
- 1:29 signal peptide
- 30:718 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH-IIG
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 676 binding axial binding residue
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
26% identity, 80% coverage: 135:749/769 of query aligns to 1:521/664 of 1kv9A
- active site: E173 (≠ V334), N250 (= N398), D295 (= D442)
- binding acetone: E173 (≠ V334), D295 (= D442), P377 (≠ Y565), F378 (= F566)
- binding calcium ion: E173 (≠ V334), N250 (= N398), D295 (= D442)
- binding heme c: A101 (≠ G244), R102 (≠ V245)
- binding pyrroloquinoline quinone: E59 (≠ Q197), C105 (≠ Y248), C106 (≠ E249), R111 (≠ E254), T155 (= T312), G170 (= G331), G171 (≠ M332), A172 (= A333), E173 (≠ V334), T230 (≠ N378), W232 (= W380), N250 (= N398), D295 (= D442), K322 (= K470), N382 (= N570), W383 (= W571), W460 (≠ L686)
Sites not aligning to the query:
- binding heme c: 590, 591, 594, 595, 605, 606, 608, 611, 615, 619, 622, 623, 631, 633, 634, 636
- binding pyrroloquinoline quinone: 524, 525
1yiqA Molecular cloning and structural analysis of quinohemoprotein alcohol dehydrogenase adhiig from pseudomonas putida hk5. Compariison to the other quinohemoprotein alcohol dehydrogenase adhiib found in the same microorganism. (see paper)
26% identity, 80% coverage: 132:749/769 of query aligns to 2:538/684 of 1yiqA
- active site: E178 (≠ V334), N255 (= N398), D300 (= D442)
- binding calcium ion: E178 (≠ V334), N255 (= N398), D300 (= D442)
- binding heme c: R60 (≠ S191), G106 (= G244)
- binding pyrroloquinoline quinone: E63 (≠ Q197), C109 (≠ Y247), C110 (≠ Y248), R115 (= R253), T160 (= T312), G175 (= G331), G176 (≠ M332), A177 (= A333), E178 (≠ V334), T235 (≠ N378), W237 (= W380), N255 (= N398), D300 (= D442), K327 (= K470), W386 (≠ F566), D390 (≠ N570), W391 (= W571), F477 (≠ L686)
Sites not aligning to the query:
- binding heme c: 605, 606, 608, 609, 610, 621, 623, 626, 630, 634, 637, 638, 642, 645, 646, 647, 648, 650, 654, 662
- binding pyrroloquinoline quinone: 541, 542
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
26% identity, 80% coverage: 138:749/769 of query aligns to 26:543/690 of Q8GR64