SitesBLAST
Comparing Pf1N1B4_5582 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5582 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)
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)
26% identity, 76% coverage: 170:786/807 of query aligns to 59:571/708 of Q46444
- E101 (= E217) binding
- C147 (≠ R263) modified: Disulfide link with 148
- C148 (= C264) modified: Disulfide link with 147
- R153 (= R265) binding
- T198 (≠ S347) binding
- GA 214:215 (≠ VA 363:364) binding
- E216 (≠ D365) binding
- T274 (≠ N413) binding
- N294 (≠ S433) binding
- D339 (= D477) binding
- K366 (= K505) binding
- NW 425:426 (= NW 604:605) 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
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
26% identity, 76% coverage: 170:786/807 of query aligns to 28:540/670 of 1kb0A
- active site: E185 (≠ D365), N263 (≠ S433), D308 (= D477)
- binding calcium ion: E185 (≠ D365), N263 (≠ S433), D308 (= D477)
- binding pyrroloquinoline quinone: E70 (= E217), C116 (≠ R263), C117 (= C264), R122 (= R265), T167 (≠ S347), G182 (≠ R362), G183 (≠ V363), A184 (= A364), E185 (≠ D365), T243 (≠ N413), W245 (= W415), D308 (= D477), K335 (= K505), N394 (= N604), W395 (= W605), W479 (≠ T722)
- binding tetrahydrofuran-2-carboxylic acid: C116 (≠ R263), C117 (= C264), E185 (≠ D365), D308 (= D477), P389 (≠ S599)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
- binding pyrroloquinoline quinone: 543, 544
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
25% identity, 81% coverage: 132:786/807 of query aligns to 14:567/718 of Q4W6G0
- C138 (= C264) modified: Disulfide link with 139
- C139 (vs. gap) modified: Disulfide link with 138
- R144 (= R265) binding
- T189 (≠ S347) binding
- GA 205:206 (≠ VA 363:364) binding
- E207 (≠ D365) binding
- T264 (≠ N413) binding
- N284 (≠ S433) binding
- D329 (= D477) binding
- K356 (= K505) binding
- W415 (≠ L600) binding
- DW 419:420 (≠ NW 604:605) 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
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
26% identity, 77% coverage: 166:786/807 of query aligns to 9:540/563 of 6damA
- active site: E171 (≠ V375), N259 (≠ S433), D301 (= D477)
- binding pyrroloquinoline quinone: E55 (≠ D212), C103 (= C264), C104 (vs. gap), R109 (= R265), T153 (≠ S347), S168 (≠ P372), G169 (= G373), G170 (= G374), E171 (≠ V375), T239 (≠ N413), W241 (= W415), D303 (= D479), R328 (≠ K505), N394 (= N604), W480 (≠ L723)
Sites not aligning to the query:
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 77% coverage: 169:786/807 of query aligns to 12:541/588 of 7o6zB
- binding methanol: E173 (≠ M371), W263 (vs. gap), D314 (= D477)
- binding Neodymium Ion: E173 (≠ M371), N259 (≠ S433), D314 (= D477), D316 (= D479)
- binding pyrroloquinoline quinone: E55 (= E217), C105 (≠ Y269), C106 (≠ F270), R111 (≠ A275), T155 (≠ V339), G170 (≠ Q368), G171 (≠ T369), D172 (= D370), E173 (≠ M371), W241 (= W415), D316 (= D479), R341 (≠ K505), D403 (≠ N604), W481 (≠ L723)
Sites not aligning to the query:
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 77% coverage: 169:786/807 of query aligns to 12:541/588 of 7o6zA
Sites not aligning to the query:
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)
25% identity, 78% coverage: 155:786/807 of query aligns to 8:538/684 of 1yiqA
- active site: E178 (≠ D365), N255 (≠ S433), D300 (= D477)
- binding calcium ion: E178 (≠ D365), N255 (≠ S433), D300 (= D477)
- binding pyrroloquinoline quinone: E63 (= E217), C109 (= C264), C110 (vs. gap), R115 (= R265), T160 (≠ S347), G175 (≠ R362), G176 (≠ V363), A177 (= A364), E178 (≠ D365), T235 (≠ N413), W237 (= W415), K327 (= K505), D390 (≠ N604), W391 (= W605), F477 (≠ Q703)
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
- binding pyrroloquinoline quinone: 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)
25% identity, 77% coverage: 166:786/807 of query aligns to 35:543/690 of Q8GR64
- E81 (= E217) binding
- C127 (= C264) modified: Disulfide link with 128
- C128 (vs. gap) modified: Disulfide link with 127
- R133 (= R265) binding
- T177 (≠ S347) binding
- GA 193:194 (≠ VA 363:364) binding
- E195 (≠ D365) binding
- T252 (≠ N413) binding
- N272 (≠ S433) binding
- D317 (= D477) binding
- K344 (= K505) binding
- NW 404:405 (= NW 604:605) binding
Sites not aligning to the query:
- 1:22 signal peptide
- 23:690 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH IIB
- 547 binding
- 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)
25% identity, 77% coverage: 166:786/807 of query aligns to 13:521/664 of 1kv9A
- active site: E173 (≠ D365), N250 (≠ S433), D295 (= D477)
- binding acetone: E173 (≠ D365), D295 (= D477)
- binding calcium ion: E173 (≠ D365), N250 (≠ S433), D295 (= D477)
- binding heme c: A101 (≠ V260), R102 (≠ W261)
- binding pyrroloquinoline quinone: E59 (= E217), C105 (= C264), C106 (vs. gap), R111 (= R265), T155 (≠ S347), G170 (≠ R362), A172 (= A364), E173 (≠ D365), T230 (≠ N413), W232 (= W415), K322 (= K505), N382 (= N604), W383 (= W605), W460 (≠ Q703)
Sites not aligning to the query:
- binding heme c: 590, 591, 594, 595, 605, 606, 608, 611, 615, 619, 623, 631, 633, 636
- binding pyrroloquinoline quinone: 525
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)
25% identity, 76% coverage: 173:786/807 of query aligns to 54:583/623 of Q9Z4J7
- E95 (= E217) binding
- C139 (≠ R263) modified: Disulfide link with 140
- CC 139:140 (≠ RC 263:264) 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 (= C264) modified: Disulfide link with 139
- R145 (= R265) binding
- T189 (≠ I306) binding
- HGS 207:209 (≠ FGN 324:326) binding
- E213 (≠ V330) binding
- N300 (vs. gap) binding
- D350 (= D477) binding
- R378 (≠ K505) binding
- W523 (≠ L723) binding
Sites not aligning to the query:
- 1:34 signal peptide
- 45 binding
- 48 binding
- 51 binding
- 587 binding
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)
24% identity, 78% coverage: 156:786/807 of query aligns to 39:584/757 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
24% identity, 78% coverage: 156:786/807 of query aligns to 5:550/723 of 8gy2A
- binding calcium ion: E181 (≠ D365), N263 (≠ S433), D308 (= D477)
- binding heme c: D104 (≠ Q262)
- binding pyrroloquinoline quinone: C107 (vs. gap), C108 (vs. gap), D163 (≠ S347), G179 (≠ V363), A180 (= A364), E181 (≠ D365), W245 (= W415), N263 (≠ S433), D308 (= D477), K335 (= K505), F398 (≠ W605), W489 (≠ L708)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
25% identity, 76% coverage: 173:786/807 of query aligns to 20:549/582 of 1flgA
- active site: E179 (≠ V330), N266 (vs. gap), D316 (= D477)
- binding calcium ion: E179 (≠ V330), N266 (vs. gap), D316 (= D477)
- binding pyrroloquinoline quinone: E61 (= E217), C105 (≠ R263), C106 (= C264), R111 (= R265), T155 (≠ I306), S176 (≠ N327), G177 (= G328), D178 (≠ Q329), W248 (= W415), R344 (≠ K505), N413 (= N604), W414 (= W605), W489 (≠ L723)
Sites not aligning to the query:
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
24% identity, 75% coverage: 180:786/807 of query aligns to 26:526/562 of 6zcvA
- active site: E172 (≠ R362), N254 (≠ S433), D296 (= D477)
- binding calcium ion: N161 (≠ G354), K163 (vs. gap), P278 (≠ A459), D279 (≠ T460)
- binding pyrroloquinoline quinone: Q60 (= Q219), C104 (≠ R263), C105 (= C264), I108 (vs. gap), R110 (= R265), S154 (= S347), G170 (= G360), G171 (= G361), E172 (≠ R362), W236 (= W415), D298 (= D479), R323 (≠ K505), N390 (= N604), W466 (≠ L723)
Sites not aligning to the query:
P12293 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Paracoccus denitrificans (see 2 papers)
28% identity, 44% coverage: 162:517/807 of query aligns to 37:375/631 of P12293
- C135 (≠ R263) modified: Disulfide link with 136
- C136 (= C264) modified: Disulfide link with 135
Sites not aligning to the query:
- 1:32 signal peptide
- 418 modified: Disulfide link with 447
- 447 modified: Disulfide link with 418
6fkwA Europium-containing methanol dehydrogenase (see paper)
24% identity, 77% coverage: 166:786/807 of query aligns to 9:528/576 of 6fkwA
- active site: E172 (≠ D365), N256 (≠ S435), D299 (= D477), D301 (= D479)
- binding europium ion: E172 (≠ D365), N256 (≠ S435), D299 (= D477), D301 (= D479)
- binding pyrroloquinoline quinone: E55 (≠ D212), C104 (≠ N296), C105 (= C297), R110 (vs. gap), T154 (≠ S347), S169 (≠ R362), G170 (≠ V363), G171 (≠ A364), E172 (≠ D365), T236 (≠ N413), W238 (= W415), D301 (= D479), R326 (≠ K505), D388 (≠ N604), W467 (≠ L723)
Sites not aligning to the query:
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
24% identity, 77% coverage: 166:786/807 of query aligns to 9:528/577 of 4maeA
- active site: E172 (≠ D365), N256 (≠ S435), D299 (= D477)
- binding cerium (iii) ion: E172 (≠ D365), N256 (≠ S435), D299 (= D477), D301 (= D479)
- binding pyrroloquinoline quinone: E55 (≠ D212), C104 (≠ N296), C105 (= C297), R110 (vs. gap), T154 (≠ S347), S169 (≠ R362), G170 (≠ V363), G171 (≠ A364), E172 (≠ D365), T236 (≠ N413), W238 (= W415), D301 (= D479), R326 (≠ K505), D388 (≠ N604), W467 (≠ L723)
Sites not aligning to the query:
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
28% identity, 44% coverage: 162:517/807 of query aligns to 5:343/600 of 1lrwA
- active site: E177 (≠ D365), N261 (≠ S435), D303 (= D477)
- binding calcium ion: E177 (≠ D365), N261 (≠ S435), D303 (= D477)
- binding pyrroloquinoline quinone: E55 (≠ D212), C103 (≠ R263), C104 (= C264), R109 (= R265), T159 (≠ S347), S174 (≠ R362), G175 (≠ V363), A176 (= A364), E177 (≠ D365), T241 (≠ N413), W243 (= W415), R331 (≠ K505)
Sites not aligning to the query:
1w6sC The high resolution structure of methanol dehydrogenase from methylobacterium extorquens (see paper)
27% identity, 44% coverage: 162:517/807 of query aligns to 5:343/596 of 1w6sC
- active site: E177 (≠ D365), N261 (≠ S433), D303 (= D477)
- binding calcium ion: E177 (≠ D365), N261 (≠ S433)
- binding pyrroloquinoline quinone: E55 (= E217), C103 (≠ R263), C104 (= C264), R109 (= R265), T159 (≠ S347), S174 (≠ R362), A176 (= A364), E177 (≠ D365), T241 (≠ N413), W243 (= W415), R331 (≠ K505)
Sites not aligning to the query:
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)
27% identity, 44% coverage: 162:517/807 of query aligns to 32:370/626 of P16027
- C130 (≠ R263) modified: Disulfide link with 131; mutation to S: Inactive.
- C131 (= C264) modified: Disulfide link with 130; mutation to S: Inactive.
- D330 (= D477) mutation to E: Lower affinity for methanol.
Sites not aligning to the query:
- 1:27 signal peptide
- 413 modified: Disulfide link with 442
- 442 modified: Disulfide link with 413
Query Sequence
>Pf1N1B4_5582 FitnessBrowser__pseudo1_N1B4:Pf1N1B4_5582
MTKSRPSASVSRWPIWVVAFGVLVFGLFFATGGGYLATLGGSWYFLLAGFGLIVSAVLLF
KQRLQGAWLFAAVMVLTVIWALADVGLNFWPLISRLFALGVLSLFVALIYPHLRKANSLA
SGRSGYALSGVLAIAVVAGGAGMFVPHAPVSPTGDGPGLTTVDPAKAQKNWEHYGNDEGG
SRFAALDQINRSNVSKLVPAWTYNTGDIAISDGNGAEDQMTPLQVGDKVFICTPHNNLIA
LDADTGKQLWKNEINAKTRVWQRCRGVAYFDATAALAQPADGSTPVKPVSIPAGANCQRR
LLTNTIDARLIAVDADTGEFCQGFGNNGQVDLKAGLGDVPDSYYQLSSAPLMAGTTVVVG
GRVADNVQTDMPGGVIRGFDVVTGEMRWAFDPGNPEDKQAPAAGSTYVRSTPNSWAPMSY
DPAMNTVFLPMGSSSTDIYGVERTALNHKYGASVLALNATTGEEKWVYQTVHNDLWDFDL
PMQPSLIDFTKADGSKVPAVVIGTKAGQIFVLDRATGKPLTKVEEVPVKTSNIPNEPYSL
TQPKSVGMPEIGAQTLTESDMWGATPFDQLLCRISFKKMRYDGLYTAPGTDISLSFPGSL
GGMNWGGISTDPVHGFIFVNDMRLGLWIQMIAAKKDAKASSGGEALNTGMGAVPLKGTPY
AVNKNRFLSVAGIPCQAPPFGTLTAIDMKTQKVAWQVPVGTVQDTGPLGIKMHLPLPIGM
PTLGGTLSTQGGLVFIAGTQDYYLRAFNSANGKEAWKARLPVGSQGGPMTYVSPKTGKQY
VVITAGGARQSPDRGDYVIAYALPDSQ
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