SitesBLAST
Comparing WP_011952836.1 NCBI__GCF_000016765.1:WP_011952836.1 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)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
49% identity, 95% coverage: 15:386/390 of query aligns to 7:378/380 of 2pg0A
- active site: M124 (= M133), T125 (≠ S134), E243 (= E251), A364 (≠ G372), R376 (= R384)
- binding flavin-adenine dinucleotide: I122 (≠ V131), M124 (= M133), T125 (≠ S134), G130 (= G139), S131 (= S140), F155 (= F164), I156 (= I165), T157 (≠ S166), R269 (= R277), F272 (= F280), F279 (= F287), Q337 (= Q345), L338 (= L346), G340 (= G348), G341 (= G349), V359 (= V367), I362 (= I370), Y363 (= Y371), T366 (= T374), E368 (= E376), M369 (≠ I377)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
46% identity, 97% coverage: 14:390/390 of query aligns to 54:430/430 of P51174
- K318 (≠ R278) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ R282) 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.
8w0uA Human lcad complexed with acetoacetyl coenzyme a (see paper)
45% identity, 96% coverage: 14:389/390 of query aligns to 22:397/398 of 8w0uA
- binding acetoacetyl-coenzyme a: M140 (= M133), S147 (= S140), Q150 (= Q143), S193 (vs. gap), H196 (≠ R187), Y250 (≠ A242), E259 (= E251), R260 (= R252), Y379 (= Y371), G380 (= G372), G381 (= G373), I385 (= I377), L389 (= L381), R392 (= R384)
- binding flavin-adenine dinucleotide: I138 (≠ V131), M140 (= M133), T141 (≠ S134), G146 (= G139), S147 (= S140), F171 (= F164), S173 (= S166), R285 (= R277), F288 (= F280), L295 (≠ F287), Q353 (= Q345), L354 (= L346), G357 (= G349), V375 (= V367), Y379 (= Y371), T382 (= T374), E384 (= E376)
8w0tA Human lcad (see paper)
45% identity, 96% coverage: 14:389/390 of query aligns to 22:397/398 of 8w0tA
- binding flavin-adenine dinucleotide: I138 (≠ V131), M140 (= M133), T141 (≠ S134), G146 (= G139), S147 (= S140), F171 (= F164), I172 (= I165), S173 (= S166), R285 (= R277), F288 (= F280), L295 (≠ F287), Q353 (= Q345), L354 (= L346), G356 (= G348), G357 (= G349), V375 (= V367), T382 (= T374), E384 (= E376), I385 (= I377)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
45% identity, 96% coverage: 14:389/390 of query aligns to 54:429/430 of P28330
- E291 (= E251) 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 (≠ M263) to T: in dbSNP:rs1801204
- K333 (= K293) to Q: in dbSNP:rs2286963
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
36% identity, 96% coverage: 14:389/390 of query aligns to 9:387/387 of 1ivhA
- active site: M130 (= M133), S131 (= S134), E249 (= E251), A370 (≠ G372), R382 (= R384)
- binding coenzyme a persulfide: S137 (= S140), S185 (≠ A186), R186 (= R187), V239 (≠ F241), Y240 (≠ A242), M243 (= M245), E249 (= E251), R250 (= R252), G369 (≠ Y371), A370 (≠ G372), G371 (= G373), V375 (≠ I377)
- binding flavin-adenine dinucleotide: L128 (≠ V131), M130 (= M133), S131 (= S134), G136 (= G139), S137 (= S140), W161 (≠ F164), T163 (≠ S166), R275 (= R277), F278 (= F280), F285 (= F287), M288 (≠ S290), Q343 (= Q345), C344 (≠ L346), G347 (= G349), T372 (= T374), E374 (= E376)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
36% identity, 96% coverage: 14:389/390 of query aligns to 13:391/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S134), G140 (= G139), S141 (= S140), W165 (≠ F164), T167 (≠ S166), R279 (= R277), F282 (= F280), I286 (≠ V284), F289 (= F287), Q347 (= Q345), C348 (≠ L346), G351 (= G349), L369 (≠ V367), G375 (= G373), T376 (= T374), L382 (= L380)
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)
36% identity, 96% coverage: 14:389/390 of query aligns to 46:424/426 of P26440
- 165:174 (vs. 131:140, 80% identical) binding FAD
- S174 (= S140) binding substrate
- WIT 198:200 (≠ FIS 164:166) binding FAD
- SR 222:223 (≠ AR 186:187) binding substrate
- G250 (= G215) to A: in IVA; uncertain significance
- Y277 (≠ A242) binding substrate
- DLER 284:287 (≠ PQER 249:252) binding substrate
- E286 (= E251) 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 (= A256) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R277) binding FAD
- Q323 (= Q288) binding FAD
- I379 (≠ L344) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QLFGG 345:349) binding FAD
- R398 (≠ K363) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ F368) to N: in IVA; uncertain significance
- A407 (≠ G372) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ GG 372:373) binding substrate
- TSE 409:411 (= TSE 374:376) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
38% identity, 86% coverage: 52:386/390 of query aligns to 40:372/374 of 5lnxD
- active site: L122 (≠ M133), T123 (≠ S134), G239 (≠ E251), E358 (≠ G372), K370 (≠ R384)
- binding flavin-adenine dinucleotide: L122 (≠ M133), T123 (≠ S134), G128 (= G139), S129 (= S140), F153 (= F164), T155 (≠ S166), R265 (= R277), Q267 (≠ A279), F268 (= F280), I272 (≠ V284), N275 (≠ F287), I278 (≠ S290), Q331 (= Q345), I332 (≠ L346), G335 (= G349), Y357 (= Y371), T360 (= T374), E362 (= E376)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
35% identity, 96% coverage: 12:386/390 of query aligns to 3:376/378 of 5ol2F
- active site: L124 (≠ M133), T125 (≠ S134), G241 (≠ E251), G374 (≠ R384)
- binding calcium ion: E29 (≠ R38), E33 (= E42), R35 (≠ G44)
- binding coenzyme a persulfide: L238 (= L248), R242 (= R252), E362 (≠ G372), G363 (= G373)
- binding flavin-adenine dinucleotide: F122 (≠ V131), L124 (≠ M133), T125 (≠ S134), P127 (= P136), T131 (≠ S140), F155 (= F164), I156 (= I165), T157 (≠ S166), E198 (≠ L208), R267 (= R277), F270 (= F280), L274 (≠ V284), F277 (= F287), Q335 (= Q345), L336 (= L346), G338 (= G348), G339 (= G349), Y361 (= Y371), T364 (= T374), E366 (= E376)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
34% identity, 96% coverage: 14:389/390 of query aligns to 6:380/380 of 4l1fA
- active site: L125 (≠ M133), T126 (≠ S134), G242 (≠ E251), E363 (≠ G372), R375 (= R384)
- binding coenzyme a persulfide: T132 (≠ S140), H179 (≠ R187), F232 (= F241), M236 (= M245), E237 (= E246), L239 (= L248), D240 (≠ P249), R243 (= R252), Y362 (= Y371), E363 (≠ G372), G364 (= G373), R375 (= R384)
- binding flavin-adenine dinucleotide: F123 (≠ V131), L125 (≠ M133), T126 (≠ S134), G131 (= G139), T132 (≠ S140), F156 (= F164), I157 (= I165), T158 (≠ S166), R268 (= R277), Q270 (≠ A279), F271 (= F280), I275 (≠ V284), F278 (= F287), L281 (≠ S290), Q336 (= Q345), I337 (≠ L346), G340 (= G349), I358 (≠ V367), Y362 (= Y371), T365 (= T374), Q367 (≠ E376)
- binding 1,3-propandiol: Q10 (≠ R18)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
36% identity, 96% coverage: 11:386/390 of query aligns to 1:378/378 of 4n5fA
- active site: L126 (≠ M133), T127 (≠ S134), G243 (≠ E251), E364 (≠ G372), R376 (= R384)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M133), T127 (≠ S134), G132 (= G139), S133 (= S140), F157 (= F164), T159 (≠ S166), T210 (= T218), Y363 (= Y371), T366 (= T374), E368 (= E376), M372 (≠ L380)
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
33% identity, 98% coverage: 9:389/390 of query aligns to 2:380/381 of 2jifA
- active site: L125 (≠ M133), S126 (= S134), G242 (≠ E251), E363 (≠ G372), K375 (≠ R384)
- binding coenzyme a persulfide: S132 (= S140), S134 (≠ L142), Y178 (≠ A186), Y232 (≠ F241), I236 (≠ M245), L239 (= L248), N240 (≠ P249), R243 (= R252), Y362 (= Y371), E363 (≠ G372), G364 (= G373), I368 (= I377)
- binding flavin-adenine dinucleotide: F123 (≠ V131), L125 (≠ M133), S126 (= S134), G131 (= G139), S132 (= S140), W156 (≠ F164), I157 (= I165), S158 (= S166), K201 (= K210), T209 (= T218), R268 (= R277), F271 (= F280), L275 (≠ V284), F278 (= F287), L281 (≠ S290), E336 (≠ Q345), W337 (≠ L346), G340 (= G349), N367 (≠ E376), I368 (= I377)
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)
33% identity, 98% coverage: 9:389/390 of query aligns to 53:431/432 of P45954
- V137 (≠ F93) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ A94) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 131:140, 60% identical) binding in other chain
- S183 (= S140) binding substrate
- WIS 207:209 (≠ FIS 164:166) binding in other chain
- S210 (≠ N167) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ A186) binding substrate
- L255 (≠ Q213) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F241) binding substrate
- NEGR 291:294 (≠ PQER 249:252) binding substrate
- I316 (≠ T274) to V: in dbSNP:rs1131430
- R319 (= R277) binding FAD
- Q330 (= Q288) binding FAD
- EWMGG 387:391 (≠ QLFGG 345:349) binding FAD
- A416 (≠ T374) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TSE 374:376) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
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)
36% identity, 86% coverage: 53:386/390 of query aligns to 36:367/369 of 3pfdC
- active site: L116 (≠ M133), S117 (= S134), T233 (≠ E251), E353 (≠ G372), R365 (= R384)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ V131), L116 (≠ M133), S117 (= S134), G122 (= G139), S123 (= S140), W147 (≠ F164), I148 (= I165), T149 (≠ S166), R259 (= R277), F262 (= F280), V266 (= V284), N269 (≠ F287), Q326 (= Q345), L327 (= L346), G330 (= G349), I348 (≠ V367), Y352 (= Y371), T355 (= T374), Q357 (≠ E376)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
36% identity, 85% coverage: 56:386/390 of query aligns to 47:376/379 of 1ukwB
- active site: L124 (≠ M133), S125 (= S134), T241 (≠ E251), E362 (≠ G372), R374 (= R384)
- binding cobalt (ii) ion: D145 (= D154), H146 (= H155)
- binding flavin-adenine dinucleotide: F122 (≠ V131), L124 (≠ M133), S125 (= S134), G130 (= G139), S131 (= S140), W155 (≠ F164), S157 (= S166), K200 (= K210), L357 (≠ V367), Y361 (= Y371), E362 (≠ G372), T364 (= T374), E366 (= E376), L370 (= L380)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
36% identity, 85% coverage: 56:386/390 of query aligns to 47:376/379 of 1ukwA
- active site: L124 (≠ M133), S125 (= S134), T241 (≠ E251), E362 (≠ G372), R374 (= R384)
- binding flavin-adenine dinucleotide: F122 (≠ V131), L124 (≠ M133), S125 (= S134), G130 (= G139), S131 (= S140), W155 (≠ F164), S157 (= S166), L357 (≠ V367), Y361 (= Y371), E362 (≠ G372), T364 (= T374), E366 (= E376), L370 (= L380)
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
34% identity, 96% coverage: 14:386/390 of query aligns to 5:376/376 of 4m9aB
- active site: L124 (≠ M133), T125 (≠ S134), G241 (≠ E251), E362 (≠ G372), R374 (= R384)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ V131), T125 (≠ S134), G130 (= G139), S131 (= S140), F155 (= F164), T157 (≠ S166), T208 (= T218), Y361 (= Y371), T364 (= T374), E366 (= E376), M370 (≠ L380)
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
36% identity, 97% coverage: 9:386/390 of query aligns to 1:377/378 of 3r7kA
- active site: V126 (≠ M133), T127 (≠ S134), E242 (= E251), G363 (= G372), K375 (≠ R384)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ M133), T127 (≠ S134), G132 (= G139), S133 (= S140), F157 (= F164), I158 (= I165), T159 (≠ S166), R268 (= R277), T270 (≠ A279), F271 (= F280), L275 (≠ V284), R278 (≠ F287), I281 (≠ S290), Q336 (= Q345), I337 (≠ L346), G340 (= G349), I358 (≠ V367), T365 (= T374), E367 (= E376)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
37% identity, 86% coverage: 52:388/390 of query aligns to 72:412/412 of P15651
- 152:161 (vs. 131:140, 70% identical) binding FAD
- S161 (= S140) binding substrate
- WIT 185:187 (≠ FIS 164:166) binding FAD
- DMGR 269:272 (≠ PQER 249:252) binding substrate
- R297 (= R277) binding FAD
- QILGG 365:369 (≠ QLFGG 345:349) binding FAD
- E392 (≠ G372) active site, Proton acceptor
- TSE 394:396 (= TSE 374:376) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
Query Sequence
>WP_011952836.1 NCBI__GCF_000016765.1:WP_011952836.1
MSAIDVARPAHMDSEELRMFEDSVSRFLAAHAGPDRTRHWREQGFVDRDTWRAAGEAGLL
GLSVPVEYGGAGVDFTFDAVIMEQLGRHHALNFAIPLHNAVVAPYIVSYANEEQKRRWLP
GVVTGETILAVAMSEPGAGSDLQAMKTSARREGDHYVINGQKTFISNGAHASLIIVAAKT
DPEAGARGLSLFAVETDEVEGFTRGRLLDKIGQEGRDTAELFFSDMRVPVENRIGPEGGG
FAMLMEKLPQERLVIAWQALAMMEAAIDHTIAYTAERRAFGRAVLDFQNSQFKLAECKTQ
ATIARVFLDHCTQQLLAGTLDAATASMAKYWITEAQGKVIDECLQLFGGYGYMTEYPIAE
MYKDARVFRIYGGTSEIMKLLIARSLRSDA
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