SitesBLAST
Comparing BWI76_RS13270 FitnessBrowser__Koxy:BWI76_RS13270 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)
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, 82% coverage: 125:769/790 of query aligns to 5:567/718 of Q4W6G0
- C138 (≠ V274) modified: Disulfide link with 139
- C139 (≠ S275) modified: Disulfide link with 138
- R144 (≠ A280) binding
- T189 (= T335) binding
- GA 205:206 (≠ VA 351:352) binding
- E207 (≠ D353) binding
- T264 (≠ N401) binding
- N284 (= N421) binding
- D329 (= D465) binding
- K356 (= K493) binding
- W415 (≠ L588) binding
- DW 419:420 (≠ NW 592:593) 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)
28% identity, 77% coverage: 159:769/790 of query aligns to 13:538/684 of 1yiqA
- active site: E178 (≠ D353), N255 (= N421), D300 (= D465)
- binding calcium ion: E178 (≠ D353), N255 (= N421), D300 (= D465)
- binding pyrroloquinoline quinone: E63 (= E214), C109 (≠ V274), C110 (≠ S275), R115 (≠ A280), T160 (= T335), G175 (≠ R350), G176 (≠ V351), A177 (= A352), E178 (≠ D353), T235 (≠ N401), W237 (= W403), K327 (= K493), D390 (≠ N592), W391 (= W593), F477 (≠ E686)
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)
28% identity, 77% coverage: 160:769/790 of query aligns to 32:543/690 of Q8GR64
- E81 (≠ G212) binding
- C127 (≠ V274) modified: Disulfide link with 128
- C128 (≠ S275) modified: Disulfide link with 127
- R133 (≠ A280) binding
- T177 (= T335) binding
- GA 193:194 (≠ VA 351:352) binding
- E195 (≠ D353) binding
- T252 (≠ N401) binding
- N272 (= N421) binding
- D317 (= D465) binding
- K344 (= K493) binding
- NW 404:405 (= NW 592:593) 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)
28% identity, 77% coverage: 160:769/790 of query aligns to 10:521/664 of 1kv9A
- active site: E173 (≠ D353), N250 (= N421), D295 (= D465)
- binding acetone: E173 (≠ D353), D295 (= D465)
- binding calcium ion: E173 (≠ D353), N250 (= N421), D295 (= D465)
- binding heme c: A101 (≠ S270), R102 (≠ Q271)
- binding pyrroloquinoline quinone: E59 (≠ G212), C105 (≠ V274), C106 (≠ S275), R111 (≠ A280), T155 (= T335), G170 (≠ R350), A172 (= A352), E173 (≠ D353), T230 (≠ N401), W232 (= W403), K322 (= K493), N382 (= N592), W383 (= W593), W460 (≠ E686)
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
6fkwA Europium-containing methanol dehydrogenase (see paper)
27% identity, 77% coverage: 164:769/790 of query aligns to 17:528/576 of 6fkwA
- active site: E172 (= E359), N256 (= N421), D299 (= D465), D301 (= D467)
- binding europium ion: E172 (= E359), N256 (= N421), D299 (= D465), D301 (= D467)
- binding pyrroloquinoline quinone: E55 (≠ N209), C104 (≠ A277), C105 (≠ A278), R110 (vs. gap), T154 (≠ A329), S169 (= S356), G170 (≠ T357), G171 (= G358), E172 (= E359), T236 (≠ N401), W238 (= W403), D301 (= D467), R326 (≠ K493), D388 (≠ N592), W467 (≠ P700)
Sites not aligning to the query:
4maeA Methanol dehydrogenase from methylacidiphilum fumariolicum solv (see paper)
27% identity, 77% coverage: 164:769/790 of query aligns to 17:528/577 of 4maeA
- active site: E172 (= E359), N256 (= N421), D299 (= D465)
- binding cerium (iii) ion: E172 (= E359), N256 (= N421), D299 (= D465), D301 (= D467)
- binding pyrroloquinoline quinone: E55 (≠ N209), C104 (≠ A277), C105 (≠ A278), R110 (vs. gap), T154 (≠ A329), S169 (= S356), G170 (≠ T357), G171 (= G358), E172 (= E359), T236 (≠ N401), W238 (= W403), D301 (= D467), R326 (≠ K493), D388 (≠ N592), W467 (≠ P700)
Sites not aligning to the query:
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
26% identity, 76% coverage: 167:769/790 of query aligns to 13:540/563 of 6damA
- active site: E171 (= E359), N259 (= N421), D301 (= D465)
- binding pyrroloquinoline quinone: E55 (≠ N209), C103 (= C261), C104 (vs. gap), R109 (= R262), T153 (= T335), S168 (= S356), G169 (≠ T357), G170 (= G358), E171 (= E359), T239 (≠ N401), W241 (= W403), D303 (= D467), R328 (≠ K493), N394 (= N592), W480 (≠ P700)
Sites not aligning to the query:
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
27% identity, 77% coverage: 163:769/790 of query aligns to 9:541/588 of 7o6zB
- binding methanol: E173 (≠ N354), W263 (vs. gap), D314 (= D465)
- binding Neodymium Ion: E173 (≠ N354), N259 (= N421), D314 (= D465), D316 (= D467)
- binding pyrroloquinoline quinone: E55 (= E214), C105 (≠ A277), C106 (≠ A278), R111 (≠ A283), T155 (= T335), G170 (≠ V351), G171 (≠ A352), D172 (= D353), E173 (≠ N354), W241 (= W403), D316 (= D467), R341 (≠ K493), D403 (≠ N592), W481 (≠ L706)
Sites not aligning to the query:
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
27% identity, 77% coverage: 163:769/790 of query aligns to 9:541/588 of 7o6zA
Sites not aligning to the query:
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
27% identity, 75% coverage: 179:769/790 of query aligns to 25:533/579 of 6oc6A
- active site: E171 (= E359), N255 (= N421), D297 (= D465)
- binding pyrroloquinoline quinone: E55 (≠ N209), C103 (= C261), C104 (vs. gap), R109 (= R262), T153 (= T335), S168 (= S356), G169 (≠ T357), G170 (= G358), E171 (= E359), W237 (= W403), D299 (= D467), R324 (≠ K493), D395 (≠ N592), W473 (≠ L706)
Sites not aligning to the query:
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
26% identity, 74% coverage: 183:764/790 of query aligns to 29:522/571 of 4aahA
- active site: E171 (≠ D353), N255 (= N421), D297 (= D465)
- binding calcium ion: E171 (≠ D353), N255 (= N421)
- binding pyrroloquinoline quinone: E55 (≠ N209), C103 (≠ V274), C104 (≠ S275), R109 (≠ A280), S168 (≠ R350), A170 (= A352), E171 (≠ D353), W237 (= W403), R324 (≠ K493), N387 (= N592), W467 (≠ L706)
Sites not aligning to the query:
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, 75% coverage: 179:769/790 of query aligns to 71:571/708 of Q46444
- E101 (≠ G212) binding
- C147 (≠ Y267) modified: Disulfide link with 148
- C148 (≠ E268) modified: Disulfide link with 147
- R153 (≠ A280) binding
- T198 (= T335) binding
- GA 214:215 (≠ VA 351:352) binding
- E216 (≠ D353) binding
- T274 (≠ N401) binding
- N294 (= N421) binding
- D339 (= D465) binding
- K366 (= K493) binding
- NW 425:426 (= NW 592:593) 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
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
25% identity, 78% coverage: 157:769/790 of query aligns to 3:536/596 of 5xm3A
- active site: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding magnesium ion: E177 (≠ P360), N261 (= N421)
- binding pyrroloquinoline quinone: E55 (≠ N209), C103 (= C261), R109 (= R262), T159 (= T335), S174 (≠ T357), G175 (= G358), A176 (≠ E359), E177 (≠ P360), T241 (≠ N401), W243 (= W403), R331 (≠ K493), N394 (= N592), W476 (≠ L706)
Sites not aligning to the query:
1kb0A Crystal structure of quinohemoprotein alcohol dehydrogenase from comamonas testosteroni (see paper)
26% identity, 75% coverage: 179:769/790 of query aligns to 40:540/670 of 1kb0A
- active site: E185 (≠ D353), N263 (= N421), D308 (= D465)
- binding calcium ion: E185 (≠ D353), N263 (= N421), D308 (= D465)
- binding pyrroloquinoline quinone: E70 (≠ G212), C116 (≠ Y267), C117 (≠ E268), R122 (≠ A280), T167 (= T335), G182 (≠ R350), G183 (≠ V351), A184 (= A352), E185 (≠ D353), T243 (≠ N401), W245 (= W403), D308 (= D465), K335 (= K493), N394 (= N592), W395 (= W593), W479 (≠ L691)
- binding tetrahydrofuran-2-carboxylic acid: C116 (≠ Y267), C117 (≠ E268), E185 (≠ D353), D308 (= D465), P389 (≠ S587)
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
1flgA Crystal structure of the quinoprotein ethanol dehydrogenase from pseudomonas aeruginosa (see paper)
24% identity, 76% coverage: 170:769/790 of query aligns to 20:549/582 of 1flgA
- active site: E179 (≠ N354), N266 (= N421), D316 (= D465)
- binding calcium ion: E179 (≠ N354), N266 (= N421), D316 (= D465)
- binding pyrroloquinoline quinone: E61 (= E214), C105 (≠ V274), C106 (≠ S275), R111 (≠ A280), T155 (≠ Q334), S176 (≠ V351), G177 (≠ A352), D178 (= D353), W248 (= W403), R344 (≠ K493), N413 (= N592), W414 (= W593), W489 (≠ P700)
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, 76% coverage: 170:769/790 of query aligns to 54:583/623 of Q9Z4J7
- E95 (= E214) binding
- C139 (≠ R260) modified: Disulfide link with 140
- CC 139:140 (≠ RC 260:261) 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 (= C261) modified: Disulfide link with 139
- R145 (= R262) binding
- T189 (≠ Q334) binding
- HGS 207:209 (≠ GGR 348:350) binding
- E213 (≠ N354) binding
- N300 (= N421) binding
- D350 (= D465) binding
- R378 (≠ K493) binding
- W523 (≠ P700) binding
Sites not aligning to the query:
- 1:34 signal peptide
- 45 binding
- 48 binding
- 51 binding
- 587 binding
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
26% identity, 78% coverage: 157:769/790 of query aligns to 3:536/597 of 2d0vA
- active site: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding calcium ion: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding pyrroloquinoline quinone: E55 (≠ N209), R109 (= R262), T159 (= T335), S174 (≠ T357), G175 (= G358), A176 (≠ E359), E177 (≠ P360), T241 (≠ N401), W243 (= W403), R331 (≠ K493), N394 (= N592), W476 (≠ L706)
Sites not aligning to the query:
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
26% identity, 77% coverage: 163:769/790 of query aligns to 9:529/573 of 7ce5A
- active site: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding calcium ion: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding methanol: E177 (≠ P360)
- binding pyrroloquinoline quinone: E55 (≠ N209), C103 (= C261), C104 (vs. gap), R109 (= R262), T159 (≠ A329), A174 (≠ T357), G175 (= G358), A176 (≠ E359), E177 (≠ P360), T241 (≠ N401), W243 (= W403), R330 (≠ K493), N393 (= N592), W469 (≠ L706)
Sites not aligning to the query:
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
26% identity, 77% coverage: 163:769/790 of query aligns to 9:529/573 of 7cdlC
- active site: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding calcium ion: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding pyrroloquinoline quinone: E55 (≠ N209), R109 (= R262), T159 (≠ A329), A174 (≠ T357), A176 (≠ E359), E177 (≠ P360), T241 (≠ N401), W243 (= W403), D303 (= D465), R330 (≠ K493), N393 (= N592), W469 (≠ L706)
Sites not aligning to the query:
1lrwA Crystal structure of methanol dehydrogenase from p. Denitrificans (see paper)
25% identity, 76% coverage: 167:769/790 of query aligns to 13:536/600 of 1lrwA
- active site: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding calcium ion: E177 (≠ P360), N261 (= N421), D303 (= D465)
- binding pyrroloquinoline quinone: E55 (≠ N209), C103 (≠ R260), C104 (= C261), R109 (= R262), T159 (= T335), S174 (≠ T357), G175 (= G358), A176 (≠ E359), E177 (≠ P360), T241 (≠ N401), W243 (= W403), R331 (≠ K493), W476 (≠ L706)
Sites not aligning to the query:
Query Sequence
>BWI76_RS13270 FitnessBrowser__Koxy:BWI76_RS13270
MATDNAPRGFPRILQWLLAGLMLIIGLAIGILGAKLASVGGTFYFALMGLVMVIAAVLIF
RSRRGGIMLYAVAFVASIVWAISDAGWTYWPLFSRLFALGVLAFLCALVWPFLSRQPAKK
GPAFGLAAVIAVALLVSFAWMFKSQPLVSASEAVPVKPVAADEQQKNWAHWGNTTHGDRF
AALDQINKQNVDQLQVAWIAHTGDIPQSNGSGAEDQNTPLQIGDTLYVCTPYSKVLALDV
DSGKEKWRYDSKATAPNWQRCRGLGYYEDSQAQVSPAADAQPAACSRRLFLPTTDARLIA
IDADNGKLCDAFGDHGIVDLSIGMGEIKAGYYQQTSTPLVAGNVVVVGGRVADNFSTGEP
PGVVRAYDVHTGKLAWAWDPGNPALTGEPPAGQTYTRGTPNVWSAMSYDAKLNLIYLPTG
NATPDFFGGERTALDDKYSSSIVAVDATTGQVRWHYQTTHHDLWDFDLPSQPLLYDLPDG
KGGTTPVLVQTSKQGMIFMLNRATGEPVAKVEERPVPAGNVKGERYSPTQPYSVGMPMIG
NETLTESDMWGATPVDLLLCRIQFKEMRHQGVFTPPGEDRSLQYPGSLGGMNWGSVSVDP
NNSLIFVNDMRLGLANYMVPRAKVAKDASGIEMGIVPMEGTPFGAMRERFLSPLGIPCQK
PPFGTLSAVDLKTGKLVWQVPVGTVEDTGPLGIRMHMPIPIGMPTLGASLSTQSGLLFFA
GTQDFYLRAFDTANGKEIWKSRLPVGSQSGPMTYVSPKTGKQYIIINAGGARQSPDRGDY
IIAYALPEQK
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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