SitesBLAST
Comparing RR42_RS28380 FitnessBrowser__Cup4G11:RR42_RS28380 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)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
26% identity, 81% coverage: 44:347/375 of query aligns to 43:348/378 of 5ol2F
- active site: L124 (≠ A123), T125 (≠ S124), G241 (≠ A238)
- binding coenzyme a persulfide: L238 (≠ T235), R242 (≠ S239)
- binding flavin-adenine dinucleotide: F122 (≠ L121), L124 (≠ A123), T125 (≠ S124), P127 (≠ S126), T131 (≠ Y130), F155 (≠ L154), I156 (≠ V155), T157 (≠ L156), E198 (≠ H195), R267 (= R264), F270 (= F267), L274 (= L271), F277 (= F274), Q335 (= Q334), L336 (= L335), G338 (= G337), G339 (≠ A338)
Sites not aligning to the query:
6cxtB Crystal structure of fad-dependent dehydrogenase (see paper)
28% identity, 95% coverage: 1:355/375 of query aligns to 1:349/372 of 6cxtB
- active site: I117 (≠ A123), S118 (= S124), E234 (≠ A238)
- binding flavin-adenine dinucleotide: N115 (≠ L121), I117 (≠ A123), S118 (= S124), G123 (≠ R129), S124 (≠ Y130), Y148 (≠ L154), T150 (≠ L156), L201 (vs. gap)
- binding S-[2-({N-[(2R)-2-hydroxy-4-{[(R)-hydroxy(oxo)-lambda~5~-phosphanyl]oxy}-3,3-dimethylbutanoyl]-beta-alanyl}amino)ethyl] 1H-pyrrole-2-carbothioate: A81 (vs. gap), N115 (≠ L121), S124 (≠ Y130), F227 (≠ I231), M231 (≠ T235), E234 (≠ A238), R235 (≠ S239)
Sites not aligning to the query:
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
26% identity, 93% coverage: 4:350/375 of query aligns to 56:403/432 of P45954
- V137 (≠ W85) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ L86) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 117:126, 30% identical) binding in other chain
- S183 (= S126) binding
- WIS 207:209 (≠ LVL 154:156) binding in other chain
- S210 (≠ E157) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ D176) binding
- L255 (≠ R203) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ L228) binding
- NEGR 291:294 (≠ DRAS 236:239) binding
- I316 (≠ L261) to V: in dbSNP:rs1131430
- R319 (= R264) binding
- Q330 (= Q275) binding
- EWMGG 387:391 (≠ QLHGA 334:338) binding
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
- 416 A→T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 416:418 binding in other chain
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
26% identity, 93% coverage: 4:350/375 of query aligns to 5:352/381 of 2jifA
- active site: L125 (= L119), S126 (≠ A120), G242 (≠ A238)
- binding coenzyme a persulfide: S132 (= S126), S134 (= S128), Y178 (≠ D176), Y232 (≠ L228), I236 (≠ E232), L239 (≠ T235), N240 (≠ D236), R243 (≠ S239)
- binding flavin-adenine dinucleotide: F123 (≠ C117), L125 (= L119), S126 (≠ A120), G131 (≠ E125), S132 (= S126), W156 (≠ L154), I157 (≠ V155), S158 (≠ L156), K201 (≠ L200), T209 (vs. gap), R268 (= R264), F271 (= F267), L275 (= L271), F278 (= F274), L281 (= L277), E336 (≠ Q334), W337 (≠ L335), G340 (≠ A338)
Sites not aligning to the query:
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
26% identity, 91% coverage: 5:347/375 of query aligns to 53:398/430 of P51174
- K318 (= K265) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ T269) modified: N6-acetyllysine; alternate; mutation to R: Reduces activity by 23%; reduces activity by 80% when associated with R-318.
Sites not aligning to the query:
- 42 modified: N6-acetyllysine; K→R: Reduces activity by 90% when associated with R-318 and R-322.
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
25% identity, 98% coverage: 3:370/375 of query aligns to 4:372/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (≠ Y130), T134 (≠ L132), R180 (≠ D178), R234 (≠ P229), L237 (≠ E232), R238 (≠ A233), L240 (≠ T235), D241 (= D236), R244 (≠ S239), E365 (≠ D363), G366 (≠ A364)
- binding flavin-adenine dinucleotide: Y123 (≠ L121), L125 (≠ A123), S126 (= S124), G131 (≠ R129), S132 (≠ Y130), W156 (≠ L154), I157 (≠ V155), T158 (≠ L156), I360 (= I357), T367 (≠ S365), Q369 (≠ H367)
Sites not aligning to the query:
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
25% identity, 98% coverage: 3:370/375 of query aligns to 4:372/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ L121), L125 (≠ A123), S126 (= S124), G131 (≠ R129), S132 (≠ Y130), W156 (≠ L154), I157 (≠ V155), T158 (≠ L156), I360 (= I357), Y364 (≠ F361), T367 (≠ S365), Q369 (≠ H367)
7w0jE Acyl-coa dehydrogenase, tfu_1647
25% identity, 98% coverage: 3:370/375 of query aligns to 5:373/382 of 7w0jE
- binding [[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(2R,3S,4S)-5-azanyl-2,3,4-tris(oxidanyl)pentyl] hydrogen phosphate: S127 (= S124), W157 (≠ L154), R270 (= R264), Q272 (= Q266), F273 (= F267), I277 (≠ L271), F280 (= F274), I283 (≠ L277), Q339 (= Q334), L340 (= L335), G343 (≠ A338), Y365 (≠ F361), E366 (≠ D363), T368 (≠ S365), Q370 (≠ H367), I371 (≠ L368)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
27% identity, 96% coverage: 1:361/375 of query aligns to 6:356/377 of 4ktoA
- active site: M130 (≠ A123), S131 (= S124), E239 (≠ A238)
- binding flavin-adenine dinucleotide: L128 (= L121), M130 (≠ A123), S131 (= S124), M155 (≠ T153), W156 (≠ L154), T158 (≠ L156), R265 (= R264), F268 (= F267), I272 (≠ L271), F275 (= F274), M278 (≠ L277), Q333 (= Q334), A334 (≠ L335), G337 (≠ A338), L355 (= L360)
Sites not aligning to the query:
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
27% identity, 97% coverage: 7:371/375 of query aligns to 6:370/381 of 8sgsA
- binding coenzyme a: S131 (≠ Y130), A133 (≠ L132), N177 (≠ D177), F231 (≠ L228), M235 (≠ E232), L238 (≠ T235), I312 (≠ Q309), E362 (≠ D363), G363 (≠ A364)
- binding flavin-adenine dinucleotide: F122 (≠ L121), L124 (≠ A123), S125 (= S124), G130 (≠ R129), S131 (≠ Y130), W155 (≠ L154), T157 (≠ L156), R267 (= R264), F270 (= F267), L274 (= L271), L277 (≠ F274), Q335 (= Q334), I336 (≠ L335), G338 (= G337), G339 (≠ A338), I357 (= I357), I360 (≠ L360), Y361 (≠ F361), T364 (≠ S365), E366 (≠ H367)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
26% identity, 97% coverage: 7:371/375 of query aligns to 36:400/412 of P16219
- G90 (= G61) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E75) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 121:130, 30% identical) binding in other chain
- R171 (≠ Q140) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ LVL 154:156) binding in other chain
- A192 (= A161) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G179) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R264) binding
- Q308 (= Q275) binding in other chain
- R325 (≠ K292) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ G322) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QLHGA 334:338) binding
- R380 (vs. gap) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ SHH 365:367) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 97% coverage: 7:371/375 of query aligns to 12:376/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L121), L130 (≠ A123), S131 (= S124), G136 (≠ R129), S137 (≠ Y130), W161 (≠ L154), T163 (≠ L156), T214 (≠ A205), R273 (= R264), F276 (= F267), L280 (= L271), L283 (≠ F274), V285 (= V276), Q341 (= Q334), I342 (≠ L335), G345 (≠ A338), I363 (= I357), Y367 (≠ F361), T370 (≠ S365), E372 (≠ H367), L376 (≠ F371)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
26% identity, 83% coverage: 42:352/375 of query aligns to 51:365/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S124), G140 (≠ R129), S141 (≠ Y130), W165 (≠ L154), T167 (≠ L156), R279 (= R264), F282 (= F267), I286 (≠ L271), F289 (= F274), Q347 (= Q334), C348 (≠ L335), G351 (≠ A338)
Sites not aligning to the query:
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 97% coverage: 7:371/375 of query aligns to 9:373/385 of 7y0bA
- binding (2S,3R,4R,5S,6R)-2-[4-chloranyl-3-[[4-[(3S)-oxolan-3-yl]oxyphenyl]methyl]phenyl]-6-(hydroxymethyl)oxane-3,4,5-triol: M343 (= M339), T347 (≠ D343), E348 (= E344)
- binding flavin-adenine dinucleotide: F125 (≠ L121), L127 (≠ A123), S128 (= S124), G133 (≠ R129), S134 (≠ Y130), W158 (≠ L154), T160 (≠ L156), R270 (= R264), F273 (= F267), L280 (≠ F274), V282 (= V276), Q338 (= Q334), I339 (≠ L335), G342 (≠ A338), I360 (= I357), Y364 (≠ F361), T367 (≠ S365), E369 (≠ H367), I370 (≠ L368), L373 (≠ F371)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
26% identity, 83% coverage: 42:352/375 of query aligns to 47:361/387 of 1ivhA
- active site: M130 (≠ A123), S131 (= S124), E249 (≠ A238)
- binding coenzyme a persulfide: S137 (≠ Y130), S185 (≠ D177), R186 (≠ D178), V239 (≠ L228), Y240 (≠ P229), M243 (≠ E232), E249 (≠ A238), R250 (≠ S239)
- binding flavin-adenine dinucleotide: L128 (= L121), M130 (≠ A123), S131 (= S124), G136 (≠ R129), S137 (≠ Y130), W161 (≠ L154), T163 (≠ L156), R275 (= R264), F278 (= F267), F285 (= F274), M288 (≠ L277), Q343 (= Q334), C344 (≠ L335), G347 (≠ A338)
Sites not aligning to the query:
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
26% identity, 83% coverage: 42:352/375 of query aligns to 84:398/426 of P26440
- 165:174 (vs. 121:130, 40% identical) binding
- S174 (≠ Y130) binding
- WIT 198:200 (≠ LVL 154:156) binding
- SR 222:223 (≠ DD 177:178) binding
- G250 (= G202) to A: in IVA; uncertain significance
- Y277 (≠ P229) binding
- DLER 284:287 (≠ DRAS 236:239) binding
- E286 (≠ A238) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (≠ C243) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R264) binding
- Q323 (= Q275) binding
- I379 (= I333) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLHGA 334:338) binding
- R398 (≠ K352) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 403 Y → N: in IVA; uncertain significance
- 407 A→E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- 407:408 binding
- 409:411 binding
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
25% identity, 91% coverage: 5:347/375 of query aligns to 53:398/430 of P28330
- E291 (≠ A238) active site, Proton acceptor; mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. No effect on protein abundance. No effect on solubility. No effect on substrate binding.
- S303 (≠ L250) to T: in dbSNP:rs1801204
- K333 (≠ R280) to Q: in dbSNP:rs2286963
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
26% identity, 97% coverage: 7:371/375 of query aligns to 3:360/371 of 2vigB
- active site: L121 (≠ A123), S122 (= S124), G231 (≠ A238), E352 (≠ D363)
- binding coenzyme a persulfide: S128 (≠ Y130), F221 (≠ L228), M225 (≠ E232), Q226 (≠ A233), L228 (≠ T235), D229 (= D236), R232 (≠ S239), E352 (≠ D363), G353 (≠ A364), I357 (≠ L368)
- binding flavin-adenine dinucleotide: L121 (≠ A123), S122 (= S124), G127 (≠ R129), S128 (≠ Y130), W152 (≠ L154), T154 (≠ L156), R257 (= R264), F260 (= F267), L264 (= L271), L267 (≠ F274), Q325 (= Q334), I326 (≠ L335), G329 (≠ A338), I347 (= I357), Y351 (≠ F361), T354 (≠ S365), E356 (≠ H367)
Sites not aligning to the query:
6cy8B Crystal structure of fad-dependent dehydrogenase (see paper)
27% identity, 95% coverage: 1:355/375 of query aligns to 1:347/370 of 6cy8B
- active site: I115 (≠ A123), S116 (= S124), E232 (≠ A238)
- binding flavin-adenine dinucleotide: N113 (≠ L121), I115 (≠ A123), S116 (= S124), G121 (≠ R129), S122 (≠ Y130), Y146 (≠ L154), T148 (≠ L156), L199 (vs. gap)
- binding 4'-phosphopantetheine: S122 (≠ Y130), F225 (≠ I231), A226 (≠ E232), R233 (≠ S239)
Sites not aligning to the query:
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
26% identity, 99% coverage: 1:371/375 of query aligns to 1:370/379 of 1ukwB
- active site: L124 (≠ A123), S125 (= S124), T241 (≠ A238), E362 (≠ D363)
- binding cobalt (ii) ion: D145 (= D144), H146 (≠ G145)
- binding flavin-adenine dinucleotide: F122 (≠ L121), L124 (≠ A123), S125 (= S124), G130 (≠ R129), S131 (≠ Y130), W155 (≠ L154), S157 (≠ L156), K200 (≠ F197), L357 (≠ I357), Y361 (≠ F361), E362 (≠ D363), T364 (≠ S365), E366 (≠ H367), L370 (≠ F371)
Sites not aligning to the query:
Query Sequence
>RR42_RS28380 FitnessBrowser__Cup4G11:RR42_RS28380
MDFSYTDEHIALQDAVRRFCDGEYPAHQRGNPEAPALCAQRWASMAELGLLGLPFDSEVG
GSGQGTVELMLVAQELGRCLGGGAWLSSVVLAGQLLDQVGTARQRGRWLPEVASGKCRLA
LAASESDSRYSLSRVRTRAQASADGWRIEGRKTLVLEGGDANAFIVVARTAGDVADDDGL
TLFLVDAKTPGVAVHGFATLDGRQAAHVVLDGVQVGSDAMLGEAGRALPLIEAATDRASA
VLCAEAAGALEALIDLTAEHLKTRKQFGTTLARFQVLQHRVADMLIALEQSKSMACAAAM
AVDAGEPVQRRRLVSAAKVVVGQAGRQVSQWAIQLHGAMGMTDECRVGHYAKRLLVINQL
FGDASHHLQRFAQRP
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