SitesBLAST
Comparing GFF2133 PS417_10880 alcohol dehydrogenase to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 15 hits to proteins with known functional sites (download)
Q47945 Alcohol dehydrogenase (quinone), cytochrome c subunit; ADH; Alcohol dehydrogenase (quinone), subunit II; Cytochrome c-553; Cytochrome c553; Ethanol:Q2 reductase; G3-ADH subunit II; Quinohemoprotein-cytochrome c complex; Ubiquinol oxidase; EC 1.1.5.5 from Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans) (see paper)
47% identity, 88% coverage: 46:440/447 of query aligns to 40:443/478 of Q47945
Sites not aligning to the query:
- 1:36 signal peptide
- 37 modified: Pyrrolidone carboxylic acid
8gy2B Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
47% identity, 88% coverage: 46:440/447 of query aligns to 2:405/433 of 8gy2B
- binding heme c: C18 (= C62), C21 (= C65), H22 (= H66), T46 (= T90), I48 (= I92), Y59 (= Y103), L68 (≠ V112), R73 (≠ A117), V79 (≠ L123), Y80 (= Y124), M83 (= M127), F88 (≠ Y132), R126 (= R170), H165 (= H208), C166 (= C209), C169 (= C212), H170 (= H213), I201 (≠ Y242), A202 (= A243), P203 (= P244), L205 (= L246), W216 (= W257), F224 (= F265), A234 (≠ V275), V235 (= V276), F236 (≠ Y277), F236 (≠ Y277), M239 (= M280), N301 (≠ R337), C302 (= C338), C305 (= C341), H306 (= H342), M316 (≠ W352), F317 (≠ M353), P318 (= P354), L320 (= L356), P324 (≠ T360), G342 (≠ S378), S352 (≠ D388), V354 (≠ Y390), M356 (= M392), F359 (= F395), M375 (≠ V411)
- binding ubiquinone-10: C21 (= C65), L34 (= L78), P39 (= P83), P81 (= P125), L129 (≠ I173), W132 (= W176), E168 (≠ S211), R173 (= R216), I197 (≠ L238), D241 (≠ E282)
Sites not aligning to the query:
7w2jC Cryo-em structure of membrane-bound fructose dehydrogenase from gluconobacter japonicus
38% identity, 85% coverage: 50:431/447 of query aligns to 1:386/418 of 7w2jC
- binding heme c: C13 (= C62), C16 (= C65), H17 (= H66), T42 (= T90), I44 (= I92), Y55 (= Y103), L75 (= L123), Y76 (= Y124), A78 (= A126), M79 (= M127), R122 (= R170), H161 (= H208), C162 (= C209), C165 (= C212), H166 (= H213), A191 (= A243), P192 (= P244), R223 (≠ V275), P227 (≠ S279), M228 (= M280), V289 (≠ R337), C290 (= C338), C293 (= C341), H294 (= H342), Y305 (≠ W352), Y306 (≠ M353), P307 (= P354), L309 (= L356), N312 (≠ A359), T313 (= T360), T314 (≠ S361), D322 (≠ S369), I327 (≠ T374), V331 (≠ S378), R333 (= R380), I340 (≠ Y390), M342 (= M392), P343 (= P393), F345 (= F395)
8jejC Cryo-em structure of na-dithionite reduced membrane-bound fructose dehydrogenase from gluconobacter japonicus
37% identity, 85% coverage: 50:431/447 of query aligns to 1:400/413 of 8jejC
- binding heme c: C13 (= C62), C16 (= C65), H17 (= H66), T42 (= T90), I44 (= I92), F60 (= F108), L64 (≠ V112), L75 (= L123), Y76 (= Y124), M79 (= M127), P80 (= P128), Y84 (= Y132), R122 (= R170), C162 (= C209), C165 (= C212), H166 (= H213), I186 (≠ L238), W189 (= W241), A191 (= A243), P192 (= P244), I194 (≠ L246), W205 (= W257), Y213 (≠ F265), R223 (≠ V275), M228 (= M280), V303 (≠ R337), C304 (= C338), C307 (= C341), H308 (= H342), Y320 (≠ M353), P321 (= P354), L323 (= L356), T327 (= T360), T328 (≠ S361), D336 (≠ S369), I341 (≠ T374), V345 (≠ S378), R347 (= R380), I354 (≠ Y390), M356 (= M392), F359 (= F395), I376 (≠ V407)
- binding ubiquinone-10: M36 (≠ L84), P77 (= P125), S124 (≠ P172), W128 (= W176), C165 (= C212), L173 (= L218)
Sites not aligning to the query:
8gy3A Cryo-em structure of membrane-bound aldehyde dehydrogenase from gluconobacter oxydans
34% identity, 87% coverage: 25:414/447 of query aligns to 20:410/440 of 8gy3A
- binding heme c: Y52 (≠ D61), C53 (= C62), C56 (= C65), H57 (= H66), S84 (≠ T90), I86 (= I92), W97 (≠ Y103), F102 (= F108), L117 (= L123), F121 (≠ M127), F126 (≠ Y132), R163 (= R170), C203 (= C209), C206 (= C212), H207 (= H213), A232 (= A243), P233 (= P244), L235 (= L246), W245 (= W257), Y253 (≠ F265), L254 (= L266), G263 (≠ A274), S264 (≠ V275), M269 (= M280), Y292 (≠ L303), C337 (= C338), C340 (= C341), H341 (= H342), P353 (= P354), L355 (= L356), N358 (≠ A359), N359 (≠ T360), V372 (≠ I373), I377 (≠ V381), G382 (≠ V386), Q383 (≠ P387), I386 (≠ Y390), M388 (= M392), F391 (= F395)
- binding ubiquinone-10: E55 (≠ A64), T76 (= T82), F78 (≠ L84), Y118 (= Y124), P119 (= P125), I160 (≠ L167), G166 (vs. gap), Q167 (≠ I173), F169 (≠ L175), W170 (= W176), H202 (= H208), R210 (= R216), L213 (≠ A219)
8hddB Complex structure of catalytic, small, and a partial electron transfer subunits from burkholderia cepacia fad glucose dehydrogenase
35% identity, 28% coverage: 308:431/447 of query aligns to 1:121/121 of 8hddB
- binding protoporphyrin ix containing fe: C30 (= C338), C33 (= C341), H34 (= H342), Y46 (≠ M353), P47 (= P354), T54 (≠ S361), V66 (≠ I373), I67 (≠ T374), R73 (= R380), I80 (≠ Y390), M82 (= M392), P83 (= P393)
6fjaA Crystal structure of t2d three-domain heme-cu nitrite reductase from ralstonia pickettii
38% identity, 24% coverage: 325:431/447 of query aligns to 345:452/455 of 6fjaA
- binding protoporphyrin ix containing fe: T359 (≠ R337), C360 (= C338), C363 (= C341), H364 (= H342), P376 (= P354), P377 (= P355), L378 (= L356), F383 (≠ A362), N400 (≠ S378), G401 (≠ Q379), Y410 (≠ D388), S412 (≠ Y390), M414 (= M392), M417 (≠ F395)
Sites not aligning to the query:
- active site: 90, 93, 95, 130, 131, 139, 144, 236, 258, 259, 285
- binding copper (ii) ion: 90, 131, 139, 144
4ax3D Structure of three-domain heme-cu nitrite reductase from ralstonia pickettii at 1.6 a resolution (see paper)
38% identity, 24% coverage: 325:431/447 of query aligns to 348:455/457 of 4ax3D
- binding heme c: C363 (= C338), C366 (= C341), H367 (= H342), P379 (= P354), P380 (= P355), L381 (= L356), S384 (≠ T360), F386 (≠ A362), N403 (≠ S378), G404 (≠ Q379), S415 (≠ Y390), M417 (= M392), M420 (≠ F395)
Sites not aligning to the query:
- active site: 93, 96, 98, 133, 134, 142, 147, 239, 261, 262, 288
- binding copper (ii) ion: 93, 98, 133, 134, 142, 147
5oboA Crystal structure of nitrite bound d97n mutant of three-domain heme-cu nitrite reductase from ralstonia pickettii
38% identity, 24% coverage: 325:431/447 of query aligns to 346:453/456 of 5oboA
- binding heme c: T360 (≠ R337), C361 (= C338), C364 (= C341), H365 (= H342), P377 (= P354), P378 (= P355), L379 (= L356), S382 (≠ T360), F384 (≠ A362), I395 (= I373), N401 (≠ S378), G402 (≠ Q379), S413 (≠ Y390), M415 (= M392), M418 (≠ F395)
Sites not aligning to the query:
- active site: 91, 94, 96, 131, 132, 140, 145, 237, 259, 260, 286
- binding copper (ii) ion: 91, 96, 131, 132, 140, 145
- binding nitrite ion: 94, 96, 131
2zooA Crystal structure of nitrite reductase from pseudoalteromonas haloplanktis tac125
34% identity, 23% coverage: 330:431/447 of query aligns to 339:438/438 of 2zooA
- binding protoporphyrin ix containing fe: C347 (= C338), C350 (= C341), H351 (= H342), F362 (≠ M353), P363 (= P354), P364 (= P355), L365 (= L356), S368 (≠ T360), Y370 (≠ A362), I382 (≠ T374), L386 (vs. gap), S387 (= S378), G388 (≠ Q379), I390 (≠ V381), V392 (≠ A383), Y397 (≠ D388), N398 (≠ A389), G399 (≠ Y390), V400 (≠ R391), M401 (= M392)
Sites not aligning to the query:
- active site: 81, 84, 86, 121, 122, 130, 135, 227, 249, 250, 276
- binding copper (ii) ion: 81, 86, 121, 122, 130, 135
1r0qA Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (spirographis) heme (see paper)
40% identity, 20% coverage: 328:417/447 of query aligns to 1:92/130 of 1r0qA
- binding 2-formyl-protoporphryn ix: C13 (= C341), H14 (= H342), P26 (= P354), L28 (= L356), H31 (≠ A359), Y44 (vs. gap), V48 (≠ I373), Q54 (= Q379), G55 (vs. gap), G66 (≠ Y390), M68 (= M392)
Sites not aligning to the query:
1qyzA Characterization of the malformed, recombinant cytochrome rc552 (see paper)
40% identity, 20% coverage: 328:417/447 of query aligns to 1:92/130 of 1qyzA
- binding 2-acetyl-protoporphyrin ix: Y7 (= Y334), C10 (= C338), C13 (= C341), H14 (= H342), P26 (= P354), H31 (≠ A359), Y44 (vs. gap), Q54 (= Q379), G55 (vs. gap), G66 (≠ Y390), M68 (= M392), F71 (= F395)
Sites not aligning to the query:
1c52A Thermus thermophilus cytochrome-c552: a new highly thermostable cytochromE-C structure obtained by mad phasing (see paper)
40% identity, 20% coverage: 328:417/447 of query aligns to 2:93/131 of 1c52A
- binding protoporphyrin ix containing fe: C11 (= C338), C14 (= C341), H15 (= H342), F26 (≠ M353), P27 (= P354), L29 (= L356), H32 (≠ A359), Y45 (vs. gap), L54 (≠ S378), Q55 (= Q379), G56 (vs. gap), G67 (≠ Y390), M69 (= M392), F72 (= F395)
Sites not aligning to the query:
1dt1A Thermus thermophilus cytochrome c552 synthesized by escherichia coli (see paper)
40% identity, 20% coverage: 330:417/447 of query aligns to 2:91/129 of 1dt1A
- binding heme c: C9 (= C338), C12 (= C341), H13 (= H342), P25 (= P354), H30 (≠ A359), Y43 (vs. gap), V47 (≠ I373), Q53 (= Q379), G54 (vs. gap), G65 (≠ Y390), M67 (= M392), F70 (= F395)
Sites not aligning to the query:
Q03075 Cbb3-type cytochrome c oxidase subunit FixP; Cbb3-Cox subunit FixP; C-type cytochrome FixP; Cyt c(FixP); Cytochrome c oxidase subunit III from Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110) (see paper)
28% identity, 35% coverage: 261:416/447 of query aligns to 152:288/290 of Q03075
- C219 (= C338) mutation to S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-222 or with S-222, S-122 and S-125. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex.
- C222 (= C341) mutation to S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-219 or with S-219, S-122 and S-125. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex.
Sites not aligning to the query:
- 122 C→S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-125 or with S-125, S-219 and S-222. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex.
- 125 C→S: 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex; when associated with S-122 or with S-122, S-219 and S-222. 85% decrease in cytochrome c oxidase complex activity and assembly defects of the complex.
Query Sequence
>GFF2133 PS417_10880 alcohol dehydrogenase
MNNRRFARTAGWLALPCLVAAGLLAWYVTREPATPFEQEQAGATFEPALVSRGEYVARLS
DCVACHSLAGKAPFAGGLEMATPLGAIHATNITPDKSTGIGTYSLADFDRAVRHGVAPGG
RRLYPAMPYPSYVKLSDDDIKALYAFFMQGIKPANQPNIPSDIPWPLNMRWPIALWNGVF
APTATYAAKPDQDALWNRGAYIVQGPGHCGSCHTPRGLAFNEKALDEAGAPFLAGALLDG
WYAPSLRQDPNTGLGRWSEPQIVQFLKTGRNAHAVVYGSMTEAFNNSTQFMQDDDLAAIA
RYLKSLPGDPQRDGAPWQYQAVAAVQDAPGAHTYATRCASCHGLDGKGQPEWMPPLAGAT
SALAKESASAINITLNGSQRVVASGVPDAYRMPAFREQLSDTEIAEVLSYVRSTWGNNGG
AVDANAVGKLRGHTDPASSSPIILHMR
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