SitesBLAST
Comparing CCNA_02128 FitnessBrowser__Caulo:CCNA_02128 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)
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)
41% identity, 85% coverage: 58:397/401 of query aligns to 388:709/711 of P96855
- E581 (= E252) 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)
36% identity, 63% coverage: 9:260/401 of query aligns to 9:249/384 of 6wy8B
Sites not aligning to the query:
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
36% identity, 63% coverage: 9:260/401 of query aligns to 5:245/380 of 6wy9A
Sites not aligning to the query:
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)
39% identity, 53% coverage: 49:260/401 of query aligns to 39:249/387 of P71858
- E241 (= E252) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
32% identity, 86% coverage: 55:397/401 of query aligns to 42:382/386 of 4x28A
- active site: Y122 (= Y137), S123 (= S138), E240 (= E252), G365 (= G380), M377 (≠ K392)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q135), Y122 (= Y137), S123 (= S138), G128 (= G143), T129 (≠ S144), W153 (= W168), S155 (= S170), F363 (vs. gap), T367 (= T382), E369 (= E384), V370 (= V385)
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)
32% identity, 86% coverage: 55:397/401 of query aligns to 49:395/400 of I6YCA3
- IGYS 127:130 (≠ QGYS 135:138) binding
- T136 (≠ S144) binding
- S162 (= S170) binding
- E247 (= E252) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ TSE 382:384) binding
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
29% identity, 94% coverage: 20:395/401 of query aligns to 15:377/380 of 4l1fA
- active site: L125 (≠ Y137), T126 (≠ S138), G242 (≠ E252), E363 (≠ G380), R375 (= R393)
- binding coenzyme a persulfide: T132 (≠ S144), H179 (≠ E191), F232 (≠ W242), M236 (≠ K246), E237 (≠ R247), L239 (= L249), D240 (≠ Q250), R243 (= R253), Y362 (≠ E379), E363 (≠ G380), G364 (= G381), R375 (= R393)
- binding flavin-adenine dinucleotide: F123 (≠ Q135), L125 (≠ Y137), T126 (≠ S138), G131 (= G143), T132 (≠ S144), F156 (≠ W168), I157 (≠ T169), T158 (≠ S170), R268 (≠ V279), Q270 (≠ S281), F271 (≠ E282), I275 (≠ D287), F278 (= F290), L281 (vs. gap), Q336 (≠ E345), I337 (≠ A346), G340 (= G351), I358 (≠ G375), Y362 (≠ E379), T365 (= T382), Q367 (≠ E384)
Sites not aligning to the query:
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
36% identity, 51% coverage: 58:262/401 of query aligns to 46:255/389 of C3UVB0
- A80 (≠ L89) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ P96) binding
- V88 (≠ A97) mutation to S: A residual dehydrogenase activity is observed.
- N91 (≠ S100) binding
- FGIT 126:129 (≠ QGYS 135:138) binding
- S135 (= S144) binding ; binding
- WIS 159:161 (≠ WTS 168:170) binding
- S181 (≠ H190) binding
Sites not aligning to the query:
- 271 binding
- 281:284 binding
- 340 binding
- 344 binding
- 366 V→Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- 367:371 binding
- 385 binding
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
36% identity, 51% coverage: 58:262/401 of query aligns to 46:255/393 of 3mpjB
- active site: I128 (≠ Y137), T129 (≠ S138), T245 (≠ E252)
- binding flavin-adenine dinucleotide: F126 (≠ Q135), I128 (≠ Y137), T129 (≠ S138), G134 (= G143), S135 (= S144), W159 (= W168), I160 (≠ T169), S161 (= S170)
- binding : A164 (≠ D173), Q165 (= Q174), D167 (= D176), N193 (≠ T201)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
36% identity, 51% coverage: 58:262/401 of query aligns to 46:255/395 of 3mpiC
- active site: I128 (≠ Y137), T129 (≠ S138), T245 (≠ E252)
- binding flavin-adenine dinucleotide: I128 (≠ Y137), T129 (≠ S138), G134 (= G143), S135 (= S144), W159 (= W168), I160 (≠ T169), S161 (= S170)
- binding glutaryl-coenzyme A: R87 (≠ P96), F126 (≠ Q135), S135 (= S144), V137 (≠ L146), S181 (≠ H190), F239 (≠ K246), R246 (= R253)
Sites not aligning to the query:
- active site: 367, 379
- binding flavin-adenine dinucleotide: 365, 366, 369, 371, 375
- binding glutaryl-coenzyme A: 315, 366, 367, 368, 376, 385, 389
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
28% identity, 85% coverage: 55:396/401 of query aligns to 42:378/379 of 1ukwB
- active site: L124 (≠ Y137), S125 (= S138), T241 (≠ E252), E362 (≠ G380), R374 (≠ K392)
- binding cobalt (ii) ion: D145 (= D158), H146 (= H159)
- binding flavin-adenine dinucleotide: F122 (≠ Q135), L124 (≠ Y137), S125 (= S138), G130 (= G143), S131 (= S144), W155 (= W168), S157 (= S170), K200 (= K211), L357 (≠ G375), Y361 (≠ E379), E362 (≠ G380), T364 (= T382), E366 (= E384), L370 (≠ N388)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
28% identity, 85% coverage: 55:396/401 of query aligns to 42:378/379 of 1ukwA
- active site: L124 (≠ Y137), S125 (= S138), T241 (≠ E252), E362 (≠ G380), R374 (≠ K392)
- binding flavin-adenine dinucleotide: F122 (≠ Q135), L124 (≠ Y137), S125 (= S138), G130 (= G143), S131 (= S144), W155 (= W168), S157 (= S170), L357 (≠ G375), Y361 (≠ E379), E362 (≠ G380), T364 (= T382), E366 (= E384), L370 (≠ N388)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
29% identity, 85% coverage: 55:395/401 of query aligns to 41:377/378 of 5ol2F
- active site: L124 (≠ Y137), T125 (≠ S138), G241 (≠ E252), G374 (≠ K392)
- binding coenzyme a persulfide: L238 (= L249), R242 (= R253), E362 (≠ G380), G363 (= G381)
- binding flavin-adenine dinucleotide: F122 (≠ Q135), L124 (≠ Y137), T125 (≠ S138), P127 (= P140), T131 (≠ S144), F155 (≠ W168), I156 (≠ T169), T157 (≠ S170), E198 (≠ P209), R267 (≠ E276), F270 (≠ V279), L274 (vs. gap), F277 (vs. gap), Q335 (≠ E345), L336 (≠ A346), G338 (= G348), G339 (= G351), Y361 (≠ E379), T364 (= T382), E366 (= E384)
Sites not aligning to the query:
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
32% identity, 61% coverage: 12:256/401 of query aligns to 12:247/379 of 8hk0B
Sites not aligning to the query:
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
31% identity, 62% coverage: 12:260/401 of query aligns to 12:251/380 of 2pg0A
Sites not aligning to the query:
- active site: 364, 376
- binding flavin-adenine dinucleotide: 269, 272, 279, 337, 338, 340, 341, 359, 362, 363, 366, 368, 369
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)
30% identity, 83% coverage: 62:395/401 of query aligns to 41:368/369 of 3pfdC
- active site: L116 (≠ Y137), S117 (= S138), T233 (≠ E252), E353 (≠ G380), R365 (≠ K392)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ Q135), L116 (≠ Y137), S117 (= S138), G122 (= G143), S123 (= S144), W147 (= W168), I148 (≠ T169), T149 (≠ S170), R259 (≠ L277), F262 (≠ E282), V266 (≠ I285), N269 (≠ G288), Q326 (≠ E345), L327 (≠ A346), G330 (= G351), I348 (≠ G375), Y352 (≠ E379), T355 (= T382), Q357 (≠ E384)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
29% identity, 85% coverage: 55:395/401 of query aligns to 41:377/379 of 6fahD
- active site: L124 (≠ Y137), T125 (≠ S138), G241 (≠ E252), G374 (≠ K392)
- binding flavin-adenine dinucleotide: F122 (≠ Q135), L124 (≠ Y137), T125 (≠ S138), R152 (≠ Q165), F155 (≠ W168), T157 (≠ S170), E198 (vs. gap), R267 (vs. gap), Q269 (≠ E276), F270 (≠ L277), I274 (= I285), F277 (= F290), Q335 (≠ E345), I336 (≠ A346), G339 (= G351), Y361 (≠ E379), T364 (= T382), Q366 (≠ E384)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
32% identity, 83% coverage: 63:395/401 of query aligns to 51:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S144), T134 (≠ L146), R180 (≠ E191), R234 (≠ D243), L237 (≠ K246), R238 (= R247), L240 (= L249), D241 (≠ Q250), R244 (= R253), E365 (≠ G380), G366 (= G381), R377 (≠ K392)
- binding flavin-adenine dinucleotide: Y123 (≠ Q135), L125 (≠ Y137), S126 (= S138), G131 (= G143), S132 (= S144), W156 (= W168), I157 (≠ T169), T158 (≠ S170), I360 (≠ G375), T367 (= T382), Q369 (≠ E384)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
32% identity, 83% coverage: 63:395/401 of query aligns to 51:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ Q135), L125 (≠ Y137), S126 (= S138), G131 (= G143), S132 (= S144), W156 (= W168), I157 (≠ T169), T158 (≠ S170), I360 (≠ G375), Y364 (≠ E379), T367 (= T382), Q369 (≠ E384)
7w0jE Acyl-coa dehydrogenase, tfu_1647
32% identity, 83% coverage: 63:395/401 of query aligns to 52:381/382 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 (= S138), W157 (= W168), R270 (≠ G283), Q272 (vs. gap), F273 (vs. gap), I277 (≠ D287), F280 (= F290), I283 (vs. gap), Q339 (≠ E345), L340 (≠ A346), G343 (= G351), Y365 (≠ E379), E366 (≠ G380), T368 (= T382), Q370 (≠ E384), I371 (≠ V385)
Query Sequence
>CCNA_02128 FitnessBrowser__Caulo:CCNA_02128
MADFGATDLDAFRADTRAWLEANYPKSLNAPMGEDEAPWGGRKMVWKNPDAKLWLDRMAE
RGWTAPMWPKEYGGGGLSKAQNKVLEQELRRLKARPALMSFGVWMLGPVLLEYATEEQKQ
RFLPAIVRGETRWCQGYSEPGAGSDLASLQTKCEDKGDHYLINGQKVWTSYADQADWIFC
LVRTDTSKKHEGISFVLFDMTSPGVEARPIKLISGSSPFCETFFDNVKVPKEQLVGKLNG
GWDIAKRLLQYERQNISASGFGGGGGLSVVEAAKKELGVDSEGRIADGDFRARLAAHSMD
AHAFMLTVRRAEAESKQGSGPSAAVSIIKYAAAKMNQERTELLVEALGLQGLGWSGEDFS
AEELAAPRAMLRAKGNSIEGGTSEVNLNVVAKRVLGLLDHQ
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