SitesBLAST
Comparing WP_011653270.1 NCBI__GCF_000009265.1:WP_011653270.1 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)
27% identity, 77% coverage: 157:751/772 of query aligns to 59:571/708 of Q46444
- E101 (≠ D199) binding pyrroloquinoline quinone
- C147 (≠ M253) modified: Disulfide link with 148
- C148 (≠ P254) modified: Disulfide link with 147
- R153 (≠ S259) binding pyrroloquinoline quinone
- T198 (= T314) binding pyrroloquinoline quinone
- GA 214:215 (≠ NQ 333:334) binding pyrroloquinoline quinone
- E216 (= E335) binding Ca(2+)
- T274 (≠ N380) binding pyrroloquinoline quinone
- N294 (= N400) binding Ca(2+)
- D339 (= D444) binding Ca(2+)
- K366 (= K472) binding pyrroloquinoline quinone
- NW 425:426 (= NW 572:573) 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)
27% identity, 77% coverage: 157:751/772 of query aligns to 28:540/670 of 1kb0A
- active site: E185 (= E335), N263 (= N400), D308 (= D444)
- binding calcium ion: E185 (= E335), N263 (= N400), D308 (= D444)
- binding pyrroloquinoline quinone: E70 (≠ D199), C116 (≠ M253), C117 (≠ P254), R122 (≠ S259), T167 (= T314), G182 (≠ D332), G183 (≠ N333), A184 (≠ Q334), E185 (= E335), T243 (≠ N380), W245 (= W382), D308 (= D444), K335 (= K472), N394 (= N572), W395 (= W573), W479 (≠ F673)
- binding tetrahydrofuran-2-carboxylic acid: C116 (≠ M253), C117 (≠ P254), E185 (= E335), D308 (= D444), P389 (≠ N567)
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
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)
27% identity, 79% coverage: 144:751/772 of query aligns to 40:584/757 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
27% identity, 79% coverage: 144:751/772 of query aligns to 6:550/723 of 8gy2A
- binding calcium ion: E181 (= E335), N263 (= N400), D308 (= D444)
- binding heme c: D104 (≠ Q243)
- binding pyrroloquinoline quinone: C107 (vs. gap), C108 (vs. gap), D163 (≠ T314), G179 (≠ N333), A180 (≠ Q334), E181 (= E335), W245 (= W382), N263 (= N400), D308 (= D444), K335 (= K472), F398 (≠ W573), W489 (≠ M681)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
C5AXV8 Lanthanide-dependent ethanol dehydrogenase; Lanthanide-dependent EtDH; Ln-dependent EtDH; Lanthanide-dependent formaldehyde dehydrogenase; PQQ-dependent ethanol dehydrogenase; EC 1.1.2.-; EC 1.2.2.- from Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) (see paper)
24% identity, 81% coverage: 123:751/772 of query aligns to 7:550/587 of C5AXV8
- D319 (= D446) mutation to S: Loss of efficient ethanol oxidation with La(3+).
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
26% identity, 78% coverage: 154:754/772 of query aligns to 10:541/596 of 5xm3A
- active site: E177 (= E335), N261 (= N400), D303 (= D444)
- binding magnesium ion: E177 (= E335), N261 (= N400)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ P240), R109 (= R246), T159 (= T314), S174 (≠ D332), G175 (≠ N333), A176 (≠ Q334), E177 (= E335), T241 (≠ N380), W243 (= W382), R331 (≠ K472), N394 (= N572), W476 (≠ Y688), G539 (= G752), W540 (≠ A753)
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, 78% coverage: 152:751/772 of query aligns to 34:543/690 of Q8GR64
- E81 (≠ D199) binding pyrroloquinoline quinone
- C127 (≠ S259) modified: Disulfide link with 128
- C128 (≠ A260) modified: Disulfide link with 127
- R133 (vs. gap) binding pyrroloquinoline quinone
- T177 (= T314) binding pyrroloquinoline quinone
- GA 193:194 (≠ NQ 333:334) binding pyrroloquinoline quinone
- E195 (= E335) binding Ca(2+)
- T252 (≠ N380) binding pyrroloquinoline quinone
- N272 (= N400) binding Ca(2+)
- D317 (= D444) binding Ca(2+)
- K344 (= K472) binding pyrroloquinoline quinone
- NW 404:405 (= NW 572:573) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:22 signal peptide
- 23:690 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH IIB
- 547 binding pyrroloquinoline quinone
- 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)
26% identity, 78% coverage: 152:751/772 of query aligns to 12:521/664 of 1kv9A
- active site: E173 (= E335), N250 (= N400), D295 (= D444)
- binding acetone: E173 (= E335), D295 (= D444)
- binding calcium ion: E173 (= E335), N250 (= N400), D295 (= D444)
- binding heme c: A101 (≠ M255), R102 (≠ E256)
- binding pyrroloquinoline quinone: E59 (≠ D199), C105 (≠ S259), C106 (≠ A260), R111 (vs. gap), T155 (= T314), G170 (≠ D332), A172 (≠ Q334), E173 (= E335), T230 (≠ N380), W232 (= W382), K322 (= K472), N382 (= N572), W383 (= W573), W460 (vs. gap)
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
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
27% identity, 76% coverage: 171:754/772 of query aligns to 27:532/571 of 4aahA
- active site: E171 (= E335), N255 (= N400), D297 (= D444)
- binding calcium ion: E171 (= E335), N255 (= N400)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ R244), C104 (= C245), R109 (= R246), S168 (≠ D332), A170 (≠ Q334), E171 (= E335), W237 (= W382), R324 (≠ K472), N387 (= N572), W467 (≠ Y688), W531 (≠ A753)
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
28% identity, 48% coverage: 118:488/772 of query aligns to 11:372/718 of Q4W6G0
- C138 (= C245) modified: Disulfide link with 139
- C139 (vs. gap) modified: Disulfide link with 138
- R144 (= R246) binding pyrroloquinoline quinone
- T189 (= T314) binding pyrroloquinoline quinone
- GA 205:206 (≠ NQ 333:334) binding pyrroloquinoline quinone
- E207 (= E335) binding Ca(2+)
- T264 (≠ N380) binding pyrroloquinoline quinone
- N284 (= N400) binding Ca(2+)
- D329 (= D444) binding Ca(2+)
- K356 (= K472) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:29 signal peptide
- 30:718 modified: mature protein, Quinohemoprotein alcohol dehydrogenase ADH-IIG
- 415 binding substrate
- 419:420 binding pyrroloquinoline quinone
- 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)
29% identity, 45% coverage: 141:488/772 of query aligns to 5:343/684 of 1yiqA
- active site: E178 (= E335), N255 (= N400), D300 (= D444)
- binding calcium ion: E178 (= E335), N255 (= N400), D300 (= D444)
- binding pyrroloquinoline quinone: E63 (≠ Q200), C109 (= C245), C110 (vs. gap), R115 (= R246), T160 (= T314), G175 (≠ D332), G176 (≠ N333), A177 (≠ Q334), E178 (= E335), T235 (≠ N380), W237 (= W382), K327 (= K472)
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: 390, 391, 477, 542
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
25% identity, 78% coverage: 154:754/772 of query aligns to 10:541/600 of 1lrwA
- active site: E177 (= E335), N261 (= N400), D303 (= D444)
- binding calcium ion: E177 (= E335), N261 (= N400), D303 (= D444)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ R244), C104 (= C245), R109 (= R246), T159 (= T314), S174 (≠ D332), G175 (≠ N333), A176 (≠ Q334), E177 (= E335), T241 (≠ N380), W243 (= W382), R331 (≠ K472), W476 (≠ Y688), W540 (≠ A753)
P12293 Methanol dehydrogenase [cytochrome c] subunit 1; MDH large subunit alpha; MEDH; EC 1.1.2.7 from Paracoccus denitrificans (see 2 papers)
25% identity, 78% coverage: 154:754/772 of query aligns to 42:572/631 of P12293
- C135 (≠ R244) modified: Disulfide link with 136
- C136 (= C245) modified: Disulfide link with 135
- C418 (≠ Q564) modified: Disulfide link with 447
- C447 (≠ S594) modified: Disulfide link with 418
Sites not aligning to the query:
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
27% identity, 80% coverage: 154:770/772 of query aligns to 10:563/563 of 6damA
- active site: E171 (= E335), N259 (= N400), D301 (= D444)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ R244), C104 (= C245), R109 (= R246), T153 (= T314), S168 (≠ D332), G169 (≠ N333), G170 (≠ Q334), E171 (= E335), T239 (≠ N380), W241 (= W382), D303 (= D446), R328 (≠ K472), N394 (= N572), W480 (≠ Y688), G543 (= G752), W544 (vs. gap)
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 78% coverage: 154:752/772 of query aligns to 10:544/588 of 7o6zB
- binding methanol: E173 (= E335), W263 (vs. gap), D314 (= D444)
- binding Neodymium Ion: E173 (= E335), N259 (= N400), D314 (= D444), D316 (= D446)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C105 (≠ P240), C106 (≠ Y241), R111 (= R246), T155 (= T314), G170 (≠ D332), G171 (≠ N333), D172 (≠ Q334), E173 (= E335), W241 (= W382), D316 (= D446), R341 (≠ K472), D403 (≠ N572), W481 (≠ Y688), G544 (= G752)
Sites not aligning to the query:
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
24% identity, 78% coverage: 154:752/772 of query aligns to 10:544/588 of 7o6zA
Sites not aligning to the query:
C5B120 Lanthanide-dependent methanol dehydrogenase; Lanthanide-dependent MDH; Ln(3+)-dependent MDH; La(3+)- and PQQ-dependent MDH; La(3+)-dependent methanol dehydrogenase; La(3+)-dependent MDH; EC 1.1.2.10 from Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) (see 2 papers)
27% identity, 76% coverage: 166:752/772 of query aligns to 43:557/601 of C5B120
- R130 (= R246) binding pyrroloquinoline quinone
- T174 (= T314) binding pyrroloquinoline quinone
- S189 (≠ D332) binding pyrroloquinoline quinone
- G190 (≠ N333) binding pyrroloquinoline quinone
- G191 (≠ Q334) binding pyrroloquinoline quinone
- E192 (= E335) binding La(3+)
- W258 (vs. gap) binding pyrroloquinoline quinone
- N276 (= N400) binding La(3+)
- D318 (= D444) binding La(3+)
- D320 (= D446) binding La(3+); mutation to A: Loss of methanol dehydrogenase activity. In contrast to wild-type, the mutant cells are incapable of growth with methanol and La(3+). The mutant protein is unable to bind La(3+) and is loaded with Ca(2+) regardless of whether or not La(3+) is included in the growth medium, but is inactive.
- R345 (≠ K472) binding pyrroloquinoline quinone
- W494 (≠ Y688) binding pyrroloquinoline quinone
Sites not aligning to the query:
- 1:21 signal peptide
- 558 binding pyrroloquinoline quinone
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
27% identity, 76% coverage: 166:752/772 of query aligns to 22:536/579 of 6oc6A
- active site: E171 (= E335), N255 (= N400), D297 (= D444)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C103 (≠ R244), C104 (= C245), R109 (= R246), T153 (= T314), S168 (≠ D332), G169 (≠ N333), G170 (≠ Q334), E171 (= E335), W237 (vs. gap), D299 (= D446), R324 (≠ K472), D395 (≠ I562), W473 (≠ Y688), G536 (= G752)
Sites not aligning to the query:
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
27% identity, 43% coverage: 153:484/772 of query aligns to 9:343/597 of 2d0vA
- active site: E177 (= E335), N261 (= N400), D303 (= D444)
- binding calcium ion: E177 (= E335), N261 (= N400), D303 (= D444)
- binding pyrroloquinoline quinone: E55 (≠ Q200), R109 (= R246), T159 (= T314), S174 (≠ D332), G175 (≠ N333), A176 (≠ Q334), E177 (= E335), T241 (≠ N380), W243 (= W382), R331 (≠ K472)
Sites not aligning to the query:
6fkwA Europium-containing methanol dehydrogenase (see paper)
28% identity, 44% coverage: 150:491/772 of query aligns to 6:344/576 of 6fkwA
- active site: E172 (= E335), N256 (≠ T402), D299 (= D444), D301 (= D446)
- binding europium ion: E172 (= E335), N256 (≠ T402), D299 (= D444), D301 (= D446)
- binding pyrroloquinoline quinone: E55 (≠ Q200), C104 (≠ R244), C105 (= C245), R110 (= R246), T154 (= T308), S169 (≠ D332), G170 (≠ N333), G171 (≠ Q334), E172 (= E335), T236 (≠ N380), W238 (= W382), D301 (= D446), R326 (≠ K472)
Sites not aligning to the query:
Query Sequence
>WP_011653270.1 NCBI__GCF_000009265.1:WP_011653270.1
MKFLATLFCIVLALIGLGLIGGGAWLLRLGGSPYYAAVGLAYLVAALLLWRRKTRGALIV
LLVAVFTLPWALWESGLNFWALFARLMSPIALAGFALLFAPSLSPTANRKLFYGGALVTA
LIFATGFGLSFVPHGIIQPSADITAYKTAKGDNSPSDWTSYGRTTAGDRYSPFDQINRGN
VSKLDLAWTYRTGKGDGADQNTPLQIGDTVYTCTPTDVIAALDADTGKPRWTFDPKATAP
YWQRCRGLGYYKMPMEAQSADGLCNERLVQTTIDARLLAIDSKTGAPCKDFGDNGTVQLS
QGMGEVKTGYYFQTSAPLIARNLIVVGGWVTDNQEVGEPSGVIRAFNVVTGELEWAWDLG
NPEITKLPPEGQTYTRATPNMWTTAAFDDKLGLIYAPLGNTTPDYYGVNRPAFADQYNAT
LVALDVTTGREKWKFQTVHHDIWDYDLPAQPVLVDLPDGNGVTVPALLQTTKRGQLFLLD
RRTGTPLAEVQEKPVPQQGGVPEEKLSPTQPYSVGMPTIGAERVTEQTAWGLTIFDQLAC
RIAFRKMRYDGDFTPIGTQYAIQQPGNLGGLNWGSVSVDLPNNRVFMNDIRVPSLFALIP
REEYVDFALTTTAHGPSAPQRGTPYAMATEMWTSRLRVPCTQPPFGTVTAVDLKTRKIAW
QVPAGTAEELGPFKIKTKLPMPMGLPSYAGTSATAGGVVFFAGFQDYYIRAYDAENGTEL
WKYPLPVGSSATPMTYVSPKTGKQYVLISVGGAPYSKDVGDYVLAFSLKNRD
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