SitesBLAST
Comparing RR42_RS28375 FitnessBrowser__Cup4G11:RR42_RS28375 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)
6wy8B Tcur3481-tcur3483 steroid acad (see paper)
32% identity, 99% coverage: 1:396/402 of query aligns to 1:375/384 of 6wy8B
- active site: Y126 (≠ F128), T127 (≠ S129), E241 (= E247)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (≠ F128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W161), S159 (= S163), V359 (≠ D377), F362 (≠ I383), G363 (≠ Y384), V366 (= V387), E368 (= E389)
Sites not aligning to the query:
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
32% identity, 97% coverage: 7:396/402 of query aligns to 3:371/380 of 6wy9A
- active site: Y122 (≠ F128), T123 (≠ S129), E237 (= E247)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W161), S155 (= S163), F358 (≠ I383), V362 (= V387), E364 (= E389)
Sites not aligning to the query:
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
33% identity, 100% coverage: 1:400/402 of query aligns to 1:380/386 of 4x28A
- active site: Y122 (≠ F128), S123 (= S129), E240 (= E247), G365 (= G385), M377 (≠ K397)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W161), S155 (= S163), F363 (≠ I383), T367 (≠ V387), E369 (= E389), V370 (= V390)
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)
33% identity, 100% coverage: 1:400/402 of query aligns to 1:393/400 of I6YCA3
- IGYS 127:130 (≠ QGFS 126:129) binding
- T136 (≠ S135) binding
- S162 (= S163) binding
- E247 (= E247) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ VNE 387:389) binding
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)
32% identity, 86% coverage: 54:400/402 of query aligns to 392:707/711 of P96855
- E581 (= E247) 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.
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)
30% identity, 100% coverage: 1:400/402 of query aligns to 1:380/387 of P71858
- E241 (= E247) mutation to Q: Unable to dehydrogenate pregnene-carboxyl-CoA ester.
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
30% identity, 96% coverage: 15:399/402 of query aligns to 24:373/379 of 8hk0B
- binding flavin-adenine dinucleotide: V126 (≠ Q126), Y128 (≠ F128), T129 (≠ S129), G134 (= G134), S135 (= S135), F159 (≠ W161), S160 (≠ T162), L161 (≠ S163), G354 (≠ K380), S358 (≠ Y384), T361 (≠ V387), E363 (= E389)
2z1qB Crystal structure of acyl coa dehydrogenase
27% identity, 91% coverage: 37:400/402 of query aligns to 49:409/549 of 2z1qB
- active site: L144 (≠ F128), T145 (≠ S129), G259 (= G245), E394 (≠ G385), G406 (≠ K397)
- binding flavin-adenine dinucleotide: Y142 (≠ Q126), L144 (≠ F128), T145 (≠ S129), G150 (= G134), S151 (= S135), W177 (= W161), S179 (= S163), R285 (vs. gap), F288 (vs. gap), I292 (≠ L273), F295 (≠ D276), I298 (≠ L279), H369 (≠ A336), G370 (= G337), F393 (≠ Y384), I399 (≠ V390)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
28% identity, 99% coverage: 5:400/402 of query aligns to 3:377/379 of 6fahD
- active site: L124 (≠ F128), T125 (≠ S129), G241 (≠ E247), G374 (≠ K397)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ F128), T125 (≠ S129), R152 (≠ H158), F155 (≠ W161), T157 (≠ S163), E198 (≠ R206), R267 (≠ Q271), Q269 (≠ L273), F270 (≠ G274), I274 (≠ V278), F277 (≠ C281), Q335 (≠ E334), I336 (≠ V335), G339 (≠ P338), Y361 (= Y384), T364 (≠ V387), Q366 (≠ E389)
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
26% identity, 99% coverage: 5:401/402 of query aligns to 53:428/430 of P51174
- K318 (≠ G272) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ D276) 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.
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
26% identity, 86% coverage: 54:397/402 of query aligns to 49:376/380 of 2pg0A
- active site: M124 (≠ F128), T125 (≠ S129), E243 (= E247), A364 (≠ G385), R376 (≠ K397)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ F128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W161), I156 (≠ T162), T157 (≠ S163), R269 (= R265), F272 (≠ D269), F279 (≠ D276), Q337 (≠ A347), L338 (≠ M348), G340 (= G350), G341 (≠ A351), V359 (≠ K380), I362 (= I383), Y363 (= Y384), T366 (≠ V387), E368 (= E389), M369 (≠ V390)
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
27% identity, 77% coverage: 90:400/402 of query aligns to 136:427/430 of P28330
- E291 (= E247) 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 (vs. gap) to T: in dbSNP:rs1801204
- K333 (≠ R282) to Q: in dbSNP:rs2286963
P49748 Very long-chain specific acyl-CoA dehydrogenase, mitochondrial; VLCAD; EC 1.3.8.9 from Homo sapiens (Human) (see 8 papers)
28% identity, 59% coverage: 101:337/402 of query aligns to 189:438/655 of P49748
- 214:223 (vs. 126:135, 40% identical) binding
- WIS 249:251 (≠ WTS 161:163) binding
Sites not aligning to the query:
- 1:40 modified: transit peptide, Mitochondrion
- 458 F → L: in ACADVLD; loss of acyl-CoA dehydrogenase activity; Loss of FAD cofactor-binding; dbSNP:rs118204017; F→T: Decreased acyl-CoA dehydrogenase activity. Decreased affinity for acyl-CoA. No effect on FAD cofactor-binding.; F→V: Loss of acyl-CoA dehydrogenase activity. Loss of FAD cofactor-binding.; F→Y: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. Decreased FAD cofactor-binding.
- 461:463 binding
- 462 active site, Proton acceptor; E→D: Decreased acyl-CoA dehydrogenase activity. No effect on affinity for acyl-CoA. No effect on FAD cofactor-binding.; E→Q: Loss of acyl-CoA dehydrogenase activity. No effect on FAD cofactor-binding.
- 464:466 binding
- 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
- 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)
28% identity, 59% coverage: 101:337/402 of query aligns to 121:370/554 of 3b96A
- active site: L148 (≠ F128), T149 (≠ S129), G272 (≠ E247)
- binding flavin-adenine dinucleotide: F146 (≠ Q126), L148 (≠ F128), T149 (≠ S129), G154 (= G134), S155 (= S135), W181 (= W161), I182 (≠ T162), S183 (= S163)
- binding tetradecanoyl-coa: F146 (≠ Q126), L269 (= L244)
Sites not aligning to the query:
2uxwA Crystal structure of human very long chain acyl-coa dehydrogenase (acadvl)
28% identity, 59% coverage: 101:337/402 of query aligns to 121:370/567 of 2uxwA
- active site: L148 (≠ F128), T149 (≠ S129), G272 (≠ E247)
- binding flavin-adenine dinucleotide: F146 (≠ Q126), L148 (≠ F128), T149 (≠ S129), G154 (= G134), S155 (= S135), W181 (= W161), I182 (≠ T162), S183 (= S163)
- binding trans delta2 palmitenoyl-coenzymea: F146 (≠ Q126), L269 (= L244)
Sites not aligning to the query:
- active site: 21, 394, 406
- binding flavin-adenine dinucleotide: 393, 396, 398, 399, 474
- binding trans delta2 palmitenoyl-coenzymea: 96, 107, 110, 393, 394, 395
7s7gA Crystal structure analysis of human vlcad
28% identity, 59% coverage: 101:337/402 of query aligns to 121:370/571 of 7s7gA
Sites not aligning to the query:
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
27% identity, 88% coverage: 47:400/402 of query aligns to 43:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S135), T134 (≠ L137), R180 (≠ Q185), R234 (≠ S238), L237 (≠ K241), R238 (≠ Y242), L240 (= L244), D241 (≠ G245), R244 (= R248), E365 (≠ G385), G366 (= G386), R377 (≠ K397)
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W161), I157 (≠ T162), T158 (≠ S163), I360 (≠ K380), T367 (≠ V387), Q369 (≠ E389)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
27% identity, 88% coverage: 47:400/402 of query aligns to 43:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ Q126), L125 (≠ F128), S126 (= S129), G131 (= G134), S132 (= S135), W156 (= W161), I157 (≠ T162), T158 (≠ S163), I360 (≠ K380), Y364 (= Y384), T367 (≠ V387), Q369 (≠ E389)
7w0jE Acyl-coa dehydrogenase, tfu_1647
27% identity, 88% coverage: 47:400/402 of query aligns to 44:381/382 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 (= W161), R270 (≠ Q260), Q272 (≠ A262), F273 (≠ R263), I277 (≠ L267), F280 (≠ E270), I283 (≠ L273), Q339 (≠ A347), L340 (≠ M348), G343 (≠ A351), Y365 (= Y384), E366 (≠ G385), T368 (≠ V387), Q370 (≠ E389), I371 (≠ V390)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
28% identity, 85% coverage: 61:400/402 of query aligns to 85:407/412 of P16219
- G90 (= G66) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E80) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 126:135, 60% identical) binding in other chain
- R171 (≠ V145) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WTS 161:163) binding in other chain
- A192 (≠ C168) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G187) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (≠ Q271) binding
- Q308 (≠ R282) binding in other chain
- R325 (= R299) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ T322) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QI-------------LGG 365:369 (≠ EVAGPHAVPFDEAAMLGA 334:351) binding
- R380 (≠ A373) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ VNE 387:389) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
Query Sequence
>RR42_RS28375 FitnessBrowser__Cup4G11:RR42_RS28375
MQLEFSAADDAFRQEVRAFVKARLPSDIKRKVELGLRLEHADYVTWFRILEARGWITPGW
PVEHGGPGWSHLQRYIFDEETLLGGAPRIIASGIQMLGPVLIAFGTPEQKARYLPDIRHS
NTWWAQGFSEPGAGSDLAAVRTTAVLEPDGRHFVVNGHKVWTSYAHWCSMMFALVRTDPD
AAKPQEGISFILIDMASPGVEVRPIRMLEGGTDLNECYLDNVRVPVENLVGEINKGWSYG
KYLLGHERTGIAGIGSCKQQLARARTLADEQGLGDDAVLQCRLAQFEIELMALEYTALRL
LGDNQRSRVPSVEASMLKVRGTELRQAIYELLVEVAGPHAVPFDEAAMLGAAGYEQSTAA
DAASPPTLAALAANYLDSRKLSIYGGVNEVQRNLISKAFLAA
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