SitesBLAST
Comparing WP_012386539.1 NCBI__GCF_000019845.1:WP_012386539.1 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)
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
39% identity, 90% coverage: 55:566/566 of query aligns to 26:556/562 of 6zcvA
- active site: E172 (= E201), N254 (= N267), D296 (= D309)
- binding calcium ion: N161 (≠ K190), K163 (= K192), P278 (= P291), D279 (≠ A292)
- binding pyrroloquinoline quinone: Q60 (≠ E87), C104 (= C133), C105 (= C134), I108 (≠ V137), R110 (= R139), S154 (≠ T183), G170 (= G199), G171 (= G200), E172 (= E201), W236 (= W249), D298 (= D311), R323 (= R336), N390 (= N395), W466 (≠ N473), G529 (= G537), A530 (≠ G538)
Q9Z4J7 Quinoprotein ethanol dehydrogenase; QEDH; Quinoprotein alcohol dehydrogenase (cytochrome c); Quinoprotein alcohol dehydrogenase (cytochrome c550); EC 1.1.2.8 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 4 papers)
40% identity, 92% coverage: 47:566/566 of query aligns to 53:613/623 of Q9Z4J7
- E95 (= E87) binding pyrroloquinoline quinone
- C139 (= C133) modified: Disulfide link with 140
- CC 139:140 (= CC 133:134) mutation to AA: 15-fold decrease in catalytic activity with the natural electron acceptor cytochrome c550. Does not affect, or even increases, catalytic activity with artificial electron acceptors. Shows high decreased affinity for primary alcohols, while the affinity for the secondary alcohol 2-propanol is unaltered.
- C140 (= C134) modified: Disulfide link with 139
- R145 (= R139) binding pyrroloquinoline quinone
- T189 (= T183) binding pyrroloquinoline quinone
- HGS 207:209 (≠ -GV 196:197) binding pyrroloquinoline quinone
- E213 (= E201) binding Ca(2+)
- N300 (= N267) binding Ca(2+)
- D350 (= D309) binding Ca(2+)
- R378 (= R336) binding pyrroloquinoline quinone
- W523 (≠ N473) binding pyrroloquinoline quinone
- A587 (≠ G538) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:34 signal peptide
- 45 binding Ca(2+)
- 48 binding Ca(2+)
- 51 binding Ca(2+)
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
39% identity, 92% coverage: 47:566/566 of query aligns to 19:579/582 of 1flgA
- active site: E179 (= E201), N266 (= N267), D316 (= D309)
- binding calcium ion: E179 (= E201), N266 (= N267), D316 (= D309)
- binding pyrroloquinoline quinone: E61 (= E87), C105 (= C133), C106 (= C134), R111 (= R139), T155 (= T183), S176 (= S198), G177 (= G199), D178 (≠ G200), W248 (= W249), R344 (= R336), N413 (= N395), W414 (= W396), W489 (≠ N473), G552 (= G537), A553 (≠ G538)
Sites not aligning to the query:
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
37% identity, 98% coverage: 12:566/566 of query aligns to 5:572/690 of Q8GR64
- E81 (= E87) binding pyrroloquinoline quinone
- C127 (= C133) modified: Disulfide link with 128
- C128 (= C134) modified: Disulfide link with 127
- R133 (= R139) binding pyrroloquinoline quinone
- T177 (= T183) binding pyrroloquinoline quinone
- GA 193:194 (≠ GG 199:200) binding pyrroloquinoline quinone
- E195 (= E201) binding Ca(2+)
- T252 (≠ P247) binding pyrroloquinoline quinone
- N272 (= N267) binding Ca(2+)
- D317 (= D309) binding Ca(2+)
- K344 (≠ R336) binding pyrroloquinoline quinone
- NW 404:405 (= NW 395:396) binding pyrroloquinoline quinone
- V547 (≠ G538) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:22 signal peptide
- 23:690 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH IIB
- 613 binding covalent
- 616 binding covalent
- 617 binding axial binding residue
- 655 binding axial binding residue
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
37% identity, 95% coverage: 30:566/566 of query aligns to 1:550/664 of 1kv9A
- active site: E173 (= E201), N250 (= N267), D295 (= D309)
- binding acetone: E173 (= E201), D295 (= D309)
- binding calcium ion: E173 (= E201), N250 (= N267), D295 (= D309)
- binding heme c: A101 (≠ L129), R102 (≠ K130)
- binding pyrroloquinoline quinone: E59 (= E87), C105 (= C133), C106 (= C134), R111 (= R139), T155 (= T183), G170 (≠ S198), A172 (≠ G200), E173 (= E201), T230 (≠ P247), W232 (= W249), K322 (≠ R336), N382 (= N395), W383 (= W396), W460 (= W472), V525 (≠ G538)
Sites not aligning to the query:
- binding heme c: 590, 591, 594, 595, 605, 606, 608, 611, 615, 619, 623, 631, 633, 636
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)
38% identity, 88% coverage: 40:537/566 of query aligns to 54:574/708 of Q46444
- E101 (= E87) binding pyrroloquinoline quinone
- C147 (= C133) modified: Disulfide link with 148
- C148 (= C134) modified: Disulfide link with 147
- R153 (= R139) binding pyrroloquinoline quinone
- T198 (= T183) binding pyrroloquinoline quinone
- GA 214:215 (≠ GG 199:200) binding pyrroloquinoline quinone
- E216 (= E201) binding Ca(2+)
- T274 (≠ P247) binding pyrroloquinoline quinone
- N294 (= N267) binding Ca(2+)
- D339 (= D309) binding Ca(2+)
- K366 (≠ R336) binding pyrroloquinoline quinone
- NW 425:426 (= NW 395:396) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:31 signal peptide
- 575 binding pyrroloquinoline quinone
- 635 binding covalent
- 638 binding covalent
- 639 binding axial binding residue
- 678 binding axial binding residue
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
38% identity, 88% coverage: 40:537/566 of query aligns to 23:543/670 of 1kb0A
- active site: E185 (= E201), N263 (= N267), D308 (= D309)
- binding calcium ion: E185 (= E201), N263 (= N267), D308 (= D309)
- binding pyrroloquinoline quinone: E70 (= E87), C116 (= C133), C117 (= C134), R122 (= R139), T167 (= T183), G182 (≠ S198), G183 (= G199), A184 (≠ G200), E185 (= E201), T243 (≠ P247), W245 (= W249), D308 (= D309), K335 (≠ R336), N394 (= N395), W395 (= W396), W479 (= W472), G543 (= G537)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C133), C117 (= C134), E185 (= E201), D308 (= D309), P389 (≠ F390)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
- binding pyrroloquinoline quinone: 544
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
37% identity, 87% coverage: 44:537/566 of query aligns to 12:543/563 of 6damA
- active site: E171 (= E201), N259 (= N267), D301 (= D309)
- binding pyrroloquinoline quinone: E55 (= E87), C103 (= C133), C104 (= C134), R109 (= R139), T153 (= T183), S168 (= S198), G169 (= G199), G170 (= G200), E171 (= E201), T239 (≠ P247), W241 (= W249), D303 (= D311), R328 (= R336), N394 (= N395), W480 (≠ N473), G543 (= G537)
Sites not aligning to the query:
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
37% identity, 87% coverage: 46:537/566 of query aligns to 14:531/577 of 4maeA
- active site: E172 (= E201), N256 (= N267), D299 (= D309)
- binding cerium (iii) ion: E172 (= E201), N256 (= N267), D299 (= D309), D301 (= D311)
- binding pyrroloquinoline quinone: E55 (= E87), C104 (= C133), C105 (= C134), R110 (= R139), T154 (= T183), S169 (= S198), G170 (= G199), G171 (= G200), E172 (= E201), T236 (≠ P247), W238 (= W249), D301 (= D311), R326 (= R336), D388 (≠ N395), W467 (≠ N473), G531 (= G537)
Sites not aligning to the query:
6fkwA Europium-containing methanol dehydrogenase (see paper)
37% identity, 87% coverage: 46:537/566 of query aligns to 14:531/576 of 6fkwA
- active site: E172 (= E201), N256 (= N267), D299 (= D309), D301 (= D311)
- binding europium ion: E172 (= E201), N256 (= N267), D299 (= D309), D301 (= D311)
- binding pyrroloquinoline quinone: E55 (= E87), C104 (= C133), C105 (= C134), R110 (= R139), T154 (= T183), S169 (= S198), G170 (= G199), G171 (= G200), E172 (= E201), T236 (≠ P247), W238 (= W249), D301 (= D311), R326 (= R336), D388 (≠ N395), W467 (≠ N473), G531 (= G537)
Sites not aligning to the query:
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
36% identity, 98% coverage: 7:559/566 of query aligns to 11:598/718 of Q4W6G0
- C138 (= C133) modified: Disulfide link with 139
- C139 (= C134) modified: Disulfide link with 138
- R144 (= R139) binding pyrroloquinoline quinone
- T189 (= T183) binding pyrroloquinoline quinone
- GA 205:206 (≠ GG 199:200) binding pyrroloquinoline quinone
- E207 (= E201) binding Ca(2+)
- T264 (≠ P247) binding pyrroloquinoline quinone
- N284 (= N267) binding Ca(2+)
- D329 (= D309) binding Ca(2+)
- K356 (≠ R336) binding pyrroloquinoline quinone
- W415 (≠ L391) binding substrate
- DW 419:420 (≠ NW 395:396) binding pyrroloquinoline quinone
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
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
36% identity, 92% coverage: 46:566/566 of query aligns to 14:588/588 of 7o6zB
- binding methanol: E173 (= E201), W263 (= W271), D314 (= D309)
- binding Neodymium Ion: E173 (= E201), N259 (= N267), D314 (= D309), D316 (= D311)
- binding pyrroloquinoline quinone: E55 (= E87), C105 (= C133), C106 (= C134), R111 (= R139), T155 (= T183), G170 (≠ S198), G171 (= G199), D172 (≠ G200), E173 (= E201), W241 (= W249), D316 (= D311), R341 (= R336), D403 (≠ N395), W481 (≠ N473), G544 (= G537), W545 (vs. gap)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
36% identity, 92% coverage: 46:566/566 of query aligns to 14:588/588 of 7o6zA
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)
36% identity, 94% coverage: 30:559/566 of query aligns to 5:569/684 of 1yiqA
- active site: E178 (= E201), N255 (= N267), D300 (= D309)
- binding calcium ion: E178 (= E201), N255 (= N267), D300 (= D309)
- binding pyrroloquinoline quinone: E63 (= E87), C109 (= C133), C110 (= C134), R115 (= R139), T160 (= T183), G175 (≠ S198), G176 (= G199), A177 (≠ G200), E178 (= E201), T235 (≠ P247), W237 (= W249), K327 (≠ R336), D390 (≠ N395), W391 (= W396), F477 (≠ W472), A542 (≠ G538)
Sites not aligning to the query:
- binding heme c: 605, 606, 608, 609, 610, 623, 626, 630, 634, 637, 638, 642, 645, 646, 647, 648, 650
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
35% identity, 89% coverage: 34:537/566 of query aligns to 2:536/579 of 6oc6A
- active site: E171 (= E201), N255 (= N267), D297 (= D309)
- binding pyrroloquinoline quinone: E55 (= E87), C103 (= C133), C104 (= C134), R109 (= R139), T153 (= T183), S168 (= S198), G169 (= G199), G170 (= G200), E171 (= E201), W237 (= W249), D299 (= D311), R324 (= R336), D395 (≠ N395), W473 (≠ N473), G536 (= G537)
Sites not aligning to the query:
O05542 Alcohol dehydrogenase (quinone), dehydrogenase subunit; ADH; Alcohol dehydrogenase (quinone), acceptor subunit; Alcohol dehydrogenase (quinone), subunit I; Ethanol:Q2 reductase; G3-ADH subunit I; Quinohemoprotein alcohol dehydrogenase; Quinohemoprotein-cytochrome c complex; Ubiquinol oxidase; EC 1.1.5.5 from Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) (see paper)
36% identity, 93% coverage: 22:548/566 of query aligns to 32:598/757 of O05542
- Q35 (≠ A25) modified: Pyrrolidone carboxylic acid
Sites not aligning to the query:
8gy2A Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
36% identity, 92% coverage: 26:548/566 of query aligns to 2:564/723 of 8gy2A
- binding calcium ion: E181 (= E201), N263 (= N267), D308 (= D309)
- binding heme c: D104 (≠ K130)
- binding pyrroloquinoline quinone: C107 (= C133), C108 (= C134), D163 (≠ T183), G179 (= G199), A180 (≠ G200), E181 (= E201), W245 (= W249), N263 (= N267), D308 (= D309), K335 (≠ R336), F398 (≠ W396), W489 (= W472)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
P12293 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Paracoccus denitrificans (see 2 papers)
35% identity, 93% coverage: 9:537/566 of query aligns to 11:570/631 of P12293
- C135 (= C133) modified: Disulfide link with 136
- C136 (= C134) modified: Disulfide link with 135
- C418 (= C387) modified: Disulfide link with 447
- C447 (= C416) modified: Disulfide link with 418
Sites not aligning to the query:
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
35% identity, 87% coverage: 43:537/566 of query aligns to 11:532/573 of 7ce5A
- active site: E177 (= E201), N261 (= N267), D303 (= D309)
- binding calcium ion: E177 (= E201), N261 (= N267), D303 (= D309)
- binding methanol: E177 (= E201)
- binding pyrroloquinoline quinone: E55 (= E87), C103 (= C133), C104 (= C134), R109 (= R139), T159 (= T183), A174 (≠ S198), G175 (= G199), A176 (≠ G200), E177 (= E201), T241 (≠ P247), W243 (= W249), R330 (= R336), N393 (= N395), W469 (≠ N473), G532 (= G537)
Sites not aligning to the query:
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
35% identity, 87% coverage: 43:537/566 of query aligns to 11:532/573 of 7cdlC
- active site: E177 (= E201), N261 (= N267), D303 (= D309)
- binding calcium ion: E177 (= E201), N261 (= N267), D303 (= D309)
- binding pyrroloquinoline quinone: E55 (= E87), R109 (= R139), T159 (= T183), A174 (≠ S198), A176 (≠ G200), E177 (= E201), T241 (≠ P247), W243 (= W249), D303 (= D309), R330 (= R336), N393 (= N395), W469 (≠ N473), G532 (= G537)
Sites not aligning to the query:
Query Sequence
>WP_012386539.1 NCBI__GCF_000019845.1:WP_012386539.1
MKRSNFLRSTSLAVALMLTGGAIAAEETYAPVTDARLGAAAKDAGWLMYRRDYTGSGYAP
FDTINTSNVANLKQVWDYKTDFDMGHESPAIVNGDYLFITTPKNELHAFQASTGKPLWVY
KHDLTGVGLKTICCDVVNRGVALYGDNVYMATLDNRVVALDAKTGKPVWNTQLEKPDVGY
AMTVAPLALKGKVVVGVSGGEYGARGYIAALDASTGKEVWRRHTIPAPNEPGGDTWPEGA
YKTGGGPAWLTGSYDADTDTLFWGVGNPGPWLATLRPGDNLYTDSVLALDPATGNIKWHY
QYTPNDTWDYDGTNEQVLIDITHEGKPYKALVSASRNGWLYAIDRTNGKLIYGEKFATAT
SVTGFKDGKPVTDPDKRPDINKEIFTCPSFLGGKNWWPISVDVKTQIAYVPTMHTCMTMK
GNAVSYRAGLPFLGESFKVVRDPAFPNHWGAVQAIDLNTGKQVWDFPSELPWNDGTLTTA
GGVVFSGSADGYLHAFDAKTGKVLWKSPQATSGFLGVPSTWKVGDKQYIGIYAGWGGGTP
IWGGDMAKDPRVLNIPLGGHFYVFSL
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