SitesBLAST
Comparing Dsui_2086 Dsui_2086 cytochrome c 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)
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)
42% identity, 59% coverage: 20:430/696 of query aligns to 18:434/478 of Q47945
- Q37 (≠ E41) modified: Pyrrolidone carboxylic acid
Sites not aligning to the query:
8gy2B Cryo-em structure of membrane-bound alcohol dehydrogenase from gluconobacter oxydans
43% identity, 56% coverage: 43:430/696 of query aligns to 1:396/433 of 8gy2B
- binding heme c: C18 (= C60), C21 (= C63), H22 (= H64), T46 (= T88), I48 (= I90), Y59 (= Y101), L68 (≠ M110), R73 (≠ A115), V79 (≠ L121), Y80 (= Y122), M83 (= M125), F88 (≠ Y130), R126 (= R168), H165 (= H206), C166 (= C207), C169 (= C210), H170 (= H211), I201 (≠ R243), A202 (= A244), P203 (≠ L245), L205 (= L247), W216 (= W251), F224 (= F259), A234 (≠ T269), V235 (≠ A270), F236 (≠ S271), F236 (≠ S271), M239 (= M274), N301 (≠ F337), C302 (= C338), C305 (= C341), H306 (= H342), M316 (≠ I352), F317 (= F353), P318 (= P354), L320 (= L356), P324 (= P360), G342 (≠ W378), S352 (≠ R388), V354 (≠ F390), M356 (= M392), F359 (= F395), M375 (≠ V410)
- binding ubiquinone-10: C21 (= C63), L34 (≠ R76), P39 (= P81), P81 (= P123), L129 (= L171), W132 (= W174), E168 (≠ A209), R173 (= R214), I197 (≠ V239), D241 (≠ E276)
Sites not aligning to the query:
7w2jC Cryo-em structure of membrane-bound fructose dehydrogenase from gluconobacter japonicus
38% identity, 55% coverage: 48:431/696 of query aligns to 1:387/418 of 7w2jC
- binding heme c: C13 (= C60), C16 (= C63), H17 (= H64), T42 (= T88), I44 (= I90), Y55 (= Y101), L75 (= L121), Y76 (= Y122), A78 (= A124), M79 (= M125), R122 (= R168), H161 (= H206), C162 (= C207), C165 (= C210), H166 (= H211), A191 (= A244), P192 (≠ L245), R223 (≠ T269), P227 (≠ N273), M228 (= M274), V289 (≠ F337), C290 (= C338), C293 (= C341), H294 (= H342), Y305 (≠ I352), Y306 (≠ F353), P307 (= P354), L309 (= L356), N312 (= N359), T313 (≠ P360), T314 (≠ A361), D322 (≠ T369), I327 (≠ T374), V331 (≠ W378), R333 (≠ T380), I340 (≠ F390), M342 (= M392), P343 (= P393), F345 (= F395)
8jejC Cryo-em structure of na-dithionite reduced membrane-bound fructose dehydrogenase from gluconobacter japonicus
38% identity, 55% coverage: 48:431/696 of query aligns to 1:401/413 of 8jejC
- binding heme c: C13 (= C60), C16 (= C63), H17 (= H64), T42 (= T88), I44 (= I90), F60 (= F106), L64 (≠ M110), L75 (= L121), Y76 (= Y122), M79 (= M125), P80 (= P126), Y84 (= Y130), R122 (= R168), C162 (= C207), C165 (= C210), H166 (= H211), I186 (≠ V239), W189 (= W242), A191 (= A244), P192 (≠ L245), I194 (≠ L247), W205 (= W251), Y213 (≠ F259), R223 (≠ T269), M228 (= M274), V303 (≠ F337), C304 (= C338), C307 (= C341), H308 (= H342), Y320 (≠ F353), P321 (= P354), L323 (= L356), T327 (≠ P360), T328 (≠ A361), D336 (≠ T369), I341 (≠ T374), V345 (≠ W378), R347 (≠ T380), I354 (≠ F390), M356 (= M392), F359 (= F395), I376 (≠ L406)
- binding ubiquinone-10: M36 (≠ F82), P77 (= P123), S124 (≠ G170), W128 (= W174), C165 (= C210), L173 (≠ F218)
Sites not aligning to the query:
8gy3A Cryo-em structure of membrane-bound aldehyde dehydrogenase from gluconobacter oxydans
34% identity, 54% coverage: 40:413/696 of query aligns to 33:410/440 of 8gy3A
- binding heme c: Y52 (≠ D59), C53 (= C60), C56 (= C63), H57 (= H64), S84 (≠ T88), I86 (= I90), W97 (≠ Y101), F102 (= F106), L117 (= L121), F121 (≠ M125), F126 (≠ Y130), R163 (= R168), C203 (= C207), C206 (= C210), H207 (= H211), A232 (= A244), P233 (≠ L245), L235 (= L247), W245 (= W251), Y253 (≠ F259), L254 (= L260), G263 (≠ A268), S264 (≠ T269), M269 (= M274), Y292 (≠ L297), C337 (= C338), C340 (= C341), H341 (= H342), P353 (= P354), L355 (= L356), N358 (= N359), N359 (≠ P360), V372 (≠ I373), I377 (≠ W378), G382 (≠ T383), Q383 (≠ A384), I386 (≠ F390), M388 (= M392), F391 (= F395)
- binding ubiquinone-10: E55 (≠ A62), T76 (= T80), F78 (= F82), Y118 (= Y122), P119 (= P123), I160 (≠ F165), G166 (= G170), Q167 (≠ L171), F169 (≠ L173), W170 (= W174), H202 (= H206), R210 (= R214), L213 (≠ A217)
D3RVD4 Thiosulfate dehydrogenase; Tetrathionate synthase; EC 1.8.2.2 from Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D) (Chromatium vinosum) (see 2 papers)
43% identity, 32% coverage: 461:684/696 of query aligns to 50:270/270 of D3RVD4
- C123 (= C530) mutation to G: Loss of function.
Sites not aligning to the query:
4v2kA Crystal structure of the thiosulfate dehydrogenase tsda in complex with thiosulfate (see paper)
43% identity, 31% coverage: 461:678/696 of query aligns to 20:234/235 of 4v2kA
- active site: R79 (= R516), R89 (= R526), C93 (= C530), S97 (= S534)
- binding heme c: C46 (= C487), H48 (≠ S489), C49 (= C490), C49 (= C490), H50 (= H491), P51 (≠ L492), F66 (= F503), C93 (= C530), F94 (= F531), S97 (= S534), L98 (≠ M535), G134 (= G571), I135 (= I572), R156 (≠ Q593), C157 (= C594), C160 (= C597), H161 (= H598), F177 (≠ Y614), P178 (= P615), P179 (= P616), L180 (= L617), F186 (= F623), F201 (= F638), M206 (= M643), P207 (= P644), L208 (≠ I645)
- binding thiosulfate: R79 (= R516), R89 (= R526), C93 (= C530), R96 (= R533), S97 (= S534), A190 (= A627), G191 (= G628)
4wqaA Thiosulfate dehydrogenase (tsda) from allochromatium vinosum - tetrathionate co-crystallization (see paper)
42% identity, 31% coverage: 461:678/696 of query aligns to 19:227/227 of 4wqaA
- binding heme c: C45 (= C487), H47 (≠ S489), C48 (= C490), C48 (= C490), H49 (= H491), F65 (= F503), R88 (= R526), C92 (= C530), F93 (= F531), S96 (= S534), L97 (≠ M535), G133 (= G571), I134 (= I572), R155 (≠ Q593), C156 (= C594), C159 (= C597), H160 (= H598), F176 (≠ Y614), P177 (= P615), P178 (= P616), L179 (= L617), F185 (= F623), F185 (= F623), F200 (= F638), K204 (≠ N642), M205 (= M643)
- binding sulfite ion: R78 (= R516), R88 (= R526), C92 (= C530), R95 (= R533), S96 (= S534), A189 (= A627), G190 (= G628)
5lo9A Thiosulfate dehydrogenase (tsdba) from marichromatium purpuratum - "as isolated" form (see paper)
33% identity, 49% coverage: 338:680/696 of query aligns to 121:436/471 of 5lo9A
- binding heme c: C121 (= C338), R123 (≠ D340), C124 (= C341), H125 (= H342), F136 (= F353), P137 (= P354), L139 (= L356), Y146 (≠ L370), Y146 (≠ L370), Q150 (≠ T374), W154 (= W378), R159 (≠ T383), E162 (≠ H386), M167 (≠ T391), R225 (vs. gap), Q241 (≠ L485), C243 (= C487), A244 (≠ T488), G245 (≠ S489), C246 (= C490), C246 (= C490), H247 (= H491), M259 (≠ F503), A262 (≠ V506), Y266 (≠ F510), R282 (= R526), C286 (= C530), F287 (= F531), S290 (= S534), M291 (= M535), R333 (= R570), Y335 (≠ I572), H357 (≠ Q593), C358 (= C594), C361 (= C597), H362 (= H598), F377 (≠ Y614), P378 (= P615), L380 (= L617), Y386 (≠ F623), Y386 (≠ F623), F401 (= F638), I402 (≠ V639), M406 (= M643), P407 (= P644)
- binding thiosulfate: R282 (= R526), C286 (= C530), S290 (= S534)
Sites not aligning to the query:
- binding heme c: 21, 24, 25, 36, 37, 40, 47, 47, 51, 54, 60, 62, 64, 65, 68, 80
4ax3D Structure of three-domain heme-cu nitrite reductase from ralstonia pickettii at 1.6 a resolution (see paper)
38% identity, 14% coverage: 338:432/696 of query aligns to 363:457/457 of 4ax3D
- binding heme c: C363 (= C338), C366 (= C341), H367 (= H342), P379 (= P354), P380 (= P355), L381 (= L356), S384 (≠ N359), F386 (≠ A361), N403 (≠ K379), G404 (vs. gap), S415 (≠ F390), 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, 14% coverage: 338:432/696 of query aligns to 361:455/456 of 5oboA
- binding heme c: C361 (= C338), C364 (= C341), H365 (= H342), P377 (= P354), P378 (= P355), L379 (= L356), S382 (≠ N359), F384 (≠ A361), I395 (= I373), N401 (≠ K379), G402 (vs. gap), S413 (≠ F390), 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 heme c: 360
- binding nitrite ion: 94, 96, 131
6fjaA Crystal structure of t2d three-domain heme-cu nitrite reductase from ralstonia pickettii
38% identity, 14% coverage: 338:432/696 of query aligns to 360:454/455 of 6fjaA
- binding protoporphyrin ix containing fe: C360 (= C338), C363 (= C341), H364 (= H342), P376 (= P354), P377 (= P355), L378 (= L356), F383 (≠ A361), N400 (≠ K379), G401 (vs. gap), Y410 (≠ R388), S412 (≠ F390), 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
- binding protoporphyrin ix containing fe: 359
1r0qA Characterization of the conversion of the malformed, recombinant cytochrome rc552 to a 2-formyl-4-vinyl (spirographis) heme (see paper)
34% identity, 15% coverage: 330:432/696 of query aligns to 3:113/130 of 1r0qA
- binding 2-formyl-protoporphryn ix: C13 (= C341), H14 (= H342), P26 (= P354), L28 (= L356), H31 (≠ N359), Y44 (vs. gap), V48 (≠ I373), Q54 (≠ K379), G55 (vs. gap), G66 (≠ F390), M68 (= M392)
Sites not aligning to the query:
1qyzA Characterization of the malformed, recombinant cytochrome rc552 (see paper)
34% identity, 15% coverage: 330:432/696 of query aligns to 3:113/130 of 1qyzA
- binding 2-acetyl-protoporphyrin ix: Y7 (= Y334), C10 (= C338), C13 (= C341), H14 (= H342), P26 (= P354), H31 (≠ N359), Y44 (vs. gap), Q54 (≠ K379), G55 (vs. gap), G66 (≠ F390), M68 (= M392), F71 (= F395)
Sites not aligning to the query:
1dt1A Thermus thermophilus cytochrome c552 synthesized by escherichia coli (see paper)
34% identity, 15% coverage: 330:432/696 of query aligns to 2:112/129 of 1dt1A
- binding heme c: C9 (= C338), C12 (= C341), H13 (= H342), P25 (= P354), H30 (≠ N359), Y43 (vs. gap), V47 (≠ I373), Q53 (≠ K379), G54 (vs. gap), G65 (≠ F390), M67 (= M392), F70 (= 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)
34% identity, 15% coverage: 330:432/696 of query aligns to 4:114/131 of 1c52A
- binding protoporphyrin ix containing fe: C11 (= C338), C14 (= C341), H15 (= H342), F26 (= F353), P27 (= P354), L29 (= L356), H32 (≠ N359), Y45 (vs. gap), L54 (≠ W378), Q55 (≠ K379), G56 (vs. gap), G67 (≠ F390), M69 (= M392), F72 (= F395)
Sites not aligning to the query:
2zooA Crystal structure of nitrite reductase from pseudoalteromonas haloplanktis tac125
31% identity, 15% coverage: 330:430/696 of query aligns to 339:438/438 of 2zooA
- binding protoporphyrin ix containing fe: C347 (= C338), C350 (= C341), H351 (= H342), F362 (= F353), P363 (= P354), P364 (= P355), L365 (= L356), S368 (≠ N359), Y370 (≠ A361), I382 (≠ T374), L386 (≠ W378), S387 (≠ K379), G388 (≠ T380), I390 (≠ S382), V392 (≠ A384), Y397 (≠ V389), N398 (≠ F390), G399 (≠ T391), V400 (≠ M392), M401 (≠ P393)
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
8hddB Complex structure of catalytic, small, and a partial electron transfer subunits from burkholderia cepacia fad glucose dehydrogenase
31% identity, 14% coverage: 334:430/696 of query aligns to 26:121/121 of 8hddB
- binding protoporphyrin ix containing fe: C30 (= C338), C33 (= C341), H34 (= H342), Y46 (≠ F353), P47 (= P354), T54 (≠ A361), V66 (≠ I373), I67 (≠ T374), R73 (≠ T380), I80 (≠ F390), M82 (= M392), P83 (= P393)
O33434 L-cysteine S-thiosulfotransferase subunit SoxA; Cytochrome c551 subunit diheme; Protein SoxA; SoxAX cytochrome complex subunit A; Sulfur oxidizing protein A; Thiosulfate-oxidizing multienzyme system protein SoxA; TOMES protein SoxA; EC 2.8.5.2 from Paracoccus pantotrophus (Thiosphaera pantotropha) (see 2 papers)
27% identity, 18% coverage: 486:609/696 of query aligns to 105:221/290 of O33434
- C106 (= C487) binding covalent
- C109 (= C490) binding covalent
- H110 (= H491) binding axial binding residue
- C143 (= C530) binding axial binding residue
- H190 (≠ N585) binding
- C206 (= C594) binding covalent
- H210 (= H598) binding axial binding residue
Sites not aligning to the query:
- 1:26 signal peptide
- 27:290 modified: mature protein, L-cysteine S-thiosulfotransferase subunit SoxA
- 78 binding
- 81 binding
- 251 active site, Cysteine persulfide intermediate; binding axial binding residue
- 266 binding
2c1dA Crystal structure of soxxa from p. Pantotrophus (see paper)
27% identity, 18% coverage: 486:609/696 of query aligns to 79:195/264 of 2c1dA
- binding heme c: C80 (= C487), C83 (= C490), H84 (= H491), M90 (≠ V497), R99 (≠ S512), H103 (≠ R516), Y113 (≠ R526), C117 (= C530), R121 (≠ S534), M122 (= M535), M137 (= M550), C180 (= C594), C183 (= C597), H184 (= H598)
- binding zinc ion: H164 (≠ N585)
Sites not aligning to the query:
- binding heme c: 42, 197, 198, 200, 201, 221, 222, 225, 263
- binding zinc ion: 52, 55, 240
Query Sequence
>Dsui_2086 Dsui_2086 cytochrome c
MTHVPSVPAGAPAGALTRLWRSAAATFLLSALAAAGLGRAEAADAGQIARGEYLARLGDC
VACHTAEGGKSMAGGRELATPFGVLFSTNITPDKETGIGNYTFAQFDRAMRKGVAADGHN
LYPAMPYPSYAKMTGEDMQALYAYLMQGLAPVKQANKPTAMRWPFNQRWGLSLWNWAFLD
ATPFQPDAGKDATWNRGAYLVQGLGHCGACHTPRGIAFQEKAMSDAGSKGKHFLAGETVE
SWRALSLRGLWTVEDTALFLKTGQNRFATASGNMAEVIHHSTQHVKDEDLVAIATYLKSL
PPGEHELPAPSVPRSEVAGKVPGNLFSSRGGLAYVQFCGDCHRQDGNGVSKIFPPLAGNP
AVTAKDPATLLHITLTGWKTASTAAHPRVFTMPGFARLNDQELAELITFVRSSWGNGGEA
VTASQVKKMRAEVVKQDPKAIDNSKFETPRLADMLAKPNAEQLVRGMRLHLETKDLLPNH
VGDQLNCTSCHLNAGTVADGSPFVGVSAFFPSYAPRAGRIITLEDRINGCFKRSMNGKPL
PVESADMKAMVAYFDWMKGATKPEDKVPGRGIGKIDRSLKPDSDNGKKIYAEQCAVCHGE
NGEGLKSADGKMVYPPLWGDESFNIGAGMARTYTAAAFVKRNMPIGFHGKFPLGQGGLSD
QEALDVAEYFSHQPRPDFPEKVKDWPNGKKPEDARY
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