SitesBLAST
Comparing BWI76_RS16705 FitnessBrowser__Koxy:BWI76_RS16705 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)
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)
25% identity, 78% coverage: 159:782/801 of query aligns to 47:571/708 of Q46444
- E101 (= E219) binding
- C147 (vs. gap) modified: Disulfide link with 148
- C148 (vs. gap) modified: Disulfide link with 147
- R153 (= R265) binding
- T198 (= T342) binding
- GA 214:215 (≠ DI 360:361) binding
- E216 (≠ V362) binding
- T274 (vs. gap) binding
- N294 (= N427) binding
- D339 (= D471) binding
- K366 (= K499) binding
- NW 425:426 (= NW 598:599) 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)
25% identity, 79% coverage: 154:782/801 of query aligns to 11:540/670 of 1kb0A
- active site: E185 (≠ R359), N263 (= N427), D308 (= D471)
- binding calcium ion: E185 (≠ R359), N263 (= N427), D308 (= D471)
- binding pyrroloquinoline quinone: E70 (= E219), C116 (vs. gap), C117 (vs. gap), R122 (= R265), T167 (≠ E334), G182 (= G356), G183 (≠ W357), A184 (≠ V358), E185 (≠ R359), T243 (vs. gap), W245 (vs. gap), D308 (= D471), K335 (= K499), N394 (= N598), W395 (= W599), W479 (≠ L719)
- binding tetrahydrofuran-2-carboxylic acid: C116 (vs. gap), C117 (vs. gap), E185 (≠ R359), D308 (= D471), P389 (≠ L593)
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
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
25% identity, 79% coverage: 165:799/801 of query aligns to 7:561/563 of 6damA
- active site: E171 (= E365), N259 (= N427), D301 (= D471)
- binding pyrroloquinoline quinone: E55 (= E219), C103 (= C264), C104 (vs. gap), R109 (= R265), T153 (= T333), S168 (≠ V362), G169 (≠ H363), G170 (= G364), E171 (= E365), T239 (≠ N407), W241 (= W409), D303 (= D473), R328 (≠ K499), N394 (= N598), W480 (≠ L719), G543 (vs. gap), W544 (vs. gap)
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
25% identity, 78% coverage: 160:782/801 of query aligns to 2:536/597 of 2d0vA
- active site: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding calcium ion: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding pyrroloquinoline quinone: E55 (= E219), R109 (= R265), T159 (= T333), S174 (≠ W357), G175 (≠ V358), A176 (≠ R359), E177 (≠ D360), T241 (vs. gap), W243 (vs. gap), R331 (≠ K499), N394 (= N598), W476 (≠ L719)
Sites not aligning to the query:
1kv9A Structure at 1.9 a resolution of a quinohemoprotein alcohol dehydrogenase from pseudomonas putida hk5 (see paper)
25% identity, 76% coverage: 171:782/801 of query aligns to 17:521/664 of 1kv9A
- active site: E173 (≠ R359), N250 (= N427), D295 (= D471)
- binding acetone: E173 (≠ R359), D295 (= D471)
- binding calcium ion: E173 (≠ R359), N250 (= N427), D295 (= D471)
- binding heme c: A101 (≠ H261), R102 (≠ V262)
- binding pyrroloquinoline quinone: E59 (= E219), C105 (≠ A280), C106 (≠ E281), R111 (≠ P286), T155 (= T342), G170 (= G356), A172 (≠ V358), E173 (≠ R359), T230 (vs. gap), W232 (vs. gap), K322 (= K499), N382 (= N598), W383 (= W599), W460 (≠ M710)
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
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, 76% coverage: 171:782/801 of query aligns to 39:543/690 of Q8GR64
- E81 (= E219) binding
- C127 (≠ A280) modified: Disulfide link with 128
- C128 (≠ E281) modified: Disulfide link with 127
- R133 (≠ P286) binding
- T177 (= T342) binding
- GA 193:194 (≠ WV 357:358) binding
- E195 (≠ R359) binding
- T252 (vs. gap) binding
- N272 (= N427) binding
- D317 (= D471) binding
- K344 (= K499) binding
- NW 404:405 (= NW 598:599) 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
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, 76% coverage: 171:782/801 of query aligns to 50:567/718 of Q4W6G0
- C138 (vs. gap) modified: Disulfide link with 139
- C139 (vs. gap) modified: Disulfide link with 138
- R144 (≠ P286) binding
- T189 (= T342) binding
- GA 205:206 (≠ WV 357:358) binding
- E207 (≠ R359) binding
- T264 (vs. gap) binding
- N284 (= N427) binding
- D329 (= D471) binding
- K356 (= K499) binding
- W415 (≠ L594) binding
- DW 419:420 (≠ NW 598:599) 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
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, 76% coverage: 171:782/801 of query aligns to 21:538/684 of 1yiqA
- active site: E178 (≠ R359), N255 (= N427), D300 (= D471)
- binding calcium ion: E178 (≠ R359), N255 (= N427), D300 (= D471)
- binding pyrroloquinoline quinone: E63 (= E219), C109 (vs. gap), C110 (vs. gap), R115 (≠ P286), T160 (= T342), G175 (= G356), G176 (≠ W357), A177 (≠ V358), E178 (≠ R359), T235 (vs. gap), W237 (= W409), K327 (= K499), D390 (≠ N598), W391 (= W599), F477 (≠ E699)
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
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: 162:782/801 of query aligns to 38:584/757 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: 162:782/801 of query aligns to 4:550/723 of 8gy2A
- binding calcium ion: E181 (≠ D360), N263 (= N427), D308 (= D471)
- binding heme c: D104 (≠ E260)
- binding pyrroloquinoline quinone: C107 (≠ T263), C108 (= C264), D163 (≠ T342), G179 (≠ V358), A180 (≠ R359), E181 (≠ D360), W245 (= W409), N263 (= N427), D308 (= D471), K335 (= K499), F398 (≠ W599), W489 (≠ T718)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
29% identity, 43% coverage: 178:524/801 of query aligns to 20:349/579 of 6oc6A
- active site: E171 (≠ W357), N255 (= N427), D297 (= D471)
- binding pyrroloquinoline quinone: E55 (= E219), C103 (= C264), C104 (vs. gap), R109 (= R265), T153 (≠ S336), S168 (≠ L354), G169 (= G355), G170 (= G356), E171 (≠ W357), W237 (vs. gap), D299 (= D473), R324 (≠ K499)
Sites not aligning to the query:
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 78% coverage: 160:782/801 of query aligns to 2:541/588 of 7o6zB
- binding methanol: E173 (≠ I361), W263 (= W433), D314 (= D471)
- binding Neodymium Ion: E173 (≠ I361), N259 (= N427), D314 (= D471), D316 (= D473)
- binding pyrroloquinoline quinone: E55 (= E219), C105 (= C264), C106 (vs. gap), R111 (= R265), T155 (= T344), G170 (≠ V358), G171 (≠ R359), D172 (= D360), E173 (≠ I361), W241 (= W409), D316 (= D473), R341 (≠ K499), D403 (≠ N598), W481 (≠ L719)
Sites not aligning to the query:
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 78% coverage: 160:782/801 of query aligns to 2:541/588 of 7o6zA
Sites not aligning to the query:
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
28% identity, 44% coverage: 160:515/801 of query aligns to 2:347/596 of 5xm3A
- active site: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding magnesium ion: E177 (≠ D360), N261 (= N427)
- binding pyrroloquinoline quinone: E55 (= E219), C103 (= C264), R109 (= R265), T159 (= T342), S174 (≠ W357), G175 (≠ V358), A176 (≠ R359), E177 (≠ D360), T241 (vs. gap), W243 (vs. gap), R331 (≠ K499)
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)
27% identity, 45% coverage: 158:515/801 of query aligns to 32:379/631 of P12293
- C135 (= C264) modified: Disulfide link with 136
- C136 (vs. gap) 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
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
24% identity, 74% coverage: 185:777/801 of query aligns to 27:522/571 of 4aahA
- active site: E171 (≠ V353), N255 (= N427), D297 (= D471)
- binding calcium ion: E171 (≠ V353), N255 (= N427)
- binding pyrroloquinoline quinone: E55 (= E219), C103 (≠ Y269), C104 (≠ Y270), R109 (≠ P286), S168 (≠ H350), A170 (= A352), E171 (≠ V353), W237 (= W409), R324 (≠ K499), N387 (= N598), W467 (≠ L719)
Sites not aligning to the query:
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
27% identity, 44% coverage: 160:515/801 of query aligns to 2:347/600 of 1lrwA
- active site: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding calcium ion: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding pyrroloquinoline quinone: E55 (= E219), C103 (= C264), C104 (vs. gap), R109 (= R265), T159 (= T342), S174 (≠ W357), G175 (≠ V358), A176 (≠ R359), E177 (≠ D360), T241 (vs. gap), W243 (vs. gap), R331 (≠ K499)
Sites not aligning to the query:
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
28% identity, 44% coverage: 165:515/801 of query aligns to 7:346/573 of 7ce5A
- active site: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding calcium ion: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding methanol: E177 (≠ D360)
- binding pyrroloquinoline quinone: E55 (= E219), C103 (= C264), C104 (vs. gap), R109 (= R265), T159 (= T342), A174 (≠ W357), G175 (≠ V358), A176 (≠ R359), E177 (≠ D360), T241 (vs. gap), W243 (vs. gap), R330 (≠ K499)
Sites not aligning to the query:
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
28% identity, 44% coverage: 165:515/801 of query aligns to 7:346/573 of 7cdlC
- active site: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding calcium ion: E177 (≠ D360), N261 (= N427), D303 (= D471)
- binding pyrroloquinoline quinone: E55 (= E219), R109 (= R265), T159 (= T342), A174 (≠ W357), A176 (≠ R359), E177 (≠ D360), T241 (vs. gap), W243 (vs. gap), D303 (= D471), R330 (≠ K499)
Sites not aligning to the query:
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)
24% identity, 77% coverage: 175:794/801 of query aligns to 55:595/623 of Q9Z4J7
- E95 (= E219) binding
- C139 (≠ T263) modified: Disulfide link with 140
- CC 139:140 (≠ TC 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 (= T342) binding
- HG-----S 207:209 (≠ GGWVRDIV 355:362) binding
- E213 (≠ P366) binding
- N300 (= N427) binding
- D350 (= D471) binding
- R378 (≠ K499) binding
- W523 (≠ L719) binding
- A587 (≠ H786) binding
Sites not aligning to the query:
- 1:34 signal peptide
- 45 binding
- 48 binding
- 51 binding
Query Sequence
>BWI76_RS16705 FitnessBrowser__Koxy:BWI76_RS16705
MDERQGSGRGVFFTVYRLLFVLLSFGIGLFFTLWGGKLLSLGGSAWYLLAGLAYLLIAVG
YLIRSRYVLPFAILTFLLTLCWALYEVQFSYWGLIPRLVVPALMLMLALWLAATLPMRPA
RRRYANWSASAIFLVLLATLVSAFYPHGAIHNGVVNASGDATPTLASKSDNWAFFGRDAS
GTRFAPYDEITPQNVKNLKVAWTYHTGRRLTGAGIGVDENTPLQIGDTLYSCTPLNVVTA
LDADTGKARWRFDPHAGTAEHVTCRGVGYYDVQSDDSLSAEEKASPALLQCPQRILVSTV
DARLIALNAKTGEPCDDFGDHGSVDLKQGMDNTENSKRYHPTSTPVIMGHIAVLGGWVRD
IVHGEPSGVVRAFDVRNGNVVWAWDVGQPENVTDPVKGRVYTLETPNVWTVPGFDKELNL
IYLPTGNGPPDYWGGDRNAAKEKYGSSVVAVDASTGETKWVFQTVHHDIWDYDLPSQPVL
FHMKNERGEEVPVLIQTTKTGQIYVLDRRTGKPVTRVEERPVAHDGAEGEHLSATQPFST
GMPQLGVEPLTEKSMWGVTPFDQLMCRIDFKESTYLGMYTPPSEKPYIEWPSLLGGMNWG
GITIDERTGTLFVNDMRMPLRMSLVRKEDMAKYKVSTDEVPGFMGTVRPQIAGPYGGVRI
DILQSALGVPCNTPPFGTMSAIDLNTRQLMWQVPMGSVEDTGPLGLKTHMHIPLGMPTLG
GPTSTASGLVFFAGTQDNYLRALDSATGKELWRARLPVGAVAAPLIYKSPKTGKEYVVIS
AGGASHSPDVGDDIIAFALEE
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