SitesBLAST
Comparing GFF3989 FitnessBrowser__Marino:GFF3989 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)
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
33% identity, 100% coverage: 1:398/398 of query aligns to 1:382/386 of 4x28A
- active site: Y122 (= Y128), S123 (= S129), E240 (= E244), G365 (= G381), M377 (≠ K393)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (≠ T161), F363 (≠ I379), T367 (≠ S383), E369 (= E385), V370 (≠ I386)
I6YCA3 Acyl-CoA dehydrogenase FadE26; ACAD; 3-oxocholest-4-en-26-oyl-CoA dehydrogenase alpha subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
33% identity, 100% coverage: 1:398/398 of query aligns to 1:395/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 126:129) binding FAD
- T136 (≠ S135) binding FAD
- S162 (≠ T161) binding FAD
- E247 (= E244) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ SNE 383:385) binding FAD
P96855 Acyl-CoA dehydrogenase FadE34; ACAD; 3-oxochol-4-en-24-oyl-CoA dehydrogenase; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
34% identity, 89% coverage: 43:398/398 of query aligns to 381:709/711 of P96855
- E581 (= E244) mutation to Q: Displays less than 1% activity with cholyl-CoA as substrate. Still binds FAD.
Sites not aligning to the query:
- 236 R→A: Displays less than 2% activity with cholyl-CoA as substrate. Cannot bind FAD.
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
33% identity, 100% coverage: 1:398/398 of query aligns to 1:381/384 of 6wy8B
- active site: Y126 (= Y128), T127 (≠ S129), E241 (= E244), T376 (≠ K393)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (= Y128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (≠ T161), V359 (≠ F380), F362 (vs. gap), G363 (vs. gap), V366 (≠ S383), E368 (= E385)
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
33% identity, 97% coverage: 12:398/398 of query aligns to 8:377/380 of 6wy9A
- active site: Y122 (= Y128), T123 (≠ S129), E237 (= E244), T372 (≠ K393)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (= Y128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (≠ T161), F358 (vs. gap), V362 (≠ S383), E364 (= E385)
P71858 Acyl-CoA dehydrogenase FadE29; ACAD; 3-oxo-23,24-bisnorchol-4-en-22-oyl-CoA dehydrogenase beta subunit; 3-oxo-4-pregnene-20-carboxyl-CoA dehydrogenase beta subunit; EC 1.3.99.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
30% identity, 98% coverage: 1:392/398 of query aligns to 1:376/387 of P71858
- E241 (= E244) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
33% identity, 88% coverage: 46:395/398 of query aligns to 42:378/380 of 2pg0A
- active site: M124 (≠ Y128), T125 (≠ S129), E243 (= E244), A364 (≠ G381), R376 (≠ K393)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ Y128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (= T161), R269 (= R268), F272 (≠ N271), F279 (≠ D278), Q337 (≠ R336), L338 (≠ A337), G340 (= G339), G341 (≠ P340), V359 (≠ K376), I362 (= I379), Y363 (≠ F380), T366 (≠ S383), E368 (= E385), M369 (≠ I386)
2z1qB Crystal structure of acyl coa dehydrogenase
32% identity, 87% coverage: 52:396/398 of query aligns to 67:409/549 of 2z1qB
- active site: L144 (vs. gap), T145 (≠ S129), G259 (≠ E244), E394 (≠ G381), G406 (≠ K393)
- binding flavin-adenine dinucleotide: Y142 (= Y128), L144 (vs. gap), T145 (≠ S129), G150 (= G134), S151 (= S135), W177 (= W159), S179 (≠ T161), R285 (= R268), F288 (≠ N271), I292 (≠ L275), F295 (≠ D278), I298 (≠ F281), H369 (≠ Y354), G370 (≠ D355), F393 (= F380), I399 (= I386)
Sites not aligning to the query:
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
29% identity, 87% coverage: 50:396/398 of query aligns to 42:376/383 of 4iv6B
- active site: L121 (≠ Y128), T122 (≠ S129), G240 (vs. gap), E361 (vs. gap), K373 (= K393)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ Y128), T122 (≠ S129), G126 (≠ A133), G127 (= G134), S128 (= S135), W152 (= W159), I153 (≠ T160), S154 (≠ T161), R266 (= R268), S268 (≠ K270), F269 (≠ N271), I273 (≠ L275), H276 (≠ D278), V279 (≠ F281), R334 (= R336), V335 (≠ A337), G338 (≠ P340), L356 (= L377), G360 (= G381), T363 (≠ S383), E365 (= E385), I366 (= I386)
3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr (see paper)
29% identity, 97% coverage: 10:396/398 of query aligns to 2:368/369 of 3pfdC
- active site: L116 (≠ Y128), S117 (= S129), T233 (≠ E244), E353 (≠ G381), R365 (≠ K393)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ Q126), L116 (≠ Y128), S117 (= S129), G122 (= G134), S123 (= S135), W147 (= W159), I148 (≠ T160), T149 (= T161), R259 (= R268), F262 (≠ N271), V266 (≠ L275), N269 (≠ D278), Q326 (≠ R336), L327 (≠ A337), G330 (≠ P340), I348 (≠ K376), Y352 (≠ F380), T355 (≠ S383), Q357 (≠ E385)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
29% identity, 99% coverage: 5:397/398 of query aligns to 2:374/374 of 5lnxD
- active site: L122 (≠ Y128), T123 (≠ S129), G239 (≠ E244), E358 (≠ G381), K370 (= K393)
- binding flavin-adenine dinucleotide: L122 (≠ Y128), T123 (≠ S129), G128 (= G134), S129 (= S135), F153 (≠ W159), T155 (= T161), R265 (= R268), Q267 (≠ K270), F268 (≠ N271), I272 (≠ L275), N275 (≠ D278), I278 (≠ F281), Q331 (≠ A342), I332 (= I343), G335 (= G356), Y357 (≠ F380), T360 (≠ S383), E362 (= E385)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
29% identity, 98% coverage: 4:395/398 of query aligns to 5:377/381 of 2jifA
- active site: L125 (≠ Y128), S126 (= S129), G242 (≠ E244), E363 (≠ G381), K375 (= K393)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ L137), Y178 (≠ Q182), Y232 (≠ W234), I236 (≠ K238), L239 (= L241), N240 (≠ T242), R243 (= R245), Y362 (≠ F380), E363 (≠ G381), G364 (= G382), I368 (= I386)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), S158 (≠ T161), K201 (≠ T204), T209 (≠ V211), R268 (= R268), F271 (≠ N271), L275 (= L275), F278 (≠ D278), L281 (≠ F281), E336 (= E347), W337 (≠ E348), G340 (≠ D351), N367 (≠ E385), I368 (= I386)
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)
29% identity, 98% coverage: 4:395/398 of query aligns to 56:428/432 of P45954
- V137 (= V90) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ P91) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 126:135, 60% identical) binding in other chain
- S183 (= S135) binding substrate
- WIS 207:209 (≠ WTT 159:161) binding in other chain
- S210 (≠ L162) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ Q182) binding substrate
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W234) binding substrate
- NEGR 291:294 (≠ TYER 242:245) binding substrate
- I316 (≠ A265) to V: in dbSNP:rs1131430
- R319 (= R268) binding FAD
- Q330 (≠ A279) binding FAD
- EWMGG 387:391 (≠ EEELD 347:351) binding FAD
- A416 (≠ S383) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ SNE 383:385) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
32% identity, 62% coverage: 1:248/398 of query aligns to 1:247/379 of 8hk0B
Sites not aligning to the query:
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 87% coverage: 50:397/398 of query aligns to 45:378/379 of 1ukwB
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E244), E362 (≠ G381), R374 (≠ K393)
- binding cobalt (ii) ion: D145 (= D149), H146 (= H150)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), K200 (≠ L205), L357 (≠ K376), Y361 (≠ F380), E362 (≠ G381), T364 (≠ S383), E366 (= E385), L370 (≠ N389)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 87% coverage: 50:397/398 of query aligns to 45:378/379 of 1ukwA
- active site: L124 (≠ Y128), S125 (= S129), T241 (≠ E244), E362 (≠ G381), R374 (≠ K393)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), L357 (≠ K376), Y361 (≠ F380), E362 (≠ G381), T364 (≠ S383), E366 (= E385), L370 (≠ N389)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
28% identity, 99% coverage: 1:396/398 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ Y128), T126 (≠ S129), G242 (≠ E244), E363 (≠ G381), R375 (≠ K393)
- binding coenzyme a persulfide: T132 (≠ S135), H179 (≠ E183), F232 (≠ W234), M236 (≠ K238), E237 (≠ Y239), L239 (= L241), D240 (≠ T242), R243 (= R245), Y362 (≠ F380), E363 (≠ G381), G364 (= G382), R375 (≠ K393)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ Y128), T126 (≠ S129), G131 (= G134), T132 (≠ S135), F156 (≠ W159), I157 (≠ T160), T158 (= T161), R268 (= R268), Q270 (≠ K270), F271 (≠ N271), I275 (≠ L275), F278 (≠ D278), L281 (≠ F281), Q336 (≠ R336), I337 (≠ A337), G340 (≠ P340), I358 (≠ L377), Y362 (≠ F380), T365 (≠ S383), Q367 (≠ E385)
- binding 1,3-propandiol: L5 (≠ Y5), Q10 (≠ L10)
7w0jE Acyl-coa dehydrogenase, tfu_1647
28% identity, 98% coverage: 6:396/398 of query aligns to 8:381/382 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 (= S129), W157 (= W159), R270 (= R268), Q272 (≠ K270), F273 (≠ N271), I277 (≠ L275), F280 (≠ D278), I283 (≠ F281), Q339 (≠ R336), L340 (≠ A337), G343 (≠ P340), Y365 (≠ F380), E366 (≠ G381), T368 (≠ S383), Q370 (≠ E385), I371 (= I386)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
28% identity, 87% coverage: 50:396/398 of query aligns to 44:377/378 of 5ol2F
- active site: L124 (≠ Y128), T125 (≠ S129), G241 (≠ E244), G374 (≠ K393)
- binding coenzyme a persulfide: L238 (= L241), R242 (= R245), E362 (≠ G381), G363 (= G382)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ Y128), T125 (≠ S129), P127 (= P131), T131 (≠ S135), F155 (≠ W159), I156 (≠ T160), T157 (= T161), E198 (≠ R200), R267 (= R268), F270 (≠ N271), L274 (= L275), F277 (≠ D278), Q335 (≠ R336), L336 (≠ A337), G338 (= G339), G339 (≠ P340), Y361 (≠ F380), T364 (≠ S383), E366 (= E385)
Sites not aligning to the query:
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
28% identity, 98% coverage: 6:396/398 of query aligns to 7:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S135), T134 (≠ L137), R180 (≠ E183), R234 (≠ T235), L237 (≠ K238), R238 (≠ Y239), L240 (= L241), D241 (≠ T242), R244 (= R245), E365 (≠ G381), G366 (= G382), R377 (≠ K393)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ Y128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (= T161), I360 (≠ K376), T367 (≠ S383), Q369 (≠ E385)
Query Sequence
>GFF3989 FitnessBrowser__Marino:GFF3989
MNLNYTTEELAFRDEVRAFLDKKLPGDIAAKVKGFRRLSKEDHQRWQKILSEQGWYATHW
PEEYGGVNWSPVQKHIWDEESSRYGAPRSVPFGVNMVAPVIIKFGTEEQKQRYLPRILSG
EDWWCQGYSEPGAGSDLASLKTRAVRDGDHYIVNGQKTWTTLGQHANMIFCLVRTNTEVK
AQEGISFLLIDMDTPGITVRPIITLDGEHEVNEVFFEDVKVPAENLVGEEDKGWTYAKYL
LTYERTGLAGIGISKAALQHLKELATRRVKNGRPLIEDASFGQRIAQVEIDLMAAAISNL
RIIASVEGGGMPGAESSMLKVRGTEIRQTINDLARRAIGPYAIPFVEEELDLDYDGDFLS
DENAAPVAPQYFNNRKLSIFGGSNEIQKNIVSKMILGL
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