SitesBLAST
Comparing RR42_RS11485 FitnessBrowser__Cup4G11:RR42_RS11485 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
63% identity, 96% coverage: 22:580/580 of query aligns to 1:559/562 of 6zcvA
- active site: E172 (= E193), N254 (= N275), D296 (= D317)
- binding calcium ion: N161 (≠ K182), K163 (≠ M184), P278 (= P299), D279 (≠ A300)
- binding pyrroloquinoline quinone: Q60 (≠ E81), C104 (= C125), C105 (= C126), I108 (≠ V129), R110 (= R131), S154 (≠ T175), G170 (= G191), G171 (= G192), E172 (= E193), W236 (= W257), D298 (= D319), R323 (= R340), N390 (= N411), W466 (= W487), G529 (= G550), A530 (= A551)
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)
55% identity, 96% coverage: 23:577/580 of query aligns to 37:613/623 of Q9Z4J7
- D45 (= D31) binding
- T48 (≠ S34) binding
- D51 (= D37) binding
- E95 (= E81) binding
- C139 (= C125) modified: Disulfide link with 140
- CC 139:140 (= CC 125:126) 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 (= C126) modified: Disulfide link with 139
- R145 (= R131) binding
- T189 (= T175) binding
- HGS 207:209 (≠ TGI 187:189) binding
- E213 (= E193) binding
- N300 (= N275) binding
- D350 (= D317) binding
- R378 (= R340) binding
- W523 (= W487) binding
- A587 (= A551) binding
Sites not aligning to the query:
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
55% identity, 96% coverage: 23:577/580 of query aligns to 3:579/582 of 1flgA
- active site: E179 (= E193), N266 (= N275), D316 (= D317)
- binding calcium ion: D11 (= D31), T14 (≠ S34), D17 (= D37), E179 (= E193), N266 (= N275), D316 (= D317)
- binding pyrroloquinoline quinone: E61 (= E81), C105 (= C125), C106 (= C126), R111 (= R131), T155 (= T175), S176 (= S190), G177 (= G191), D178 (≠ G192), W248 (= W257), R344 (= R340), N413 (= N411), W414 (≠ Q412), W489 (= W487), G552 (= G550), A553 (= A551)
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
39% identity, 95% coverage: 25:577/580 of query aligns to 1:561/563 of 6damA
- active site: E171 (= E193), N259 (= N275), D301 (= D317)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C125), C104 (= C126), R109 (= R131), T153 (= T175), S168 (= S190), G169 (= G191), G170 (= G192), E171 (= E193), T239 (≠ A255), W241 (= W257), D303 (= D319), R328 (= R340), N394 (= N411), W480 (= W487), G543 (= G550), W544 (= W555)
6fkwA Europium-containing methanol dehydrogenase (see paper)
43% identity, 91% coverage: 25:550/580 of query aligns to 2:531/576 of 6fkwA
- active site: E172 (= E193), N256 (= N275), D299 (= D317), D301 (= D319)
- binding europium ion: E172 (= E193), N256 (= N275), D299 (= D317), D301 (= D319)
- binding pyrroloquinoline quinone: E55 (= E81), C104 (= C125), C105 (= C126), R110 (= R131), T154 (= T175), S169 (= S190), G170 (= G191), G171 (= G192), E172 (= E193), T236 (≠ A255), W238 (= W257), D301 (= D319), R326 (= R340), D388 (≠ N411), W467 (= W487), G531 (= G550)
Sites not aligning to the query:
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
43% identity, 91% coverage: 25:550/580 of query aligns to 2:531/577 of 4maeA
- active site: E172 (= E193), N256 (= N275), D299 (= D317)
- binding cerium (iii) ion: E172 (= E193), N256 (= N275), D299 (= D317), D301 (= D319)
- binding pyrroloquinoline quinone: E55 (= E81), C104 (= C125), C105 (= C126), R110 (= R131), T154 (= T175), S169 (= S190), G170 (= G191), G171 (= G192), E172 (= E193), T236 (≠ A255), W238 (= W257), D301 (= D319), R326 (= R340), D388 (≠ N411), W467 (= W487), G531 (= G550)
Sites not aligning to the query:
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
42% identity, 87% coverage: 49:550/580 of query aligns to 25:536/579 of 6oc6A
- active site: E171 (= E193), N255 (= N275), D297 (= D317)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C125), C104 (= C126), R109 (= R131), T153 (= T175), S168 (= S190), G169 (= G191), G170 (= G192), E171 (= E193), W237 (= W257), D299 (= D319), R324 (= R340), D395 (≠ N411), W473 (= W487), G536 (= G550)
Sites not aligning to the query:
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
40% identity, 93% coverage: 21:558/580 of query aligns to 1:532/664 of 1kv9A
- active site: E173 (= E193), N250 (= N275), D295 (= D317)
- binding acetone: E173 (= E193), D295 (= D317)
- binding calcium ion: E173 (= E193), N250 (= N275), D295 (= D317)
- binding heme c: A101 (≠ G121), R102 (≠ I122)
- binding pyrroloquinoline quinone: E59 (= E81), C105 (= C125), C106 (= C126), R111 (= R131), T155 (= T175), G170 (≠ S190), A172 (≠ G192), E173 (= E193), T230 (= T256), W232 (= W257), K322 (≠ R340), N382 (= N411), W383 (≠ Q412), W460 (= W487), V525 (≠ A551)
Sites not aligning to the query:
- binding heme c: 590, 591, 594, 595, 605, 606, 608, 611, 615, 619, 623, 631, 633, 636
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
39% identity, 87% coverage: 49:554/580 of query aligns to 25:548/588 of 7o6zB
- binding methanol: E173 (= E193), W263 (= W279), D314 (= D317)
- binding Neodymium Ion: E173 (= E193), N259 (= N275), D314 (= D317), D316 (= D319)
- binding pyrroloquinoline quinone: E55 (= E81), C105 (= C125), C106 (= C126), R111 (= R131), T155 (= T175), G170 (≠ S190), G171 (= G191), D172 (≠ G192), E173 (= E193), W241 (= W257), D316 (= D319), R341 (= R340), D403 (≠ N411), W481 (= W487), G544 (= G550), W545 (≠ A551)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
39% identity, 87% coverage: 49:554/580 of query aligns to 25:548/588 of 7o6zA
Q8GR64 Quinohemoprotein alcohol dehydrogenase ADH IIB; ADH IIB; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 3 papers)
40% identity, 92% coverage: 23:558/580 of query aligns to 25:554/690 of Q8GR64
- E81 (= E81) binding
- C127 (= C125) modified: Disulfide link with 128
- C128 (= C126) modified: Disulfide link with 127
- R133 (= R131) binding
- T177 (= T175) binding
- GA 193:194 (≠ GG 191:192) binding
- E195 (= E193) binding
- T252 (= T256) binding
- N272 (= N275) binding
- D317 (= D317) binding
- K344 (≠ R340) binding
- NW 404:405 (≠ NQ 411:412) binding
- V547 (≠ A551) binding
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
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)
37% identity, 94% coverage: 35:577/580 of query aligns to 51:614/757 of O05542
Sites not aligning to the query:
- 1:34 signal peptide
- 35 modified: Pyrrolidone carboxylic acid
8gy2A Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
37% identity, 94% coverage: 35:577/580 of query aligns to 17:580/723 of 8gy2A
- binding calcium ion: E181 (= E193), N263 (= N275), D308 (= D317)
- binding heme c: D104 (≠ P124)
- binding pyrroloquinoline quinone: C107 (= C125), C108 (= C126), D163 (≠ T175), G179 (= G191), A180 (≠ G192), E181 (= E193), W245 (= W257), N263 (= N275), D308 (= D317), K335 (≠ R340), F398 (≠ Q412), W489 (≠ L486)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
37% identity, 91% coverage: 49:577/580 of query aligns to 25:573/573 of 7ce5A
- active site: E177 (= E193), N261 (= N275), D303 (= D317)
- binding calcium ion: E177 (= E193), N261 (= N275), D303 (= D317)
- binding methanol: E177 (= E193), W533 (vs. gap)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C125), C104 (= C126), R109 (= R131), T159 (= T175), A174 (≠ S190), G175 (= G191), A176 (≠ G192), E177 (= E193), T241 (≠ A255), W243 (= W257), R330 (= R340), N393 (= N411), W469 (= W487), G532 (= G550), W533 (vs. gap)
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
37% identity, 91% coverage: 49:577/580 of query aligns to 25:573/573 of 7cdlC
- active site: E177 (= E193), N261 (= N275), D303 (= D317)
- binding calcium ion: E177 (= E193), N261 (= N275), D303 (= D317)
- binding pyrroloquinoline quinone: E55 (= E81), R109 (= R131), T159 (= T175), A174 (≠ S190), A176 (≠ G192), E177 (= E193), T241 (≠ A255), W243 (= W257), D303 (= D317), R330 (= R340), N393 (= N411), W469 (= W487), G532 (= G550), W533 (vs. gap)
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, 95% coverage: 25:575/580 of query aligns to 48:594/708 of Q46444
- E101 (= E81) binding
- C147 (= C125) modified: Disulfide link with 148
- C148 (= C126) modified: Disulfide link with 147
- R153 (= R131) binding
- T198 (= T175) binding
- GA 214:215 (≠ GG 191:192) binding
- E216 (= E193) binding
- T274 (= T256) binding
- N294 (= N275) binding
- D339 (= D317) binding
- K366 (≠ R340) binding
- NW 425:426 (≠ NQ 411:412) binding
- V575 (≠ A551) binding
Sites not aligning to the query:
- 1:31 signal peptide
- 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, 95% coverage: 25:575/580 of query aligns to 17:563/670 of 1kb0A
- active site: E185 (= E193), N263 (= N275), D308 (= D317)
- binding calcium ion: E185 (= E193), N263 (= N275), D308 (= D317)
- binding pyrroloquinoline quinone: E70 (= E81), C116 (= C125), C117 (= C126), R122 (= R131), T167 (= T175), G182 (≠ S190), G183 (= G191), A184 (≠ G192), E185 (= E193), T243 (= T256), W245 (= W257), D308 (= D317), K335 (≠ R340), N394 (= N411), W395 (≠ Q412), W479 (≠ L486), G543 (= G550), V544 (≠ A551)
- binding tetrahydrofuran-2-carboxylic acid: C116 (= C125), C117 (= C126), E185 (= E193), D308 (= D317), P389 (≠ F406)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
P16027 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) (see 3 papers)
37% identity, 96% coverage: 21:577/580 of query aligns to 25:607/626 of P16027
- C130 (= C125) modified: Disulfide link with 131; mutation to S: Inactive.
- C131 (= C126) modified: Disulfide link with 130; mutation to S: Inactive.
- D330 (= D317) mutation to E: Lower affinity for methanol.
- C413 (≠ A403) modified: Disulfide link with 442
- C442 (≠ G432) modified: Disulfide link with 413
Sites not aligning to the query:
1w6sC The high resolution structure of methanol dehydrogenase from methylobacterium extorquens (see paper)
37% identity, 96% coverage: 24:577/580 of query aligns to 1:580/596 of 1w6sC
- active site: E177 (= E193), N261 (= N275), D303 (= D317)
- binding calcium ion: E177 (= E193), N261 (= N275)
- binding pyrroloquinoline quinone: E55 (= E81), C103 (= C125), C104 (= C126), R109 (= R131), T159 (= T175), S174 (= S190), A176 (≠ G192), E177 (= E193), T241 (≠ A255), W243 (= W257), R331 (= R340), N394 (= N411), W476 (= W487), W540 (vs. gap)
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, 99% coverage: 1:577/580 of query aligns to 11:596/718 of Q4W6G0
- C138 (= C125) modified: Disulfide link with 139
- C139 (= C126) modified: Disulfide link with 138
- R144 (= R131) binding
- T189 (= T175) binding
- GA 205:206 (≠ GG 191:192) binding
- E207 (= E193) binding
- T264 (≠ A255) binding
- N284 (= N275) binding
- D329 (= D317) binding
- K356 (≠ R340) binding
- W415 (≠ L407) binding
- DW 419:420 (≠ NQ 411:412) 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
Query Sequence
>RR42_RS11485 FitnessBrowser__Cup4G11:RR42_RS11485
MRTLRVMMVLAATTASLVAQAAVTDAMIENDAKSPGDVLSWGMGPQGQRFSTLNRINTKN
ISQLVPAWSFSFGGEKQRGQEAQPLIHDGKMFVTASYSRIYALDLKTGTKLWKYEHRLPE
GIMPCCDVVNRGAALYDNLVIFGTLDAQLVALDQKTGKVVWKEKIEDYAAGYSYTAAPLI
VKGMVLTGISGGEFGVVGRVEARDAKTGQMVWSRPVVEGHMGYKYDKDGNKTENGVTGTQ
NASWPGETWKTGGAATWLGGTYDPQTGLAYFGTGNPGPWNSHMRKGDNLYSASTVALDPA
TGKIVWHYQNTPNDGWDFDGVNEFVTFDQDGKRLGGKADRNGFFYVNDATSGKLVNAFPF
VKKITWASSIDLKTGRPNMIAESRPGDPAAGGDPKKGQSVFAAPGFLGGKNQQPMAYSPQ
TGLFYVPANEWGMDIWNEPVGYKKGAAFLGAGFTIHPLNEDYIGSLRAINPKTGKIEWEV
KNYAPLWGGVMTTAGGLVFWGTPEGYLKAADAKTGKELWKFQTGSGVVAPPVTWEEGGEQ
YVAVVSGWGGAVPLWGGEVAKRVNFLEQGGSVWVFKLHKS
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