SitesBLAST
Comparing WP_084057203.1 NCBI__GCF_900176285.1:WP_084057203.1 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)
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)
36% identity, 89% coverage: 15:490/532 of query aligns to 70:567/621 of Q9H845
- R193 (≠ H134) to W: in MC1DN20; uncertain significance; dbSNP:rs377547811
- S234 (vs. gap) to F: in MC1DN20; uncertain significance
- G303 (= G239) to S: in MC1DN20; uncertain significance; dbSNP:rs143383023
- A326 (= A262) to T: in MC1DN20; uncertain significance; dbSNP:rs115532916
- E413 (= E349) to K: in MC1DN20; uncertain significance; dbSNP:rs149753643
- E426 (= E362) 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, 89% coverage: 17:490/532 of query aligns to 35:497/551 of 8pheA
- binding : L143 (= L121), D151 (= D129), A153 (≠ K131), S154 (≠ H132), I155 (= I133), K202 (≠ P175), I205 (≠ M178), F256 (= F229), M260 (= M233), F295 (= F268), N296 (≠ G269), I394 (= I367), Y398 (= Y371), L401 (= L374), Q405 (≠ R378), K451 (= K444), M454 (= M447)
8phfA Cryo-em structure of human acad9-s191a (see paper)
37% identity, 89% coverage: 17:490/532 of query aligns to 35:493/547 of 8phfA
- binding flavin-adenine dinucleotide: T144 (= T122), W176 (≠ Y154), K225 (= K198), R292 (= R265), Q294 (= Q267), F295 (= F268), F302 (= F275), L304 (= L277), I305 (= I278), I363 (≠ T336), G365 (= G338), G366 (= G339), F388 (= F361), E393 (= E366), M397 (≠ I370), Q453 (≠ E450)
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
35% identity, 88% coverage: 24:490/532 of query aligns to 51:514/567 of 2uxwA
- active site: L148 (= L121), T149 (= T122), G272 (= G239), E394 (= E362), L406 (= L374)
- binding flavin-adenine dinucleotide: F146 (≠ Y119), L148 (= L121), T149 (= T122), G154 (= G127), S155 (= S128), W181 (≠ Y154), I182 (= I155), S183 (≠ T156), F393 (= F361), T396 (= T364), D398 (≠ E366), I399 (= I367), Q474 (≠ E450)
- binding trans delta2 palmitenoyl-coenzymea: V96 (≠ I69), G107 (≠ A80), L110 (≠ S83), F146 (≠ Y119), L269 (= L236), F393 (= F361), E394 (= E362), G395 (= G363)
Sites not aligning to the query:
7s7gA Crystal structure analysis of human vlcad (see paper)
35% identity, 88% coverage: 24:490/532 of query aligns to 51:518/571 of 7s7gA
- binding flavin-adenine dinucleotide: F146 (≠ Y119), L148 (= L121), T149 (= T122), G154 (= G127), S155 (= S128), W181 (≠ Y154), I182 (= I155), S183 (≠ T156), I389 (≠ V357), T396 (= T364), D398 (≠ E366), I399 (= I367), Q478 (≠ E450)
3b96A Structural basis for substrate fatty-acyl chain specificity: crystal structure of human very-long-chain acyl-coa dehydrogenase (see paper)
34% identity, 88% coverage: 24:490/532 of query aligns to 51:501/554 of 3b96A
- active site: L148 (= L121), T149 (= T122), G272 (= G239), E394 (= E362), L406 (= L374)
- binding flavin-adenine dinucleotide: F146 (≠ Y119), L148 (= L121), T149 (= T122), G154 (= G127), S155 (= S128), W181 (≠ Y154), I182 (= I155), S183 (≠ T156), I389 (≠ V357), F393 (= F361), T396 (= T364), D398 (≠ E366), I399 (= I367), Q461 (≠ E450)
- binding tetradecanoyl-coa: V96 (≠ I69), G107 (≠ A80), F146 (≠ Y119), L269 (= L236), F393 (= F361), E394 (= E362)
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
34% identity, 88% coverage: 24:490/532 of query aligns to 119:602/655 of P49748
- 214:223 (vs. 119:128, 60% identical) binding FAD
- WIS 249:251 (≠ YIT 154:156) binding FAD
- F458 (≠ T358) 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 361:363) binding substrate
- E462 (= E362) 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 (≠ TTE 364:366) binding FAD
- A490 (≠ L398) to 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.
- L502 (≠ V410) to P: in ACADVLD; decreased association with mitochondrial inner membrane; decreased specific activity towards several substrates in vitro
- E534 (≠ K425) to K: in ACADVLD; uncertain significance; dbSNP:rs2230180
- Q562 (≠ E450) binding FAD
- S583 (≠ A471) to W: in ACADVLD; Loss of homodimerization; loss of localization to mitochondrial inner membrane; dbSNP:rs1085307648
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
8ca1B Cryo-em structure of the acadvl dimer from mus musculus. (see paper)
32% identity, 94% coverage: 24:521/532 of query aligns to 53:569/589 of 8ca1B
- binding flavin-adenine dinucleotide: F148 (≠ Y119), T151 (= T122), G156 (= G127), S157 (= S128), W183 (≠ Y154), S185 (≠ T156), R300 (= R265), Q302 (= Q267), F303 (= F268), I307 (= I272), V312 (≠ L277), I313 (= I278), Q369 (= Q335), I370 (≠ T336), F395 (= F361), D400 (≠ E366), I401 (= I367)
P50544 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; MVLCAD; VLCAD; EC 1.3.8.9 from Mus musculus (Mouse) (see paper)
32% identity, 94% coverage: 24:521/532 of query aligns to 120:636/656 of P50544
- C238 (≠ D142) modified: S-nitrosocysteine
2z1qB Crystal structure of acyl coa dehydrogenase
40% identity, 69% coverage: 18:383/532 of query aligns to 46:415/549 of 2z1qB
- active site: L144 (= L121), T145 (= T122), G259 (= G239), E394 (= E362), G406 (≠ L374)
- binding flavin-adenine dinucleotide: Y142 (= Y119), L144 (= L121), T145 (= T122), G150 (= G127), S151 (= S128), W177 (≠ Y154), S179 (≠ T156), R285 (= R265), F288 (= F268), I292 (= I272), F295 (= F275), I298 (= I278), H369 (≠ A337), G370 (= G338), F393 (= F361), I399 (= I367)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
39% identity, 66% coverage: 18:370/532 of query aligns to 12:366/374 of 5lnxD
- active site: L122 (= L121), T123 (= T122), G239 (= G239), E358 (= E362)
- binding flavin-adenine dinucleotide: L122 (= L121), T123 (= T122), G128 (= G127), S129 (= S128), F153 (≠ Y154), T155 (= T156), R265 (= R265), Q267 (= Q267), F268 (= F268), I272 (= I272), N275 (≠ F275), I278 (= I278), Q331 (= Q335), I332 (≠ T336), G335 (= G339), Y357 (≠ F361), T360 (= T364), E362 (= E366)
Sites not aligning to the query:
3owaC Crystal structure of acyl-coa dehydrogenase complexed with fad from bacillus anthracis
39% identity, 65% coverage: 37:382/532 of query aligns to 60:418/587 of 3owaC
- active site: L143 (= L121), T144 (= T122), G258 (= G239), E398 (= E362), G410 (≠ L374)
- binding flavin-adenine dinucleotide: Y141 (= Y119), L143 (= L121), T144 (= T122), G149 (= G127), S150 (= S128), W176 (≠ Y154), I177 (= I155), T178 (= T156), R284 (= R265), F287 (= F268), I291 (= I272), F294 (= F275), Q371 (= Q335), I372 (≠ T336), G375 (= G339), I393 (≠ V357), F397 (= F361), T400 (= T364), E402 (= E366), I403 (= I367), L406 (≠ I370)
Sites not aligning to the query:
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
37% identity, 64% coverage: 26:368/532 of query aligns to 29:368/378 of 5ol2F
- active site: L124 (= L121), T125 (= T122), G241 (= G239)
- binding calcium ion: E29 (= E26), E33 (≠ L30), R35 (= R32)
- binding coenzyme a persulfide: L238 (= L236), R242 (= R240), E362 (= E362), G363 (= G363)
- binding flavin-adenine dinucleotide: F122 (≠ Y119), L124 (= L121), T125 (= T122), P127 (= P124), T131 (≠ S128), F155 (≠ Y154), I156 (= I155), T157 (= T156), E198 (≠ M196), R267 (= R265), F270 (= F268), L274 (≠ I272), F277 (= F275), Q335 (= Q335), L336 (≠ T336), G338 (= G338), G339 (= G339), Y361 (≠ F361), T364 (= T364), E366 (= E366)
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
37% identity, 63% coverage: 36:370/532 of query aligns to 40:371/380 of 4l1fA
- active site: L125 (= L121), T126 (= T122), G242 (= G239), E363 (= E362)
- binding coenzyme a persulfide: T132 (≠ S128), H179 (= H177), F232 (= F229), M236 (= M233), E237 (≠ T234), L239 (= L236), D240 (≠ N237), R243 (= R240), Y362 (≠ F361), E363 (= E362), G364 (= G363)
- binding flavin-adenine dinucleotide: F123 (≠ Y119), L125 (= L121), T126 (= T122), G131 (= G127), T132 (≠ S128), F156 (≠ Y154), I157 (= I155), T158 (= T156), R268 (= R265), Q270 (= Q267), F271 (= F268), I275 (= I272), F278 (= F275), L281 (≠ I278), Q336 (= Q335), I337 (≠ T336), G340 (= G339), I358 (≠ V357), Y362 (≠ F361), T365 (= T364), Q367 (≠ E366)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
38% identity, 63% coverage: 33:368/532 of query aligns to 38:370/378 of 4n5fA
- active site: L126 (= L121), T127 (= T122), G243 (= G239), E364 (= E362)
- binding dihydroflavine-adenine dinucleotide: L126 (= L121), T127 (= T122), G132 (= G127), S133 (= S128), F157 (≠ Y154), T159 (= T156), T210 (= T206), Y363 (≠ F361), T366 (= T364), E368 (= E366)
Sites not aligning to the query:
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
36% identity, 63% coverage: 33:368/532 of query aligns to 36:368/376 of 4m9aB
- active site: L124 (= L121), T125 (= T122), G241 (= G239), E362 (= E362)
- binding dihydroflavine-adenine dinucleotide: F122 (≠ Y119), T125 (= T122), G130 (= G127), S131 (= S128), F155 (≠ Y154), T157 (= T156), T208 (= T206), Y361 (≠ F361), T364 (= T364), E366 (= E366)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
38% identity, 65% coverage: 26:370/532 of query aligns to 29:370/379 of 6fahD
- active site: L124 (= L121), T125 (= T122), G241 (= G239)
- binding flavin-adenine dinucleotide: F122 (≠ Y119), L124 (= L121), T125 (= T122), R152 (= R151), F155 (≠ Y154), T157 (= T156), E198 (≠ M196), R267 (= R265), Q269 (= Q267), F270 (= F268), I274 (= I272), F277 (= F275), Q335 (= Q335), I336 (≠ T336), G339 (= G339), Y361 (≠ F361), T364 (= T364), Q366 (≠ E366)
Sites not aligning to the query:
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
36% identity, 63% coverage: 34:370/532 of query aligns to 67:400/412 of P15651
- 152:161 (vs. 119:128, 60% identical) binding FAD
- S161 (= S128) binding substrate
- WIT 185:187 (≠ YIT 154:156) binding FAD
- DMGR 269:272 (≠ NFGR 237:240) binding substrate
- R297 (= R265) binding FAD
- QILGG 365:369 (≠ QTAGG 335:339) binding FAD
- E392 (= E362) active site, Proton acceptor
- TSE 394:396 (≠ TTE 364:366) 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)
36% identity, 63% coverage: 34:370/532 of query aligns to 40:373/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (≠ I89), F125 (≠ Y119), S134 (= S128), F234 (= F229), M238 (= M233), Q239 (≠ T234), L241 (= L236), D242 (≠ N237), R245 (= R240), Y364 (≠ F361), E365 (= E362), G366 (= G363)
- binding flavin-adenine dinucleotide: F125 (≠ Y119), L127 (= L121), S128 (≠ T122), G133 (= G127), S134 (= S128), W158 (≠ Y154), T160 (= T156), R270 (= R265), F273 (= F268), L280 (≠ F275), Q338 (= Q335), I339 (≠ T336), G342 (= G339), I360 (≠ V357), T367 (= T364), E369 (= E366), I370 (= I367)
Sites not aligning to the query:
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
36% identity, 63% coverage: 34:370/532 of query aligns to 67:400/412 of P16219
- G90 (= G57) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E71) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 119:128, 60% identical) binding in other chain
- R171 (≠ V138) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ YIT 154:156) binding in other chain
- A192 (= A161) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (≠ H177) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R265) binding FAD
- Q308 (≠ E276) binding in other chain
- R325 (≠ A294) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ T323) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QTAGG 335:339) binding FAD
- R380 (≠ K350) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TTE 364:366) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
Query Sequence
>WP_084057203.1 NCBI__GCF_900176285.1:WP_084057203.1
MHVNRARVEELVVAYEGLLQQFSPQEIESLGRVPDEMIGKMGQVGLFGFSIAKEYGGLGF
NLWEYLEVIRELARRDLSVALVSIAHLSIGVKGIQLFGTEEQKAKYLPLAASGDMIFSYA
LTEPHIGSDAKHIHTTAVLSDDETHYVLNGRKTYITNANYAGGLTVFAQLDPEKPGHMGA
FIVETDWEGVQIGKDMPKMGLTASSTAAIHFKDVKVPRENLLGKPGDGFKIAMTILNFGR
LGLGAASTGLMDQSATDMAKRAANRIQFGVPIENFELIQEKIVRARAHAFACDAMTTLTA
LFLEEDPHRNVAMETSHVKLFGTTRAWDVLYDALQTAGGSGYLKTNPYEKRLRDFRVTTI
FEGTTEIHSIYPPLFAIRRMTKEMAGTEQGVLGSLKVLWKHLTGGLQWDVPFRDKQLRCA
ARQAKRNARYLKFALPAVAMIHRKKVMSKEYVLRRLTTLSLYTYAILAMLARMQKDLDRG
LLSTEHRLFLDYMLEEMKECRRSCLRLWNTRKEKISARLFRWERFFREESTQ
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