SitesBLAST
Comparing 18212 FitnessBrowser__Keio:18212 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)
P33224 Putative acyl-CoA dehydrogenase AidB; EC 1.3.99.- from Escherichia coli (strain K12) (see paper)
100% identity, 100% coverage: 1:541/541 of query aligns to 1:541/541 of P33224
- 182:191 (vs. 182:191, 100% identical) binding
- T185 (= T185) binding
- S191 (= S191) binding
- FFS 216:218 (= FFS 216:218) binding
- S218 (= S218) binding
- 423:433 (vs. 423:433, 100% identical) binding
- N429 (= N429) binding
- R437 (= R437) mutation to Q: Does not affect DNA binding affinity.
- R518 (= R518) mutation to Q: Reduces DNA binding affinity.
3u33A Crystal structure of the e. Coli adaptive response protein aidb in the space group p3(2) (see paper)
100% identity, 100% coverage: 1:540/541 of query aligns to 1:540/540 of 3u33A
- active site: M184 (= M184), T185 (= T185), T298 (= T298), E425 (= E425), R437 (= R437)
- binding flavin-adenine dinucleotide: M182 (= M182), M184 (= M184), T185 (= T185), G190 (= G190), S191 (= S191), F216 (= F216), S218 (= S218), R324 (= R324), F327 (= F327), L331 (= L331), Q334 (= Q334), M337 (= M337), E398 (= E398), V399 (= V399), G401 (= G401), G402 (= G402), W424 (= W424), G426 (= G426), S427 (= S427), N429 (= N429), L433 (= L433)
5ez3B Crystal structure acyl-coa dehydrogenase from brucella melitensis in complex with fad
45% identity, 95% coverage: 4:515/541 of query aligns to 1:513/541 of 5ez3B
- active site: M181 (= M184), T182 (= T185), T295 (= T298), E423 (= E425), R435 (= R437)
- binding flavin-adenine dinucleotide: M181 (= M184), T182 (= T185), G186 (= G189), G187 (= G190), T188 (≠ S191), F213 (= F216), S215 (= S218), R321 (= R324), F324 (= F327), L328 (= L331), Q331 (= Q334), M334 (= M337), E396 (= E398), C397 (≠ V399), G399 (= G401), G400 (= G402), W422 (= W424), E423 (= E425), S425 (= S427), N427 (= N429), L431 (= L433)
4y9jB Crystal structure of caenorhabditis elegans acdh-11 in complex with c11-coa (see paper)
30% identity, 90% coverage: 43:530/541 of query aligns to 54:583/593 of 4y9jB
- active site: M190 (= M184), T191 (= T185), T315 (= T298), E446 (= E425), R458 (= R437)
- binding flavin-adenine dinucleotide: Q188 (≠ M182), M190 (= M184), T191 (= T185), G196 (= G190), S197 (= S191), F223 (= F216), S224 (≠ F217), S225 (= S218), R341 (= R324), V343 (= V326), F344 (= F327), Q348 (≠ L331), E419 (= E398), C420 (≠ V399), G422 (= G401), G423 (= G402), Y426 (= Y405), W445 (= W424), T448 (≠ S427), V451 (≠ I430), L454 (= L433)
- binding S-{(3S,5R,9R)-1-[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]-3,5,9-trihydroxy-8,8-dimethyl-3,5-dioxido-10,14-dioxo-2,4,6-trioxa-11,15-diaza-3lambda~5~,5lambda~5~-diphosphaheptadecan-17-yl} undecanethioate: S143 (≠ L132), A147 (≠ T136), Q188 (≠ M182), S197 (= S191), S249 (vs. gap), R303 (≠ E286), V305 (≠ I288), S309 (≠ L292), L312 (≠ G295), N313 (≠ G296), R316 (= R299), A322 (≠ G305), R396 (= R375), W445 (= W424), E446 (= E425), V451 (≠ I430), R458 (= R437)
Q9XWZ2 Acyl-CoA dehydrogenase family member 11; EC 1.3.99.- from Caenorhabditis elegans (see paper)
30% identity, 90% coverage: 43:530/541 of query aligns to 72:601/617 of Q9XWZ2
- E91 (≠ N63) mutation to K: In n5655; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- S156 (≠ V127) mutation to F: In n5657; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G158 (≠ A129) mutation to R: In n5661; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G214 (= G190) mutation to E: In n5879; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- G443 (= G404) mutation to R: In n5877; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
- R455 (= R416) mutation to H: In n5876; suppresses the defects in egg-laying and response to reoxygenation of paqr-2 mutants.
6sdaB Bd2924 c10 acyl-coenzymea bound form (see paper)
31% identity, 71% coverage: 62:444/541 of query aligns to 57:447/503 of 6sdaB
- active site: M171 (= M184), T172 (= T185), T296 (= T298), R439 (= R437)
- binding flavin-adenine dinucleotide: Q169 (≠ M182), M171 (= M184), T172 (= T185), G177 (= G190), S178 (= S191), F208 (= F216), T209 (≠ F217), R322 (= R324), F325 (= F327), L329 (= L331), H332 (≠ Q334), E400 (= E398), M401 (≠ V399), G404 (= G402), Y407 (= Y405), W426 (= W424), T429 (≠ S427), N431 (= N429), L435 (= L433)
- binding decanoyl-CoA: C128 (= C133), G177 (= G190), S178 (= S191), S230 (vs. gap), V286 (≠ I288), A290 (≠ L292), L293 (≠ G295), N294 (≠ G296), R297 (= R299), R377 (= R375), W426 (= W424), E427 (= E425)
6sd8X Bd2924 apo-form (see paper)
31% identity, 71% coverage: 62:444/541 of query aligns to 57:447/503 of 6sd8X
- active site: M171 (= M184), T172 (= T185), T296 (= T298), R439 (= R437)
- binding flavin-adenine dinucleotide: Q169 (≠ M182), M171 (= M184), T172 (= T185), G176 (= G189), G177 (= G190), S178 (= S191), F208 (= F216), T209 (≠ F217), R322 (= R324), F325 (= F327), L329 (= L331), H332 (≠ Q334), M401 (≠ V399), G404 (= G402), W426 (= W424), T429 (≠ S427), V432 (≠ I430), L435 (= L433)
A3SI50 3-methylmercaptopropionyl-CoA dehydrogenase; MMPA-CoA dehydrogenase; EC 1.3.99.41 from Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM) (see paper)
29% identity, 55% coverage: 182:481/541 of query aligns to 161:492/591 of A3SI50
- M161 (= M182) mutation to A: Retains 37% of wild-type activity.
- T170 (≠ S191) mutation to A: Retains 8.8% of wild-type activity.
- F195 (= F216) mutation to A: Almost completely abolishes the activity.
- S197 (= S218) mutation to A: Retains 3.6% of wild-type activity.
- K223 (vs. gap) mutation to A: Retains 9.4% of wild-type activity.
- H280 (≠ G285) mutation to A: Retains 18% of wild-type activity.
- K281 (≠ E286) mutation to A: Retains 54% of wild-type activity.
- R284 (= R289) mutation to A: Retains 97% of wild-type activity.
- F287 (≠ L292) mutation to A: Retains 76% of wild-type activity.
- Y434 (≠ W424) mutation to A: Retains 51% of wild-type activity.
- E435 (= E425) mutation to A: Loss of activity.
- R448 (= R437) mutation to A: Retains 44% of wild-type activity.
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
30% identity, 51% coverage: 154:430/541 of query aligns to 104:357/371 of 2vigB
- active site: L121 (≠ M184), S122 (≠ T185), G231 (≠ T298), E352 (= E425)
- binding coenzyme a persulfide: S128 (= S191), F221 (≠ I288), M225 (≠ L292), Q226 (≠ K293), L228 (≠ G295), D229 (≠ G296), R232 (= R299), E352 (= E425), G353 (= G426), I357 (= I430)
- binding flavin-adenine dinucleotide: L121 (≠ M184), S122 (≠ T185), G127 (= G190), S128 (= S191), W152 (= W215), T154 (≠ F217), R257 (= R324), F260 (= F327), L264 (= L331), L267 (≠ Q334), Q325 (≠ E398), I326 (≠ V399), G329 (= G402), I347 (≠ V420), Y351 (≠ W424), T354 (≠ S427), E356 (≠ N429)
Sites not aligning to the query:
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
30% identity, 51% coverage: 154:430/541 of query aligns to 113:373/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L179), L130 (≠ M184), S131 (≠ T185), G136 (= G190), S137 (= S191), W161 (= W215), T163 (≠ F217), T214 (≠ S268), R273 (= R324), F276 (= F327), L280 (= L331), L283 (≠ Q334), V285 (≠ L336), Q341 (≠ E398), I342 (≠ V399), G345 (= G402), I363 (≠ V420), Y367 (≠ W424), T370 (≠ S427), E372 (≠ N429)
Sites not aligning to the query:
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
30% identity, 51% coverage: 154:430/541 of query aligns to 107:367/381 of 8sgsA
- binding coenzyme a: S131 (= S191), A133 (≠ V193), N177 (≠ A232), F231 (≠ I288), M235 (≠ L292), L238 (≠ G295), I312 (≠ A368), E362 (= E425), G363 (= G426)
- binding flavin-adenine dinucleotide: F122 (≠ L179), L124 (≠ M184), S125 (≠ T185), G130 (= G190), S131 (= S191), W155 (= W215), T157 (≠ F217), R267 (= R324), F270 (= F327), L274 (= L331), L277 (≠ Q334), Q335 (≠ E398), I336 (≠ V399), G338 (= G401), G339 (= G402), I357 (≠ V420), I360 (= I423), Y361 (≠ W424), T364 (≠ S427), E366 (≠ N429)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
30% identity, 51% coverage: 154:430/541 of query aligns to 110:370/385 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 (≠ I403), T347 (≠ E407), E348 (= E408)
- binding flavin-adenine dinucleotide: F125 (≠ L179), L127 (≠ M184), S128 (≠ T185), G133 (= G190), S134 (= S191), W158 (= W215), T160 (≠ F217), R270 (= R324), F273 (= F327), L280 (≠ Q334), V282 (≠ L336), Q338 (≠ E398), I339 (≠ V399), G342 (= G402), I360 (≠ V420), Y364 (≠ W424), T367 (≠ S427), E369 (≠ N429), I370 (= I430)
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)
30% identity, 51% coverage: 154:430/541 of query aligns to 137:397/412 of P16219
- 152:161 (vs. 179:191, 23% identical) binding in other chain
- R171 (= R202) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ WFF 215:217) binding in other chain
- A192 (≠ S222) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G234) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R324) binding
- Q308 (≠ P335) binding in other chain
- R325 (≠ T352) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ P379) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ EVLGG 398:402) binding
- R380 (= R413) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ SGN 427:429) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 90 G → S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- 104 natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
29% identity, 52% coverage: 154:435/541 of query aligns to 110:375/384 of 1jqiA
- binding acetoacetyl-coenzyme a: F125 (≠ L179), S134 (= S191), F234 (≠ I288), M238 (≠ L292), Q239 (≠ K293), L241 (≠ G295), D242 (≠ G296), R245 (= R299), Y364 (≠ W424), E365 (= E425), G366 (= G426)
- binding flavin-adenine dinucleotide: F125 (≠ L179), L127 (≠ M184), S128 (≠ T185), G133 (= G190), S134 (= S191), W158 (= W215), T160 (≠ F217), R270 (= R324), F273 (= F327), L280 (≠ Q334), Q338 (≠ E398), I339 (≠ V399), G342 (= G402), I360 (≠ V420), T367 (≠ S427), E369 (≠ N429), I370 (= I430)
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)
29% identity, 52% coverage: 154:435/541 of query aligns to 137:402/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
O53666 Broad-specificity linear acyl-CoA dehydrogenase FadE5; Long-chain-acyl-CoA dehydrogenase; Medium-chain-acyl-CoA dehydrogenase; Short-chain-acyl-CoA dehydrogenase; EC 1.3.8.8; EC 1.3.8.7; EC 1.3.8.1 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
28% identity, 53% coverage: 175:463/541 of query aligns to 155:480/611 of O53666
- MVLT 162:165 (≠ MGMT 182:185) binding
- S171 (= S191) binding ; binding ; mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- T198 (≠ S218) binding
- TK 224:225 (vs. gap) binding
- K225 (vs. gap) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- F294 (≠ L292) mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R301 (= R299) binding ; mutation to A: Increases affinity for eicosanoyl-CoA; when associated with A-447.
- R326 (= R324) binding
- K338 (vs. gap) binding
- QTLGG 420:424 (≠ EVLGG 398:402) binding
- E447 (= E425) binding ; mutation to A: Loss of activity.
- T449 (≠ S427) binding
- D456 (= D434) binding
- R460 (= R437) mutation to A: Decreases affinity for eicosanoyl-CoA; when associated with A-447.
- RK 460:461 (≠ RV 437:438) binding
3r7kA Crystal structure of a probable acyl coa dehydrogenase from mycobacterium abscessus atcc 19977 / dsm 44196 (see paper)
31% identity, 47% coverage: 177:431/541 of query aligns to 118:369/378 of 3r7kA
- active site: V126 (≠ M184), T127 (= T185), E242 (≠ T298), G363 (≠ E425)
- binding dihydroflavine-adenine dinucleotide: V126 (≠ M184), T127 (= T185), G132 (= G190), S133 (= S191), F157 (= F216), I158 (≠ F217), T159 (≠ S218), R268 (= R324), T270 (≠ V326), F271 (= F327), L275 (= L331), R278 (≠ Q334), I281 (≠ M337), Q336 (≠ E398), I337 (≠ V399), G340 (= G402), I358 (≠ V420), T365 (≠ S427), E367 (≠ N429)
Sites not aligning to the query:
1bucA Three-dimensional structure of butyryl-coa dehydrogenase from megasphaera elsdenii (see paper)
24% identity, 57% coverage: 125:433/541 of query aligns to 80:375/383 of 1bucA
- active site: L128 (≠ M184), T129 (= T185), G246 (≠ T298), E367 (= E425)
- binding acetoacetyl-coenzyme a: L96 (≠ M148), F126 (≠ M182), G134 (= G190), T135 (≠ S191), T162 (≠ S218), N182 (≠ C237), H183 (≠ F238), F236 (≠ I288), M240 (≠ L292), M241 (≠ K293), L243 (≠ G295), D244 (≠ G296), T317 (≠ R375), Y366 (≠ W424), E367 (= E425), G368 (= G426)
- binding flavin-adenine dinucleotide: F126 (≠ M182), L128 (≠ M184), T129 (= T185), G134 (= G190), T135 (≠ S191), F160 (= F216), T162 (≠ S218), Y366 (≠ W424), T369 (≠ S427), E371 (≠ N429), M375 (≠ L433)
Sites not aligning to the query:
Q06319 Acyl-CoA dehydrogenase, short-chain specific; Butyryl-CoA dehydrogenase; BCAD; SCAD; EC 1.3.8.1 from Megasphaera elsdenii (see paper)
24% identity, 57% coverage: 125:433/541 of query aligns to 80:375/383 of Q06319
- E367 (= E425) active site, Proton acceptor; mutation to Q: Loss of activity.
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
28% identity, 53% coverage: 152:439/541 of query aligns to 98:378/378 of 4n5fA
- active site: L126 (≠ M184), T127 (= T185), G243 (≠ T298), E364 (= E425), R376 (= R437)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M184), T127 (= T185), G132 (= G190), S133 (= S191), F157 (= F216), T159 (≠ S218), T210 (≠ S268), Y363 (≠ W424), T366 (≠ S427), E368 (≠ N429), M372 (≠ L433)
Query Sequence
>18212 FitnessBrowser__Keio:18212
MHWQTHTVFNQPIPLNNSNLYLSDGALCEAVTREGAGWDSDFLASIGQQLGTAESLELGR
LANVNPPELLRYDAQGRRLDDVRFHPAWHLLMQALCTNRVHNLAWEEDARSGAFVARAAR
FMLHAQVEAGSLCPITMTFAATPLLLQMLPAPFQDWTTPLLSDRYDSHLLPGGQKRGLLI
GMGMTEKQGGSDVMSNTTRAERLEDGSYRLVGHKWFFSVPQSDAHLVLAQTAGGLSCFFV
PRFLPDGQRNAIRLERLKDKLGNRSNASCEVEFQDAIGWLLGLEGEGIRLILKMGGMTRF
DCALGSHAMMRRAFSLAIYHAHQRHVFGNPLIQQPLMRHVLSRMALQLEGQTALLFRLAR
AWDRRADAKEALWARLFTPAAKFVICKRGMPFVAEAMEVLGGIGYCEESELPRLYREMPV
NSIWEGSGNIMCLDVLRVLNKQAGVYDLLSEAFVEVKGQDRYFDRAVRRLQQQLRKPAEE
LGREITHQLFLLGCGAQMLKYASPPMAQAWCQVMLDTRGGVRLSEQIQNDLLLRATGGVC
V
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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