SitesBLAST
Comparing PfGW456L13_4805 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4805 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)
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, 78% coverage: 154:783/803 of query aligns to 24:543/690 of Q8GR64
- E81 (= E221) binding
- C127 (≠ F267) modified: Disulfide link with 128
- C128 (≠ A268) modified: Disulfide link with 127
- R133 (= R273) binding
- T177 (= T355) binding
- GA 193:194 (≠ ES 375:376) binding
- E195 (≠ T377) binding
- T252 (≠ N421) binding
- N272 (= N441) binding
- D317 (= D485) binding
- K344 (= K512) binding
- NW 404:405 (= NW 609:610) 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, 78% coverage: 154:783/803 of query aligns to 2:521/664 of 1kv9A
- active site: E173 (≠ T377), N250 (= N441), D295 (= D485)
- binding acetone: E173 (≠ T377), D295 (= D485)
- binding calcium ion: E173 (≠ T377), N250 (= N441), D295 (= D485)
- binding heme c: A101 (≠ G263), R102 (≠ F264)
- binding pyrroloquinoline quinone: E59 (= E221), C105 (≠ F267), C106 (≠ A268), R111 (= R273), T155 (= T355), G170 (≠ N374), A172 (≠ S376), E173 (≠ T377), T230 (≠ N421), W232 (= W423), K322 (= K512), N382 (= N609), W383 (= W610), W460 (≠ S720)
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
6damA Crystal structure of lanthanide-dependent methanol dehydrogenase xoxf from methylomicrobium buryatense 5g (see paper)
27% identity, 79% coverage: 171:801/803 of query aligns to 13:561/563 of 6damA
- active site: E171 (= E375), N259 (= N441), D301 (= D485)
- binding pyrroloquinoline quinone: E55 (= E221), C103 (≠ A268), C104 (≠ H269), R109 (= R273), T153 (= T355), S168 (≠ T372), G169 (≠ D373), G170 (≠ N374), E171 (= E375), T239 (≠ N421), W241 (= W423), D303 (= D487), R328 (≠ K512), N394 (= N609), W480 (≠ D706), G543 (= G786), W544 (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)
27% identity, 77% coverage: 171:789/803 of query aligns to 59:577/708 of Q46444
- E101 (= E221) binding
- C147 (≠ F267) modified: Disulfide link with 148
- C148 (≠ A268) modified: Disulfide link with 147
- R153 (= R273) binding
- T198 (= T355) binding
- GA 214:215 (≠ VT 371:372) binding
- E216 (≠ D373) binding
- T274 (≠ N421) binding
- N294 (= N441) binding
- D339 (= D485) binding
- K366 (= K512) binding
- NW 425:426 (= NW 609:610) binding
- V575 (≠ S787) 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)
27% identity, 77% coverage: 171:789/803 of query aligns to 28:546/670 of 1kb0A
- active site: E185 (≠ T377), N263 (= N441), D308 (= D485)
- binding calcium ion: E185 (≠ T377), N263 (= N441), D308 (= D485)
- binding pyrroloquinoline quinone: E70 (= E221), C116 (≠ F267), C117 (≠ A268), R122 (= R273), T167 (= T355), G182 (≠ N374), G183 (≠ E375), A184 (≠ S376), E185 (≠ T377), T243 (≠ N421), W245 (= W423), D308 (= D485), K335 (= K512), N394 (= N609), W395 (= W610), W479 (≠ S720), G543 (= G786), V544 (≠ S787)
- binding tetrahydrofuran-2-carboxylic acid: C116 (≠ F267), C117 (≠ A268), E185 (≠ T377), D308 (= D485), P389 (≠ N604)
Sites not aligning to the query:
- binding heme c: 598, 599, 602, 603, 617, 620, 631, 637, 640, 642, 643, 645
5xm3A Crystal structure of methanol dehydrogenase from methylophaga aminisulfidivorans (see paper)
26% identity, 76% coverage: 171:783/803 of query aligns to 13:536/596 of 5xm3A
- active site: E177 (≠ T377), N261 (= N441), D303 (= D485)
- binding magnesium ion: E177 (≠ T377), N261 (= N441)
- binding pyrroloquinoline quinone: E55 (= E221), C103 (≠ F267), R109 (= R273), T159 (= T355), S174 (≠ N374), G175 (≠ E375), A176 (≠ S376), E177 (≠ T377), T241 (vs. gap), W243 (vs. gap), R331 (≠ K512), N394 (= N609), W476 (≠ M721)
Sites not aligning to the query:
4aahA Methanol dehydrogenase from methylophilus w3a1 (see paper)
26% identity, 75% coverage: 180:784/803 of query aligns to 22:530/571 of 4aahA
- active site: E171 (≠ T377), N255 (= N441), D297 (= D485)
- binding calcium ion: E171 (≠ T377), N255 (= N441)
- binding pyrroloquinoline quinone: E55 (= E221), C103 (≠ F267), C104 (≠ A268), R109 (= R273), S168 (≠ N374), A170 (≠ S376), E171 (≠ T377), W237 (= W423), R324 (≠ K512), N387 (= N609), W467 (≠ M721)
Sites not aligning to the query:
7o6zB Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
25% identity, 77% coverage: 171:789/803 of query aligns to 13:547/588 of 7o6zB
- binding methanol: E173 (≠ N374), W263 (= W447), D314 (= D485)
- binding Neodymium Ion: E173 (≠ N374), N259 (= N441), D314 (= D485), D316 (= D487)
- binding pyrroloquinoline quinone: E55 (= E221), C105 (≠ F267), C106 (≠ A268), R111 (= R273), T155 (≠ S356), G170 (≠ V371), G171 (≠ T372), D172 (= D373), E173 (≠ N374), W241 (= W423), D316 (= D487), R341 (≠ K512), D403 (≠ N609), W481 (≠ M721), G544 (= G786), W545 (≠ S787)
7o6zA Structure of a neodymium-containing, xoxf1-type methanol dehydrogenase (see paper)
25% identity, 77% coverage: 171:789/803 of query aligns to 13:547/588 of 7o6zA
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)
29% identity, 45% coverage: 170:527/803 of query aligns to 52:384/757 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
29% identity, 45% coverage: 170:527/803 of query aligns to 18:350/723 of 8gy2A
- binding calcium ion: E181 (≠ T377), N263 (= N441), D308 (= D485)
- binding heme c: D104 (≠ F264)
- binding pyrroloquinoline quinone: C107 (≠ F267), C108 (≠ A268), D163 (≠ T355), G179 (≠ E375), A180 (≠ S376), E181 (≠ T377), W245 (= W423), N263 (= N441), D308 (= D485), K335 (= K512)
Sites not aligning to the query:
- binding heme c: 618, 619, 622, 623, 633, 634, 636, 639, 652, 660, 662, 665
- binding pyrroloquinoline quinone: 398, 489
6oc6A Lanthanide-dependent methanol dehydrogenase xoxf from methylobacterium extorquens, in complex with lanthanum and pyrroloquinoline quinone (see paper)
26% identity, 76% coverage: 183:793/803 of query aligns to 25:545/579 of 6oc6A
- active site: E171 (= E375), N255 (= N441), D297 (= D485)
- binding pyrroloquinoline quinone: E55 (= E221), C103 (≠ F267), C104 (≠ A268), R109 (= R273), T153 (= T355), S168 (≠ T372), G169 (≠ D373), G170 (≠ N374), E171 (= E375), W237 (= W423), D299 (= D487), R324 (≠ K512), D395 (≠ N609), W473 (≠ M721), G536 (= G784), W537 (≠ H785)
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)
26% identity, 77% coverage: 169:783/803 of query aligns to 38:563/626 of P16027
- C130 (≠ F267) modified: Disulfide link with 131; mutation to S: Inactive.
- C131 (≠ A268) modified: Disulfide link with 130; mutation to S: Inactive.
- D330 (= D485) mutation to E: Lower affinity for methanol.
- C413 (≠ Y601) modified: Disulfide link with 442
- C442 (vs. gap) modified: Disulfide link with 413
Sites not aligning to the query:
1w6sC The high resolution structure of methanol dehydrogenase from methylobacterium extorquens (see paper)
26% identity, 77% coverage: 169:783/803 of query aligns to 11:536/596 of 1w6sC
- active site: E177 (≠ T377), N261 (= N441), D303 (= D485)
- binding calcium ion: E177 (≠ T377), N261 (= N441)
- binding pyrroloquinoline quinone: E55 (= E221), C103 (≠ F267), C104 (≠ A268), R109 (= R273), T159 (≠ G343), S174 (≠ N374), A176 (≠ S376), E177 (≠ T377), T241 (≠ N421), W243 (= W423), R331 (≠ K512), N394 (= N609), W476 (≠ M721)
Sites not aligning to the query:
2d0vA Crystal structure of methanol dehydrogenase from hyphomicrobium denitrificans (see paper)
25% identity, 76% coverage: 171:783/803 of query aligns to 13:536/597 of 2d0vA
- active site: E177 (≠ P380), N261 (= N441), D303 (= D485)
- binding calcium ion: E177 (≠ P380), N261 (= N441), D303 (= D485)
- binding pyrroloquinoline quinone: E55 (= E221), R109 (= R273), T159 (= T355), S174 (≠ T377), G175 (≠ N378), A176 (≠ E379), E177 (≠ P380), T241 (≠ N421), W243 (= W423), R331 (≠ K512), N394 (= N609), W476 (≠ M721)
Sites not aligning to the query:
6zcvA Crystal structure of lanthanide-dependent alcohol dehydrogenase pedh from pseudomonas putida kt2440
25% identity, 76% coverage: 181:788/803 of query aligns to 26:531/562 of 6zcvA
- active site: E172 (= E379), N254 (≠ T443), D296 (= D485)
- binding calcium ion: N161 (≠ G368), K163 (≠ H370), P278 (≠ L467), D279 (≠ A468)
- binding pyrroloquinoline quinone: Q60 (≠ E221), C104 (≠ F267), C105 (≠ A268), I108 (≠ T271), R110 (= R273), S154 (= S356), G170 (≠ T377), G171 (≠ N378), E172 (= E379), W236 (≠ K431), D298 (= D487), R323 (≠ K512), N390 (= N609), W466 (≠ M721), G529 (= G786), A530 (≠ S787)
Q4W6G0 Quinohemoprotein alcohol dehydrogenase ADH-IIG; ADH IIG; Alcohol dehydrogenase (azurin); EC 1.1.9.1 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
23% identity, 84% coverage: 121:793/803 of query aligns to 10:577/718 of Q4W6G0
- C138 (≠ F267) modified: Disulfide link with 139
- C139 (≠ A268) modified: Disulfide link with 138
- R144 (= R273) binding
- T189 (≠ G350) binding
- GA 205:206 (≠ HV 370:371) binding
- E207 (≠ T372) binding
- T264 (≠ N421) binding
- N284 (= N441) binding
- D329 (= D485) binding
- K356 (= K512) binding
- W415 (≠ V605) binding
- DW 419:420 (≠ NW 609:610) 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
7ce5A Methanol-pqq bound methanol dehydrogenase (mdh) from methylococcus capsulatus (bath) (see paper)
24% identity, 76% coverage: 171:783/803 of query aligns to 13:529/573 of 7ce5A
- active site: E177 (≠ D373), N261 (= N441), D303 (= D485)
- binding calcium ion: E177 (≠ D373), N261 (= N441), D303 (= D485)
- binding methanol: E177 (≠ D373)
- binding pyrroloquinoline quinone: E55 (= E221), C103 (≠ F267), C104 (≠ A268), R109 (= R273), T159 (= T355), A174 (≠ H370), G175 (≠ V371), A176 (≠ T372), E177 (≠ D373), T241 (≠ N421), W243 (= W423), R330 (≠ K512), N393 (= N609), W469 (≠ M721)
Sites not aligning to the query:
7cdlC Holo-methanol dehydrogenase (mdh) with cys131-cys132 reduced from methylococcus capsulatus (bath) (see paper)
24% identity, 76% coverage: 171:783/803 of query aligns to 13:529/573 of 7cdlC
- active site: E177 (≠ D373), N261 (= N441), D303 (= D485)
- binding calcium ion: E177 (≠ D373), N261 (= N441), D303 (= D485)
- binding pyrroloquinoline quinone: E55 (= E221), R109 (= R273), T159 (= T355), A174 (≠ H370), A176 (≠ T372), E177 (≠ D373), T241 (≠ N421), W243 (= W423), D303 (= D485), R330 (≠ K512), N393 (= N609), W469 (≠ M721)
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)
23% identity, 78% coverage: 170:793/803 of query aligns to 20:548/684 of 1yiqA
- active site: E178 (≠ T372), N255 (= N441), D300 (= D485)
- binding calcium ion: E178 (≠ T372), N255 (= N441), D300 (= D485)
- binding pyrroloquinoline quinone: E63 (= E221), C109 (≠ F267), C110 (≠ A268), R115 (= R273), T160 (≠ G350), G175 (= G369), G176 (≠ H370), A177 (≠ V371), E178 (≠ T372), T235 (≠ N421), W237 (= W423), K327 (= K512), D390 (≠ N609), W391 (= W610), F477 (≠ S720), A542 (≠ S787)
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
Query Sequence
>PfGW456L13_4805 FitnessBrowser__pseudo13_GW456_L13:PfGW456L13_4805
MSTDGALSRSRLLPTLLGILLLLMGLAMLAGGIKLSMLGGSLYYLLAGIGIALSGVLLIA
ARRAALGLYALVLFASTVWALWEVGLDWWQLVPRLALWFALGVVMLLPWFRRPLLINGPA
PMGTGALSVAVVLAGATAVASQFTHPGETFGELGRDTADMTSTAPQMPEGDWQAYGRSEF
GDRYSPLKQITPANVGKLQEAWRIQTGDLPTADDPVELTNENTPLKANGMLYACTAHSKV
LALDPDTGKELWRFDPQIKSPVGFKGFAHMTCRGVSYYDEAAYAKSESAASAVISEAGKA
VAQACPRRLYLPTADARLIALNADTGKICEGFGKNGVVDLTQGIGPFTAGGYYSTSPAAI
TRDLVIMGGHVTDNESTNEPSGVIRAFDVHDGHLVWNWDSNNPDATEPLPEGEHYSRNSA
NMWSLASVDEKLGMVYLPLGNQTPDQWGADRTPGAEKFSAGLVALDLATGKVRWNYQFTH
HDLWDMDVGSQPTLLDMKTADGVKPALIAPTKQGSLYVLDRRDGTPIIPIKEIPAPQGAV
KGDRTAPTQARSDLNLLAPELTEKAMWGASPFDQMLCRIQFKELRYEGQYTPPSEQGSLI
YPGNVGVFNWGGVSVDPVRQMLFTSPNYMAFVSKMVPRAEVAADSKRESETAGVQPNTGA
PYAVIMHPFMSPLGVPCQAPAWGYVAGIDLTTSKVVWKRKNGTSRDSSPLPIGLPLGVPS
MGGSMVTAGGVGFLSGTLDQYLRAYDVNTGNELWKSRLPAGGQATPMTYTGKDGKQYVLL
VVGGHGSLGTKMGDYVIAYKLSE
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