SitesBLAST
Comparing Ga0059261_0840 FitnessBrowser__Korea:Ga0059261_0840 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)
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
32% identity, 93% coverage: 5:354/375 of query aligns to 12:369/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ D125), G140 (≠ H130), S141 (≠ G131), W165 (≠ F153), T167 (= T155), R279 (= R263), F282 (= F266), I286 (= I270), F289 (= F273), Q347 (= Q332), C348 (≠ M333), G351 (= G336), L369 (≠ V354)
Sites not aligning to the query:
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
32% identity, 93% coverage: 5:354/375 of query aligns to 8:365/387 of 1ivhA
- active site: M130 (≠ I124), S131 (≠ D125), E249 (≠ G237)
- binding coenzyme a persulfide: S137 (≠ G131), S185 (≠ D175), R186 (≠ A177), V239 (≠ R227), Y240 (≠ S228), M243 (≠ N231), E249 (≠ G237), R250 (= R238)
- binding flavin-adenine dinucleotide: L128 (= L122), M130 (≠ I124), S131 (≠ D125), G136 (≠ H130), S137 (≠ G131), W161 (≠ F153), T163 (= T155), R275 (= R263), F278 (= F266), F285 (= F273), M288 (≠ L276), Q343 (= Q332), C344 (≠ M333), G347 (= G336)
Sites not aligning to the query:
P26440 Isovaleryl-CoA dehydrogenase, mitochondrial; IVD; Butyryl-CoA dehydrogenase; EC 1.3.8.4; EC 1.3.8.1 from Homo sapiens (Human) (see 5 papers)
32% identity, 93% coverage: 5:354/375 of query aligns to 45:402/426 of P26440
- 165:174 (vs. 122:131, 30% identical) binding
- S174 (≠ G131) binding
- WIT 198:200 (≠ FVT 153:155) binding
- SR 222:223 (≠ DD 175:176) binding
- G250 (≠ S201) to A: in IVA; uncertain significance
- Y277 (≠ S228) binding
- DLER 284:287 (≠ AAGR 235:238) binding
- E286 (≠ G237) active site, Proton acceptor; mutation to D: Residual isovaleryl-CoA dehydrogenase activity.; mutation to G: Loss of isovaleryl-CoA dehydrogenase activity. Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 407-E.; mutation to Q: Loss of isovaleryl-CoA dehydrogenase activity.
- A291 (= A242) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R263) binding
- Q323 (= Q274) binding
- I379 (≠ V331) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QMHGG 332:336) binding
- R398 (≠ K350) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 403 Y → N: in IVA; uncertain significance
- 407 A→E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- 407:408 binding
- 409:411 binding
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
33% identity, 93% coverage: 5:354/375 of query aligns to 10:355/377 of 4ktoA
- active site: M130 (≠ I124), S131 (≠ D125), E239 (≠ G237)
- binding flavin-adenine dinucleotide: L128 (= L122), M130 (≠ I124), S131 (≠ D125), M155 (≠ Q152), W156 (≠ F153), T158 (= T155), R265 (= R263), F268 (= F266), I272 (= I270), F275 (= F273), M278 (≠ L276), Q333 (= Q332), A334 (≠ M333), G337 (= G336), L355 (≠ V354)
Sites not aligning to the query:
6wy8C Tcur3481-tcur3483 steroid acad (see paper)
34% identity, 97% coverage: 1:363/375 of query aligns to 1:348/364 of 6wy8C
Sites not aligning to the query:
6wy9B Tcur3481-tcur3483 steroid acad g363a variant (see paper)
34% identity, 96% coverage: 5:363/375 of query aligns to 2:345/361 of 6wy9B
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
30% identity, 94% coverage: 1:354/375 of query aligns to 1:358/380 of 4l1fA
- active site: L125 (≠ I124), T126 (≠ D125), G242 (= G237)
- binding coenzyme a persulfide: T132 (≠ K129), H179 (≠ D176), F232 (≠ R227), M236 (≠ N231), E237 (≠ A232), L239 (= L234), D240 (≠ A235), R243 (= R238)
- binding flavin-adenine dinucleotide: F123 (≠ L122), L125 (≠ I124), T126 (≠ D125), G131 (= G128), T132 (≠ K129), F156 (= F153), I157 (≠ V154), T158 (= T155), R268 (= R263), Q270 (= Q265), F271 (= F266), I275 (= I270), F278 (= F273), L281 (= L276), Q336 (= Q332), I337 (≠ M333), G340 (= G336), I358 (≠ V354)
- binding 1,3-propandiol: L5 (= L5), Q10 (≠ T10)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
28% identity, 98% coverage: 5:371/375 of query aligns to 6:375/381 of 2jifA
- active site: L125 (≠ I124), S126 (≠ D125), G242 (= G237), E363 (≠ F359), K375 (≠ R371)
- binding coenzyme a persulfide: S132 (≠ G131), S134 (≠ A133), Y178 (≠ S172), Y232 (≠ R227), I236 (≠ N231), L239 (= L234), N240 (≠ A235), R243 (= R238), Y362 (≠ M358), E363 (≠ F359), G364 (= G360), I368 (≠ F364)
- binding flavin-adenine dinucleotide: F123 (≠ L122), L125 (≠ I124), S126 (≠ D125), G131 (≠ H130), S132 (≠ G131), W156 (≠ F153), I157 (≠ V154), S158 (≠ T155), K201 (≠ L198), T209 (≠ A204), R268 (= R263), F271 (= F266), L275 (≠ I270), F278 (= F273), L281 (= L276), E336 (≠ Q332), W337 (≠ M333), G340 (= G336), N367 (= N363), I368 (≠ F364)
P45954 Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial; SBCAD; 2-methyl branched chain acyl-CoA dehydrogenase; 2-MEBCAD; 2-methylbutyryl-coenzyme A dehydrogenase; 2-methylbutyryl-CoA dehydrogenase; EC 1.3.8.5 from Homo sapiens (Human) (see 6 papers)
27% identity, 98% coverage: 5:371/375 of query aligns to 57:426/432 of P45954
- V137 (≠ P88) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (= F89) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 122:131, 20% identical) binding in other chain
- S183 (≠ G131) binding
- WIS 207:209 (≠ FVT 153:155) binding in other chain
- S210 (≠ H156) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ S172) binding
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ R227) binding
- NEGR 291:294 (≠ AAGR 235:238) binding
- I316 (≠ L260) to V: in dbSNP:rs1131430
- R319 (= R263) binding
- Q330 (= Q274) binding
- EWMGG 387:391 (≠ QMHGG 332:336) binding
- A416 (≠ D361) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ DAN 361:363) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
31% identity, 96% coverage: 4:363/375 of query aligns to 1:364/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ F89), D89 (≠ E98), S129 (≠ G131), L131 (≠ A133), K176 (≠ A177), F229 (≠ R227), M233 (≠ N231), L236 (= L234), R240 (= R238), Y360 (≠ F359), T361 (≠ G360), G362 (≠ D361)
- binding flavin-adenine dinucleotide: A122 (≠ I124), T123 (≠ D125), G128 (≠ H130), S129 (≠ G131), F153 (= F153), I154 (≠ V154), T155 (= T155), N206 (≠ A204), L356 (= L355), Y360 (≠ F359), T363 (≠ A362)
Sites not aligning to the query:
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
31% identity, 96% coverage: 4:363/375 of query aligns to 3:366/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ G131), L133 (≠ A133), K178 (≠ A177), F231 (≠ R227), M235 (≠ N231), L238 (= L234), N241 (≠ G237), R242 (= R238), Y362 (≠ F359), T363 (≠ G360), G364 (≠ D361)
- binding flavin-adenine dinucleotide: L122 (= L122), A124 (≠ I124), T125 (≠ D125), G130 (≠ H130), S131 (≠ G131), F155 (= F153), I156 (≠ V154), T157 (= T155), K200 (≠ Q196), N208 (≠ A204), L358 (= L355), T365 (≠ A362)
Sites not aligning to the query:
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
29% identity, 94% coverage: 3:355/375 of query aligns to 1:358/379 of 6fahD
- active site: L124 (≠ I124), T125 (≠ D125), G241 (= G237)
- binding flavin-adenine dinucleotide: F122 (≠ L122), L124 (≠ I124), T125 (≠ D125), R152 (≠ A150), F155 (= F153), T157 (= T155), E198 (≠ P195), R267 (= R263), Q269 (= Q265), F270 (= F266), I274 (= I270), F277 (= F273), Q335 (= Q332), I336 (≠ M333), G339 (= G336)
Sites not aligning to the query:
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
29% identity, 94% coverage: 3:354/375 of query aligns to 5:359/378 of 4n5fA
Sites not aligning to the query:
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
29% identity, 91% coverage: 5:345/375 of query aligns to 53:398/430 of P51174
- K318 (= K264) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ T268) 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
29% identity, 91% coverage: 4:345/375 of query aligns to 4:350/380 of 2pg0A
- active site: M124 (≠ I124), T125 (≠ D125), E243 (≠ G237)
- binding flavin-adenine dinucleotide: I122 (≠ L122), M124 (≠ I124), T125 (≠ D125), G130 (≠ H130), S131 (≠ G131), F155 (= F153), I156 (≠ V154), T157 (= T155), R269 (= R263), F272 (= F266), F279 (= F273), Q337 (= Q332), L338 (≠ M333), G340 (= G335), G341 (= G336)
Sites not aligning to the query:
3pfdC Crystal structure of an acyl-coa dehydrogenase from mycobacterium thermoresistibile bound to reduced flavin adenine dinucleotide solved by combined iodide ion sad mr (see paper)
30% identity, 81% coverage: 53:354/375 of query aligns to 41:348/369 of 3pfdC
- active site: L116 (≠ I124), S117 (≠ D125), T233 (≠ G237)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ L122), L116 (≠ I124), S117 (≠ D125), G122 (≠ H130), S123 (≠ G131), W147 (≠ F153), I148 (≠ V154), T149 (= T155), R259 (= R263), F262 (= F266), V266 (≠ I270), N269 (≠ F273), Q326 (= Q332), L327 (≠ M333), G330 (= G336), I348 (≠ V354)
Sites not aligning to the query:
4m9aB Crystal structure of acyl-coa dehydrogenase from burkholderia thailandensis e264
29% identity, 94% coverage: 3:354/375 of query aligns to 3:357/376 of 4m9aB
Sites not aligning to the query:
2d29A Structural study on project id tt0172 from thermus thermophilus hb8
32% identity, 93% coverage: 7:354/375 of query aligns to 9:363/386 of 2d29A
Sites not aligning to the query:
2z1qB Crystal structure of acyl coa dehydrogenase
28% identity, 80% coverage: 45:345/375 of query aligns to 61:380/549 of 2z1qB
- active site: L144 (≠ I124), T145 (≠ D125), G259 (= G237)
- binding flavin-adenine dinucleotide: Y142 (≠ L122), L144 (≠ I124), T145 (≠ D125), G150 (≠ H130), S151 (≠ G131), W177 (≠ F153), S179 (≠ T155), R285 (= R263), F288 (= F266), I292 (= I270), F295 (= F273), I298 (≠ L276), H369 (= H334), G370 (= G335)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
28% identity, 93% coverage: 7:354/375 of query aligns to 4:353/374 of 5lnxD
- active site: L122 (≠ I124), T123 (≠ D125), G239 (= G237)
- binding flavin-adenine dinucleotide: L122 (≠ I124), T123 (≠ D125), G128 (= G128), S129 (≠ K129), F153 (= F153), T155 (= T155), R265 (= R263), Q267 (= Q265), F268 (= F266), I272 (= I270), N275 (≠ F273), I278 (≠ L276), Q331 (= Q332), I332 (≠ M333), G335 (= G336)
Sites not aligning to the query:
Query Sequence
>Ga0059261_0840 FitnessBrowser__Korea:Ga0059261_0840
MPLYLNEEQTMLRDAAQQFVGEAAPVSHMRGLRDANDPTGFSRDLWKQFAEMGFTGILIP
DSHGGLGLGHVEAGVVLEEIGRNLSPSPFLTTAVAAVEALKGSAQRERWFPGILAGETVA
ALAIDEKGKHGNAVAMKAERSGNGFRLSGAKQFVTHGHVADLLIVAARTAGSPDDDAGVT
LFAVAKDAAGLTADPQRLADSSLASRLTFENVEVDADAVIGEVDGGRSILNALLAAGRTG
AAAESLGVGGGAMDLTVQYLKERKQFGTLIGSFQALQHRAAHLYTELEVARAAVLKAQQL
LDAGDAKAGEAVSVAKAMAGLASTLAVQEGVQMHGGIGMTDEFDIGFYMKRGRVLAEMFG
DANFHADQLARASGY
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