SitesBLAST
Comparing BPHYT_RS25380 FitnessBrowser__BFirm:BPHYT_RS25380 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)
4x28A Crystal structure of the chse4-chse5 complex from mycobacterium tuberculosis (see paper)
36% identity, 88% coverage: 50:399/399 of query aligns to 45:382/386 of 4x28A
- active site: Y122 (≠ F128), S123 (= S129), E240 (= E244), G365 (= G382), M377 (≠ K394)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), S123 (= S129), G128 (= G134), T129 (≠ S135), W153 (= W159), S155 (= S161), F363 (vs. gap), T367 (= T384), E369 (= E386), V370 (= V387)
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)
35% identity, 88% coverage: 50:399/399 of query aligns to 52:395/400 of I6YCA3
- IGYS 127:130 (≠ QGFS 126:129) binding
- T136 (≠ S135) binding
- S162 (= S161) binding
- E247 (= E244) mutation to A: Loss of dehydrogenase activity.
- TNE 380:382 (≠ TSE 384:386) binding
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)
37% identity, 84% coverage: 60:393/399 of query aligns to 58:376/387 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)
33% identity, 96% coverage: 17:399/399 of query aligns to 348:709/711 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)
31% identity, 99% coverage: 1:395/399 of query aligns to 1:377/384 of 6wy8B
- active site: Y126 (≠ F128), T127 (≠ S129), E241 (= E244), T376 (≠ K394)
- binding flavin-adenine dinucleotide: I124 (≠ Q126), Y126 (≠ F128), T127 (≠ S129), G132 (= G134), T133 (≠ S135), F157 (≠ W159), S159 (= S161), V359 (≠ A377), F362 (≠ I380), G363 (≠ Y381), V366 (≠ T384), E368 (= E386)
6wy9A Tcur3481-tcur3483 steroid acad g363a variant (see paper)
31% identity, 97% coverage: 7:395/399 of query aligns to 3:373/380 of 6wy9A
- active site: Y122 (≠ F128), T123 (≠ S129), E237 (= E244), T372 (≠ K394)
- binding dihydroflavine-adenine dinucleotide: I120 (≠ Q126), Y122 (≠ F128), T123 (≠ S129), G128 (= G134), T129 (≠ S135), F153 (≠ W159), S155 (= S161), F358 (≠ I380), V362 (≠ T384), E364 (= E386)
1rx0A Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
28% identity, 91% coverage: 35:398/399 of query aligns to 25:383/384 of 1rx0A
- active site: L129 (≠ F128), T130 (≠ S129), G245 (≠ E244), E367 (≠ G382), R379 (≠ K394)
- binding flavin-adenine dinucleotide: Y127 (≠ Q126), L129 (≠ F128), T130 (≠ S129), G135 (= G134), S136 (= S135), F160 (≠ W159), I161 (≠ T160), S162 (= S161), W207 (vs. gap), R271 (≠ T267), F274 (≠ V270), L278 (= L275), N281 (≠ Q278), L284 (≠ F281), Q340 (≠ E337), M341 (≠ A338), G343 (= G340), G344 (≠ D341), Y345 (= Y342), L366 (≠ Y381), S369 (≠ T384), E371 (= E386)
1rx0C Crystal structure of isobutyryl-coa dehydrogenase complexed with substrate/ligand. (see paper)
28% identity, 91% coverage: 35:398/399 of query aligns to 24:382/383 of 1rx0C
- active site: L128 (≠ F128), T129 (≠ S129), G244 (≠ E244), E366 (≠ G382), R378 (≠ K394)
- binding methacrylyl-coenzyme a: I93 (vs. gap), Y126 (≠ Q126), S135 (= S135), V238 (≠ K238), L241 (= L241), N242 (= N242), R245 (≠ H245), V316 (≠ H314), E366 (≠ G382), G367 (= G383), L375 (≠ I391), R378 (≠ K394)
- binding flavin-adenine dinucleotide: Y126 (≠ Q126), L128 (≠ F128), T129 (≠ S129), G134 (= G134), S135 (= S135), F159 (≠ W159), I160 (≠ T160), S161 (= S161), R270 (≠ T267), F273 (≠ V270), N280 (≠ Q278), L283 (≠ F281), Q339 (≠ E337), M340 (≠ A338), G342 (= G340), G343 (≠ D341), Y344 (= Y342), L365 (≠ Y381), S368 (≠ T384), E370 (= E386)
Q9UKU7 Isobutyryl-CoA dehydrogenase, mitochondrial; IBDH; Activator-recruited cofactor 42 kDa component; ARC42; Acyl-CoA dehydrogenase family member 8; ACAD-8; EC 1.3.8.5 from Homo sapiens (Human) (see 3 papers)
28% identity, 91% coverage: 35:398/399 of query aligns to 56:414/415 of Q9UKU7
- G137 (≠ A105) to R: in IBDD; loss of protein solubility; complete loss of isobutyryl-CoA dehydrogenase activity; dbSNP:rs371449613
- 158:167 (vs. 126:135, 60% identical) binding in other chain
- S167 (= S135) binding
- FIS 191:193 (≠ WTS 159:161) binding in other chain
- NGGR 274:277 (≠ NNEH 242:245) binding
- R302 (≠ T267) binding ; to Q: in IBDD; no effect on localization to the mitochondrion; complete loss of isobutyryl-CoA dehydrogenase activity; loss of protein expression in patient cells; dbSNP:rs121908422
- NQ 312:313 (≠ QP 278:279) binding
- A320 (= A286) to T: in IBDD; decreased isobutyryl-CoA dehydrogenase activity; less than 20% of wild-type; dbSNP:rs200620279
- QMHGG 371:375 (≠ EALGD 337:341) binding
- SNE 400:402 (≠ TSE 384:386) binding in other chain
- R410 (≠ K394) binding
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
28% identity, 88% coverage: 46:396/399 of query aligns to 42:378/380 of 2pg0A
- active site: M124 (≠ F128), T125 (≠ S129), E243 (= E244), A364 (≠ G382), R376 (≠ K394)
- binding flavin-adenine dinucleotide: I122 (≠ Q126), M124 (≠ F128), T125 (≠ S129), G130 (= G134), S131 (= S135), F155 (≠ W159), I156 (≠ T160), T157 (≠ S161), R269 (= R269), F272 (≠ C272), F279 (vs. gap), Q337 (≠ G340), L338 (≠ D341), G340 (= G343), G341 (≠ A344), V359 (≠ A377), I362 (= I380), Y363 (= Y381), T366 (= T384), E368 (= E386), M369 (≠ V387)
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 83% coverage: 65:397/399 of query aligns to 60:377/379 of 1ukwB
- active site: L124 (≠ F128), S125 (= S129), T241 (≠ E244), E362 (≠ G382), R374 (≠ K394)
- binding cobalt (ii) ion: D145 (= D149), H146 (= H150)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ F128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (= S161), K200 (≠ R203), L357 (≠ A377), Y361 (= Y381), E362 (≠ G382), T364 (= T384), E366 (= E386), L370 (≠ G390)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
29% identity, 83% coverage: 65:397/399 of query aligns to 60:377/379 of 1ukwA
- active site: L124 (≠ F128), S125 (= S129), T241 (≠ E244), E362 (≠ G382), R374 (≠ K394)
- binding flavin-adenine dinucleotide: F122 (≠ Q126), L124 (≠ F128), S125 (= S129), G130 (= G134), S131 (= S135), W155 (= W159), S157 (= S161), L357 (≠ A377), Y361 (= Y381), E362 (≠ G382), T364 (= T384), E366 (= E386), L370 (≠ G390)
1egcA Structure of t255e, e376g mutant of human medium chain acyl-coa dehydrogenase complexed with octanoyl-coa (see paper)
27% identity, 83% coverage: 65:394/399 of query aligns to 62:379/387 of 1egcA
- active site: V126 (≠ F128), T127 (≠ S129), E246 (= E244), G367 (= G382), R379 (≠ K394)
- binding octanoyl-coenzyme a: E90 (≠ A93), L94 (= L97), Y124 (vs. gap), S133 (= S135), V135 (≠ L137), N182 (≠ G184), F236 (≠ W234), M240 (≠ K238), F243 (≠ L241), D244 (≠ N242), R247 (≠ H245), Y366 (= Y381), G367 (= G382), G368 (= G383)
- binding flavin-adenine dinucleotide: Y124 (vs. gap), V126 (≠ F128), T127 (≠ S129), G132 (= G134), S133 (= S135), W157 (= W159), T159 (≠ S161), R272 (≠ Q268), T274 (≠ V270), F275 (≠ G271), L279 (= L275), H282 (≠ Q278), I285 (≠ F281), Q340 (≠ E337), I341 (≠ A338), G344 (≠ D341), I362 (≠ F373), I365 (= I380), Y366 (= Y381), T369 (= T384), Q371 (≠ E386)
P11310 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; Medium chain acyl-CoA dehydrogenase; MCADH; EC 1.3.8.7 from Homo sapiens (Human) (see 16 papers)
26% identity, 83% coverage: 65:394/399 of query aligns to 96:413/421 of P11310
- L98 (≠ T67) mutation to W: Strongly reduced rate of electron transfer to ETF.
- L100 (≠ W69) mutation to Y: Strongly reduced rate of electron transfer to ETF.
- I108 (≠ F77) mutation to M: Strongly reduced rate of electron transfer to ETF.
- P132 (≠ L101) to R: in a breast cancer sample; somatic mutation; dbSNP:rs875989854
- 158:167 (vs. 127:135, 50% identical) binding in other chain
- S167 (= S135) binding
- W191 (= W159) mutation to A: Loss of electron transfer to ETF.; mutation to F: Reduces rate of electron transfer to ETF about six-fold.
- WIT 191:193 (≠ WTS 159:161) binding in other chain
- T193 (≠ S161) to A: in ACADMD; the thermostability is markedly decreased; dbSNP:rs121434279
- E237 (≠ P201) mutation to A: Strongly reduced rate of electron transfer to ETF.
- D278 (≠ N242) binding
- T280 (≠ E244) mutation to E: Narrower substrate specificity. Changed substrate specificity towards longer acyl chains; when associated with G-401. Loss of acyl-CoA dehydrogenase activity; when associated with T-410.
- R281 (≠ H245) binding ; to T: in ACADMD; mild clinical phenotype; dbSNP:rs121434282
- RKT 306:308 (≠ QRV 268:270) binding
- HQ 316:317 (≠ QP 278:279) binding in other chain
- K329 (≠ E291) to E: in ACADMD; may alter splicing; decreased fatty acid beta-oxidation; dbSNP:rs77931234
- QILGG 374:378 (≠ EALGD 337:341) binding
- E384 (≠ A346) mutation to A: Reduces rate of electron transfer to ETF three-fold.; mutation to Q: Reduces rate of electron transfer to ETF two-fold.
- E401 (≠ G382) active site, Proton acceptor; binding ; mutation to G: Changed substrate specificity towards longer acyl chains; when associated with E-280.; mutation to Q: Loss of acyl-CoA dehydrogenase activity.; mutation to T: Loss of acyl-CoA dehydrogenase activity; when associated with E-280.
- EGTSQ 401:405 (≠ GGTSE 382:386) binding in other chain
Sites not aligning to the query:
- 67 Y → H: in ACADMD; mild; dbSNP:rs121434280
- 86 L→M: Strongly reduced rate of electron transfer to ETF.
2a1tC Structure of the human mcad:etf e165betaa complex (see paper)
26% identity, 83% coverage: 65:394/399 of query aligns to 63:380/388 of 2a1tC
- active site: V127 (≠ F128), T128 (≠ S129), T247 (≠ E244), E368 (≠ G382), R380 (≠ K394)
- binding flavin-adenine dinucleotide: Y125 (vs. gap), V127 (≠ F128), T128 (≠ S129), G133 (= G134), S134 (= S135), Q155 (= Q156), W158 (= W159), W158 (= W159), I159 (≠ T160), T160 (≠ S161), R273 (≠ Q268), T275 (≠ V270), F276 (≠ G271), L280 (= L275), H283 (≠ Q278), I286 (≠ F281), Q341 (≠ E337), I342 (≠ A338), G345 (≠ D341), I363 (≠ F373), T370 (= T384), Q372 (≠ E386)
3mdeA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
26% identity, 83% coverage: 65:394/399 of query aligns to 61:378/385 of 3mdeA
- active site: V125 (≠ F128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G382), R378 (≠ K394)
- binding octanoyl-coenzyme a: T86 (≠ D90), E89 (≠ A93), L93 (= L97), S132 (= S135), V134 (≠ L137), S181 (≠ G184), F235 (≠ W234), M239 (≠ K238), F242 (≠ L241), R314 (≠ A312), Y365 (= Y381), E366 (≠ G382), G367 (= G383)
- binding flavin-adenine dinucleotide: Y123 (vs. gap), V125 (≠ F128), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), I157 (≠ T160), T158 (≠ S161), R271 (≠ Q268), T273 (≠ V270), F274 (≠ G271), L278 (= L275), H281 (≠ Q278), Q339 (≠ E337), V340 (≠ A338), G343 (≠ D341), I361 (≠ F373), T368 (= T384), Q370 (≠ E386)
3mddA Crystal structures of medium chain acyl-coa dehydrogenase from pig liver mitochondria with and without substrate (see paper)
26% identity, 83% coverage: 65:394/399 of query aligns to 61:378/385 of 3mddA
- active site: V125 (≠ F128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G382), R378 (≠ K394)
- binding flavin-adenine dinucleotide: Y123 (vs. gap), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), T158 (≠ S161), R271 (≠ Q268), T273 (≠ V270), F274 (≠ G271), H281 (≠ Q278), Q339 (≠ E337), V340 (≠ A338), G343 (≠ D341), I361 (≠ F373), T368 (= T384), Q370 (≠ E386)
1udyA Medium-chain acyl-coa dehydrogenase with 3-thiaoctanoyl-coa (see paper)
26% identity, 83% coverage: 65:394/399 of query aligns to 61:378/385 of 1udyA
- active site: V125 (≠ F128), T126 (≠ S129), T245 (≠ E244), E366 (≠ G382), R378 (≠ K394)
- binding 3-thiaoctanoyl-coenzyme a: L93 (= L97), Y123 (vs. gap), S132 (= S135), S181 (≠ G184), F235 (≠ W234), M239 (≠ K238), F242 (≠ L241), V249 (≠ A246), R314 (≠ A312), Y365 (= Y381), E366 (≠ G382), G367 (= G383), I371 (≠ V387), I375 (= I391)
- binding flavin-adenine dinucleotide: Y123 (vs. gap), T126 (≠ S129), G131 (= G134), S132 (= S135), W156 (= W159), T158 (≠ S161), T273 (≠ V270), F274 (≠ G271), Q339 (≠ E337), V340 (≠ A338), G343 (≠ D341), T368 (= T384), Q370 (≠ E386)
P41367 Medium-chain specific acyl-CoA dehydrogenase, mitochondrial; MCAD; EC 1.3.8.7 from Sus scrofa (Pig) (see 2 papers)
26% identity, 83% coverage: 65:394/399 of query aligns to 96:413/421 of P41367
- 158:167 (vs. 127:135, 50% identical) binding in other chain
- S167 (= S135) binding
- WIT 191:193 (≠ WTS 159:161) binding in other chain
- S216 (≠ G184) binding
- D278 (≠ N242) binding
- R281 (≠ H245) binding
- RKT 306:308 (≠ QRV 268:270) binding
- HQ 316:317 (≠ QP 278:279) binding in other chain
- R349 (≠ A312) binding
- T351 (≠ H314) binding
- QVFGG 374:378 (≠ EALGD 337:341) binding
- E401 (≠ G382) active site, Proton acceptor; binding
- GTAQ 402:405 (≠ GTSE 383:386) binding in other chain
8hk0B Crystal structure of fic32-33 complex from streptomyces ficellus nrrl 8067 (see paper)
32% identity, 58% coverage: 12:244/399 of query aligns to 12:243/379 of 8hk0B
Sites not aligning to the query:
Query Sequence
>BPHYT_RS25380 FitnessBrowser__BFirm:BPHYT_RS25380
MDFQPDAGLEAFREQVRAFLREHLPRDLAGKPVGSVRSMRPDLVRWQKILNQQGWGAPYW
AKKDGGTGWSVLQRLVFDEECIAAGAPTQDGFAQKLLGPVLNEFASPEQKGEHVPLILAG
ERLWCQGFSEPGSGSDLASLRTRAERDGDHYIVNGQKIWTSYAHESDWIFLLVRTDTEVK
KQAGISFLLVDMKTPGITVRPIRSIDDCHHLNETFFDNVRVPVANRVGAEGAGWTITKFL
LNNEHASAADLPILRRYLMQLRTLAATQRVGCEPLIAQPAFALRLARLEAEVSAVATMVK
RVAAMEQDHSPAAHAMGSILKVRGTELQQRISELMVEALGDYGAVAYPEPHDTCEAEPLP
HQDVARGLANEMFFRRASTIYGGTSEVQRGIIAKMLFQL
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