SitesBLAST
Comparing WP_015945287.1 NCBI__GCF_000021925.1:WP_015945287.1 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)
3owaC Crystal structure of acyl-coa dehydrogenase complexed with fad from bacillus anthracis
53% identity, 99% coverage: 7:590/591 of query aligns to 2:587/587 of 3owaC
- active site: L143 (= L148), T144 (= T149), G258 (= G262), E398 (= E401), G410 (= G413)
- binding flavin-adenine dinucleotide: Y141 (= Y146), L143 (= L148), T144 (= T149), G149 (= G154), S150 (= S155), W176 (≠ F181), I177 (= I182), T178 (= T183), R284 (= R288), F287 (= F291), I291 (≠ L295), F294 (= F298), Q371 (= Q374), I372 (= I375), G375 (= G378), I393 (= I396), F397 (= F400), T400 (= T403), E402 (= E405), I403 (= I406), L406 (= L409), Q480 (= Q482)
2z1qB Crystal structure of acyl coa dehydrogenase
51% identity, 99% coverage: 4:590/591 of query aligns to 2:547/549 of 2z1qB
- active site: L144 (= L148), T145 (= T149), G259 (= G262), E394 (= E401), G406 (= G413)
- binding flavin-adenine dinucleotide: Y142 (= Y146), L144 (= L148), T145 (= T149), G150 (= G154), S151 (= S155), W177 (≠ F181), S179 (≠ T183), R285 (= R288), F288 (= F291), I292 (≠ L295), F295 (= F298), I298 (= I301), H369 (= H376), G370 (= G377), F393 (= F400), I399 (= I406), Q448 (= Q482)
Q9H845 Complex I assembly factor ACAD9, mitochondrial; Acyl-CoA dehydrogenase family member 9; ACAD-9; EC 1.3.8.- from Homo sapiens (Human) (see 4 papers)
42% identity, 69% coverage: 12:419/591 of query aligns to 43:444/621 of Q9H845
- R193 (≠ K161) to W: in MC1DN20; uncertain significance; dbSNP:rs377547811
- S234 (vs. gap) to F: in MC1DN20; uncertain significance
- G303 (= G262) to S: in MC1DN20; uncertain significance; dbSNP:rs143383023
- A326 (= A285) to T: in MC1DN20; uncertain significance; dbSNP:rs115532916
- E413 (= E388) to K: in MC1DN20; uncertain significance; dbSNP:rs149753643
- E426 (= E401) mutation to Q: Loss of long-chain-acyl-CoA dehydrogenase activity. Does not affect mitochondrial complex I assembly.
Sites not aligning to the query:
- 1:37 modified: transit peptide, Mitochondrion
8pheA Acad9-wt in complex with ecsit-cter (see paper)
37% identity, 88% coverage: 13:530/591 of query aligns to 7:506/551 of 8pheA
- binding : L143 (= L148), D151 (= D156), A153 (≠ L158), S154 (≠ G159), I155 (≠ A160), K202 (vs. gap), I205 (≠ L201), F256 (≠ H252), M260 (≠ F256), F295 (= F291), N296 (≠ G292), I394 (= I406), Y398 (≠ L410), L401 (≠ G413), Q405 (≠ K417), K451 (≠ M476), M454 (≠ K479)
8phfA Cryo-em structure of human acad9-s191a (see paper)
42% identity, 69% coverage: 13:419/591 of query aligns to 7:407/547 of 8phfA
- binding flavin-adenine dinucleotide: T144 (= T149), W176 (≠ F181), K225 (= K221), R292 (= R288), Q294 (= Q290), F295 (= F291), F302 (= F298), L304 (≠ A300), I305 (= I301), I363 (= I375), G365 (= G377), G366 (= G378), F388 (= F400), E393 (= E405), M397 (≠ L409)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
40% identity, 65% coverage: 30:416/591 of query aligns to 4:373/374 of 5lnxD
- active site: L122 (= L148), T123 (= T149), G239 (= G262), E358 (= E401), K370 (≠ G413)
- binding flavin-adenine dinucleotide: L122 (= L148), T123 (= T149), G128 (= G154), S129 (= S155), F153 (= F181), T155 (= T183), R265 (= R288), Q267 (= Q290), F268 (= F291), I272 (≠ L295), N275 (≠ F298), I278 (= I301), Q331 (= Q374), I332 (= I375), G335 (= G378), Y357 (≠ F400), T360 (= T403), E362 (= E405)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
40% identity, 66% coverage: 27:417/591 of query aligns to 2:378/378 of 5ol2F
- active site: L124 (= L148), T125 (= T149), G241 (= G262), G374 (= G413)
- binding calcium ion: E29 (≠ A53), E33 (≠ Q57), R35 (≠ D59)
- binding coenzyme a persulfide: L238 (= L259), R242 (= R263), E362 (= E401), G363 (= G402)
- binding flavin-adenine dinucleotide: F122 (≠ Y146), L124 (= L148), T125 (= T149), P127 (= P151), T131 (≠ S155), F155 (= F181), I156 (= I182), T157 (= T183), E198 (= E219), R267 (= R288), F270 (= F291), L274 (= L295), F277 (= F298), Q335 (= Q374), L336 (≠ I375), G338 (= G377), G339 (= G378), Y361 (≠ F400), T364 (= T403), E366 (= E405)
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
40% identity, 68% coverage: 11:411/591 of query aligns to 76:472/655 of P49748
- 214:223 (vs. 146:155, 80% identical) binding FAD
- WIS 249:251 (≠ FIT 181:183) binding FAD
- F458 (≠ N397) to L: in ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding; dbSNP:rs118204017; mutation to T: Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to V: Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.; mutation to Y: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
- FEG 461:463 (= FEG 400:402) binding substrate
- E462 (= E401) active site, Proton acceptor; mutation to D: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.; mutation to Q: Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
- TND 464:466 (≠ TNE 403:405) binding FAD
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
- 490 A → P: in ACADVLD; decreased association with mitochondrial inner membrane; may affect substrate specificity, possibly reducing the affinity for long-chain acyl-CoA substrates; dbSNP:rs759775666; mutation A->G,V,S,D,H: Changed substrate specificity with decreased affinity for tetradecanoyl-CoA and hexadecanoyl-CoA.
- 502 L → P: in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro
- 534 E → K: in ACADVLD; uncertain significance; dbSNP:rs2230180
- 562 binding FAD
- 583 S → W: in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane; dbSNP:rs1085307648
3b96A Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-coa dehydrogenase (see paper)
40% identity, 68% coverage: 11:411/591 of query aligns to 8:404/554 of 3b96A
- active site: L148 (= L148), T149 (= T149), G272 (= G262), E394 (= E401)
- binding flavin-adenine dinucleotide: F146 (≠ Y146), L148 (= L148), T149 (= T149), G154 (= G154), S155 (= S155), W181 (≠ F181), I182 (= I182), S183 (≠ T183), I389 (= I396), F393 (= F400), T396 (= T403), D398 (≠ E405), I399 (= I406)
- binding tetradecanoyl-coa: V96 (≠ G97), G107 (≠ A107), F146 (≠ Y146), L269 (= L259), F393 (= F400), E394 (= E401)
Sites not aligning to the query:
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
40% identity, 68% coverage: 11:411/591 of query aligns to 8:404/567 of 2uxwA
- active site: P21 (vs. gap), L148 (= L148), T149 (= T149), G272 (= G262), E394 (= E401)
- binding flavin-adenine dinucleotide: F146 (≠ Y146), L148 (= L148), T149 (= T149), G154 (= G154), S155 (= S155), W181 (≠ F181), I182 (= I182), S183 (≠ T183), F393 (= F400), T396 (= T403), D398 (≠ E405), I399 (= I406)
- binding trans delta2 palmitenoyl-coenzymea: V96 (≠ G97), G107 (≠ A107), L110 (≠ F110), F146 (≠ Y146), L269 (= L259), F393 (= F400), E394 (= E401), G395 (= G402)
Sites not aligning to the query:
7s7gA Crystal structure analysis of human vlcad (see paper)
40% identity, 68% coverage: 11:411/591 of query aligns to 8:404/571 of 7s7gA
- binding flavin-adenine dinucleotide: F146 (≠ Y146), L148 (= L148), T149 (= T149), G154 (= G154), S155 (= S155), W181 (≠ F181), I182 (= I182), S183 (≠ T183), I389 (= I396), T396 (= T403), D398 (≠ E405), I399 (= I406)
Sites not aligning to the query:
8ca1B Cryo-em structure of the acadvl dimer from mus musculus. (see paper)
39% identity, 68% coverage: 11:411/591 of query aligns to 10:406/589 of 8ca1B
- binding flavin-adenine dinucleotide: F148 (≠ Y146), T151 (= T149), G156 (= G154), S157 (= S155), W183 (≠ F181), S185 (≠ T183), R300 (= R288), Q302 (= Q290), F303 (= F291), I307 (≠ L295), V312 (≠ A300), I313 (= I301), Q369 (= Q374), I370 (= I375), F395 (= F400), D400 (≠ E405), I401 (= I406)
P50544 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; MVLCAD; VLCAD; EC 1.3.8.9 from Mus musculus (Mouse) (see paper)
39% identity, 68% coverage: 11:411/591 of query aligns to 77:473/656 of P50544
- C238 (≠ E169) modified: S-nitrosocysteine
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
38% identity, 66% coverage: 28:418/591 of query aligns to 3:379/379 of 6fahD
- active site: L124 (= L148), T125 (= T149), G241 (= G262), G374 (= G413)
- binding flavin-adenine dinucleotide: F122 (≠ Y146), L124 (= L148), T125 (= T149), R152 (≠ T178), F155 (= F181), T157 (= T183), E198 (= E219), R267 (= R288), Q269 (= Q290), F270 (= F291), I274 (≠ L295), F277 (= F298), Q335 (= Q374), I336 (= I375), G339 (= G378), Y361 (≠ F400), T364 (= T403), Q366 (≠ E405)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
38% identity, 67% coverage: 22:417/591 of query aligns to 28:408/412 of P16219
- G90 (= G85) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E99) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 146:155, 60% identical) binding in other chain
- R171 (≠ N167) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ FIT 181:183) binding in other chain
- A192 (= A188) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (vs. gap) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R288) binding FAD
- Q308 (≠ G299) binding in other chain
- R325 (≠ E316) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S362) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 374:378) binding FAD
- R380 (= R389) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNE 403:405) 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
38% identity, 67% coverage: 22:417/591 of query aligns to 4:384/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ Y146), L130 (= L148), S131 (≠ T149), G136 (= G154), S137 (= S155), W161 (≠ F181), T163 (= T183), T214 (= T229), R273 (= R288), F276 (= F291), L280 (= L295), L283 (≠ F298), V285 (≠ A300), Q341 (= Q374), I342 (= I375), G345 (= G378), I363 (= I396), Y367 (≠ F400), T370 (= T403), E372 (= E405), L376 (= L409)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
38% identity, 67% coverage: 22:417/591 of query aligns to 1:381/385 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 (≠ Y379), T347 (≠ A383), E348 (= E384)
- binding flavin-adenine dinucleotide: F125 (≠ Y146), L127 (= L148), S128 (≠ T149), G133 (= G154), S134 (= S155), W158 (≠ F181), T160 (= T183), R270 (= R288), F273 (= F291), L280 (≠ F298), V282 (≠ A300), Q338 (= Q374), I339 (= I375), G342 (= G378), I360 (= I396), Y364 (≠ F400), T367 (= T403), E369 (= E405), I370 (= I406), L373 (= L409)
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, 67% coverage: 22:417/591 of query aligns to 28:408/412 of P15651
- 152:161 (vs. 146:155, 60% identical) binding FAD
- S161 (= S155) binding substrate
- WIT 185:187 (≠ FIT 181:183) binding FAD
- DMGR 269:272 (≠ NVGR 260:263) binding substrate
- R297 (= R288) binding FAD
- QILGG 365:369 (≠ QIHGG 374:378) binding FAD
- E392 (= E401) active site, Proton acceptor
- TSE 394:396 (≠ TNE 403:405) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
37% identity, 67% coverage: 22:417/591 of query aligns to 1:381/384 of 1jqiA
- active site: G377 (= G413)
- binding acetoacetyl-coenzyme a: L95 (≠ I116), F125 (≠ Y146), S134 (= S155), F234 (≠ H252), M238 (≠ F256), Q239 (≠ N257), L241 (= L259), D242 (≠ N260), R245 (= R263), Y364 (≠ F400), E365 (= E401), G366 (= G402)
- binding flavin-adenine dinucleotide: F125 (≠ Y146), L127 (= L148), S128 (≠ T149), G133 (= G154), S134 (= S155), W158 (≠ F181), T160 (= T183), R270 (= R288), F273 (= F291), L280 (≠ F298), Q338 (= Q374), I339 (= I375), G342 (= G378), I360 (= I396), T367 (= T403), E369 (= E405), I370 (= I406)
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
38% identity, 66% coverage: 27:417/591 of query aligns to 3:378/381 of 8sgsA
- binding coenzyme a: S131 (= S155), A133 (= A157), N177 (= N203), F231 (≠ H252), M235 (≠ F256), L238 (= L259), I312 (≠ A351), E362 (= E401), G363 (= G402)
- binding flavin-adenine dinucleotide: F122 (≠ Y146), L124 (= L148), S125 (≠ T149), G130 (= G154), S131 (= S155), W155 (≠ F181), T157 (= T183), R267 (= R288), F270 (= F291), L274 (= L295), L277 (≠ F298), Q335 (= Q374), I336 (= I375), G338 (= G377), G339 (= G378), I357 (= I396), I360 (≠ L399), Y361 (≠ F400), T364 (= T403), E366 (= E405)
Query Sequence
>WP_015945287.1 NCBI__GCF_000021925.1:WP_015945287.1
MELELGLKGGGFLLAEVTPEQVYVPEELNEDHLQLKKMTRNFVEKEIGPKIEALEEQEDG
LIRDFMAQAGELGLLGLEVPEELGGMSMDKFSTVVVGEEIPRGASFAVAFMAHTGIGTLP
IVYFGTPEQKAKYLPGLATGEKIAAYCLTEPGSGSDALGAKATAVLNAEGTHYLLNGTKQ
FITNAGFADIFLVYAKVEGKLTNFIVERTMPGLSFGPEEKKMGIKGSSTRQVILEDVAVP
VENIVGELGRGHVVAFNILNVGRFKLAAAAIGSAQLALEVTLKYAAERKQFGVPLSSFGA
IQTKFAEIAAQTYLAESVVYRTAGLMEEACQDLDVTGDCRKEAGKAIEEYAIECSLNKVL
ASEVLDLAVDEGVQIHGGYGFIAEYPIERMYRDSRINRLFEGTNEINRLLVPGTLLKRAM
SGELPLLAAAKNVSKDLMSAGLGSEEEGLAALLNMTQKAKKLCLMAAGIAAQNLGMELKD
NQYVLLGLAEMVLQVYAMESGVLRALKVQDMDVTEDHKLFVEKAATLGAYSAMNIIEQHA
KEVICAAEQGDSLSTVLAGMRKLLRRPTVDMIGLRREIAKLVVEKGKYPVR
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