SitesBLAST
Comparing WP_085121631.1 NCBI__GCF_900177295.1:WP_085121631.1 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)
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)
36% identity, 100% coverage: 1:400/400 of query aligns to 1:395/400 of I6YCA3
- IGYS 127:130 (≠ QGFS 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 385:387) binding FAD
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
36% identity, 100% coverage: 1:400/400 of query aligns to 1:382/386 of 4x28A
- active site: Y122 (≠ F128), S123 (= S129), E240 (= E244), G365 (= G383), M377 (≠ K395)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (≠ T161), F363 (≠ I381), T367 (≠ S385), E369 (= E387), V370 (≠ I388)
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)
38% identity, 85% coverage: 60:398/400 of query aligns to 58:380/387 of P71858
- E241 (= E244) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
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)
37% identity, 88% coverage: 50:400/400 of query aligns to 388:709/711 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: 1:400/400 of query aligns to 1:381/384 of 6wy8B
- active site: Y126 (≠ F128), T127 (≠ S129), E241 (= E244), T376 (≠ K395)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (≠ F128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (≠ T161), V359 (≠ A366), F362 (≠ I369), G363 (≠ A370), V366 (≠ S385), E368 (= E387)
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
34% identity, 97% coverage: 12:400/400 of query aligns to 8:377/380 of 6wy9A
- active site: Y122 (≠ F128), T123 (≠ S129), E237 (= E244), T372 (≠ K395)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (≠ T161), F358 (≠ I369), V362 (≠ S385), E364 (= E387)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
29% identity, 88% coverage: 46:397/400 of query aligns to 42:378/380 of 2pg0A
- active site: M124 (≠ F128), T125 (≠ S129), E243 (= E244), A364 (≠ G383), R376 (≠ K395)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ F128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (= T161), R269 (≠ Q268), F272 (≠ G271), F279 (≠ R278), Q337 (≠ E338), L338 (≠ V339), G340 (= G341), G341 (≠ P342), V359 (≠ K378), I362 (= I381), Y363 (= Y382), T366 (≠ S385), E368 (= E387), M369 (≠ I388)
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
34% identity, 63% coverage: 1:253/400 of query aligns to 1:247/379 of 8hk0B
Sites not aligning to the query:
7w0jE Acyl-coa dehydrogenase, tfu_1647
28% identity, 86% coverage: 55:398/400 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 (= S129), W157 (= W159), R270 (≠ Q268), Q272 (≠ V270), F273 (≠ G271), I277 (≠ L275), F280 (≠ R278), I283 (≠ F281), Q339 (≠ E338), L340 (≠ V339), G343 (≠ P342), Y365 (= Y382), E366 (≠ G383), T368 (≠ S385), Q370 (≠ E387), I371 (= I388)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
28% identity, 86% coverage: 55:398/400 of query aligns to 51:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S135), T134 (≠ L137), R180 (≠ A183), R234 (≠ D235), L237 (≠ K238), R238 (≠ F239), L240 (= L241), D241 (≠ G242), R244 (= R245), E365 (≠ G383), G366 (= G384), R377 (≠ K395)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (= T161), I360 (≠ K378), T367 (≠ S385), Q369 (≠ E387)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
28% identity, 86% coverage: 55:398/400 of query aligns to 51:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (= T161), I360 (≠ K378), Y364 (= Y382), T367 (≠ S385), Q369 (≠ E387)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 85% coverage: 61:398/400 of query aligns to 56:377/379 of 1ukwB
- active site: L124 (≠ F128), S125 (= S129), T241 (≠ E244), E362 (≠ G383), R374 (≠ K395)
- binding cobalt (ii) ion: D145 (≠ E149), H146 (≠ F150)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ F128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), K200 (≠ I205), L357 (vs. gap), Y361 (= Y382), E362 (≠ G383), T364 (≠ S385), E366 (= E387), L370 (≠ S391)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 85% coverage: 61:398/400 of query aligns to 56:377/379 of 1ukwA
- active site: L124 (≠ F128), S125 (= S129), T241 (≠ E244), E362 (≠ G383), R374 (≠ K395)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ F128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (≠ T161), L357 (vs. gap), Y361 (= Y382), E362 (≠ G383), T364 (≠ S385), E366 (= E387), L370 (≠ S391)
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)
27% identity, 98% coverage: 9:398/400 of query aligns to 1:368/369 of 3pfdC
- active site: L116 (≠ F128), S117 (= S129), T233 (≠ E244), E353 (≠ G383), R365 (≠ K395)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ Q126), L116 (≠ F128), S117 (= S129), G122 (= G134), S123 (= S135), W147 (= W159), I148 (≠ T160), T149 (= T161), R259 (≠ Q268), F262 (≠ G271), V266 (≠ L275), N269 (≠ R278), Q326 (≠ E338), L327 (≠ V339), G330 (≠ P342), I348 (≠ K378), Y352 (= Y382), T355 (≠ S385), Q357 (≠ E387)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
27% identity, 84% coverage: 63:398/400 of query aligns to 106:427/430 of P51174
- K318 (≠ S269) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ V273) 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.
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)
28% identity, 98% coverage: 5:397/400 of query aligns to 57:428/432 of P45954
- V137 (≠ L90) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ A91) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 124:135, 58% 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 (≠ K181) 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 (≠ GNER 242:245) binding substrate
- I316 (≠ A265) to V: in dbSNP:rs1131430
- R319 (≠ Q268) binding FAD
- Q330 (= Q279) binding FAD
- EWMGG 387:391 (≠ EVVG- 338:341) binding FAD
- A416 (≠ S385) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ SNE 385:387) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
28% identity, 98% coverage: 5:397/400 of query aligns to 6:377/381 of 2jifA
- active site: L125 (≠ F128), S126 (= S129), G242 (≠ E244), E363 (≠ G383), K375 (= K395)
- binding coenzyme a persulfide: S132 (= S135), S134 (≠ L137), Y178 (≠ K181), Y232 (≠ W234), I236 (≠ K238), L239 (= L241), N240 (≠ G242), R243 (= R245), Y362 (= Y382), E363 (≠ G383), G364 (= G384), I368 (= I388)
- binding flavin-adenine dinucleotide: F123 (≠ W124), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), S158 (≠ T161), K201 (≠ I205), T209 (≠ V211), R268 (≠ Q268), F271 (≠ G271), L275 (= L275), F278 (≠ R278), L281 (≠ F281), E336 (= E338), W337 (≠ V339), G340 (vs. gap), N367 (≠ E387), I368 (= I388)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
24% identity, 99% coverage: 3:398/400 of query aligns to 1:377/379 of 6fahD
- active site: L124 (≠ F128), T125 (≠ S129), G241 (≠ E244), G374 (≠ K395)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ F128), T125 (≠ S129), R152 (≠ Q156), F155 (≠ W159), T157 (= T161), E198 (≠ Q203), R267 (≠ Q268), Q269 (≠ V270), F270 (≠ G271), I274 (≠ L275), F277 (≠ R278), Q335 (≠ E338), I336 (≠ V339), G339 (≠ P342), Y361 (= Y382), T364 (≠ S385), Q366 (≠ E387)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
24% identity, 100% coverage: 1:398/400 of query aligns to 1:378/380 of 4l1fA
- active site: L125 (≠ F128), T126 (≠ S129), G242 (≠ E244), E363 (≠ G383), R375 (≠ K395)
- binding coenzyme a persulfide: T132 (≠ S135), H179 (≠ A183), F232 (≠ W234), M236 (≠ K238), E237 (≠ F239), L239 (= L241), D240 (≠ G242), R243 (= R245), Y362 (= Y382), E363 (≠ G383), G364 (= G384), R375 (≠ K395)
- binding flavin-adenine dinucleotide: F123 (≠ Q126), L125 (≠ F128), T126 (≠ S129), G131 (= G134), T132 (≠ S135), F156 (≠ W159), I157 (≠ T160), T158 (= T161), R268 (≠ Q268), Q270 (≠ V270), F271 (≠ G271), I275 (≠ L275), F278 (≠ R278), L281 (≠ F281), Q336 (≠ E338), I337 (≠ V339), G340 (≠ P342), I358 (≠ K378), Y362 (= Y382), T365 (≠ S385), Q367 (≠ E387)
- binding 1,3-propandiol: L5 (≠ F5), Q10 (≠ L10)
6es9A Methylsuccinyl-coa dehydrogenase of paracoccus denitrificans with bound flavin adenine dinucleotide (see paper)
30% identity, 85% coverage: 61:398/400 of query aligns to 213:544/545 of 6es9A
- active site: F281 (= F128), T282 (≠ S129), A408 (≠ E244), R541 (≠ K395)
- binding coenzyme a: F467 (≠ L303), W470 (≠ E306)
- binding flavin-adenine dinucleotide: A279 (≠ Q126), F281 (= F128), T282 (≠ S129), G287 (= G134), S288 (= S135), W312 (= W159), I313 (≠ T160), T314 (= T161), E374 (≠ V211), R434 (≠ Q268), Q436 (≠ V270), F437 (≠ G271), L441 (= L275), F444 (≠ R278), Q502 (≠ E338), I503 (≠ V339), G505 (= G341), G506 (vs. gap), F528 (≠ Y382), A531 (≠ S385), E533 (= E387), I534 (= I388)
Sites not aligning to the query:
Query Sequence
>WP_085121631.1 NCBI__GCF_900177295.1:WP_085121631.1
MDLRFTDDELAFRDEVRAFCRTALPAGIRDKLVAGGSPSKDDMVRWTRILADRGWAVPHW
PVEHGGTGWSPIKQYIFTEELAQTPAPAPLAFGVNMVGPVIYTFGSEAQKRRFLPRIVRL
DDWWCQGFSEPGAGSDLASLRTRAVRDGEFYVVNGQKTWTTLAQHADWIFCLVRTDPAAK
KQAGISFLLIDMRSPGITVRPIQTIDGGHEVNEVFLDEVRVPVENRVGEENRGWDYAKFL
LGNERVTIARVGVSKERIRRIKALAAQQSVGGVRLLDRQDFREKLAAVEVELKALEMTQL
RVLANEAKRETGKQDPASSILKIKGSEIQQATSELLLEVVGPYALPYQPREELDGRNEPP
IGPDWASTIAPSYFNLRKVSIYGGSNEIQRSIIAKAILGL
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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