SitesBLAST
Comparing CCNA_01369 FitnessBrowser__Caulo:CCNA_01369 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)
6af6A Piga with fad and proline (see paper)
31% identity, 91% coverage: 1:346/379 of query aligns to 1:351/383 of 6af6A
- active site: A127 (≠ Y125), T128 (≠ A126), A244 (= A238)
- binding flavin-adenine dinucleotide: N125 (≠ F123), A127 (≠ Y125), T128 (≠ A126), G133 (≠ R131), S134 (≠ Y132), F158 (≠ V156), I159 (≠ V157), T160 (≠ V158), W211 (≠ A207)
- binding 1,4,7,10,13,16-hexaoxacyclooctadecane: L41 (≠ Y43), K44 (≠ A46), K275 (≠ T269), F280 (= F274)
- binding proline: G133 (≠ R131), I136 (≠ W134), F237 (≠ V231), M241 (= M235)
Sites not aligning to the query:
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
25% identity, 93% coverage: 5:357/379 of query aligns to 12:371/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ A126), G140 (≠ R131), S141 (≠ Y132), W165 (≠ V156), T167 (≠ V158), R279 (= R264), F282 (= F267), I286 (= I271), F289 (= F274), Q347 (= Q333), C348 (≠ I334), G351 (= G337), L369 (≠ M355)
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)
25% identity, 93% coverage: 5:357/379 of query aligns to 8:367/387 of 1ivhA
- active site: M130 (≠ Y125), S131 (≠ A126), E249 (≠ A238)
- binding coenzyme a persulfide: S137 (≠ Y132), S185 (≠ G180), R186 (vs. gap), V239 (≠ L228), Y240 (≠ A229), M243 (≠ E232), E249 (≠ A238), R250 (≠ I239)
- binding flavin-adenine dinucleotide: L128 (≠ F123), M130 (≠ Y125), S131 (≠ A126), G136 (≠ R131), S137 (≠ Y132), W161 (≠ V156), T163 (≠ V158), R275 (= R264), F278 (= F267), F285 (= F274), M288 (≠ L277), Q343 (= Q333), C344 (≠ I334), G347 (= G337)
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)
25% identity, 93% coverage: 5:357/379 of query aligns to 45:404/426 of P26440
- 165:174 (vs. 123:132, 40% identical) binding
- S174 (≠ Y132) binding
- WIT 198:200 (≠ VVV 156:158) binding
- SR 222:223 (≠ G- 180) binding
- G250 (= G204) to A: in IVA; uncertain significance
- Y277 (≠ A229) binding
- DLER 284:287 (≠ DEAI 236:239) binding
- E286 (≠ A238) 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 (≠ G243) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R264) binding
- Q323 (= Q275) binding
- I379 (= I332) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QIHGG 333:337) binding
- R398 (≠ K351) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ I356) to N: in IVA; uncertain significance
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 407 A→E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- 407:408 binding
- 409:411 binding
6wy8C Tcur3481-tcur3483 steroid acad (see paper)
29% identity, 100% coverage: 1:379/379 of query aligns to 1:363/364 of 6wy8C
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
25% identity, 96% coverage: 5:368/379 of query aligns to 53:419/430 of P28330
- E291 (≠ A238) 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 (≠ L250) to T: in dbSNP:rs1801204
- K333 (≠ R280) to Q: in dbSNP:rs2286963
6wy9B Tcur3481-tcur3483 steroid acad g363a variant (see paper)
28% identity, 99% coverage: 4:379/379 of query aligns to 5:360/361 of 6wy9B
P51174 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Mus musculus (Mouse) (see paper)
24% identity, 96% coverage: 5:368/379 of query aligns to 53:419/430 of P51174
- K318 (= K265) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ T269) 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.
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
25% identity, 85% coverage: 51:372/379 of query aligns to 50:385/385 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 (= M338), T347 (≠ D342), E348 (= E343)
- binding flavin-adenine dinucleotide: F125 (= F123), L127 (≠ Y125), S128 (≠ A126), G133 (≠ R131), S134 (≠ Y132), W158 (≠ V156), T160 (≠ V158), R270 (= R264), F273 (= F267), L280 (≠ F274), V282 (= V276), Q338 (= Q333), I339 (= I334), G342 (= G337), I360 (≠ M355), Y364 (≠ L359), T367 (≠ S362), E369 (≠ D364), I370 (vs. gap), L373 (vs. gap)
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
25% identity, 85% coverage: 51:372/379 of query aligns to 77:412/412 of P16219
- G90 (= G64) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E78) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 123:132, 40% identical) binding in other chain
- R171 (≠ K142) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ VVV 156:158) binding in other chain
- A192 (= A163) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G180) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R264) binding
- Q308 (= Q275) binding in other chain
- R325 (≠ V292) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ G321) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QIHGG 333:337) binding
- R380 (≠ H348) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ SVD 362:364) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
26% identity, 93% coverage: 5:358/379 of query aligns to 3:363/379 of 6fahD
- active site: L124 (≠ Y125), T125 (≠ A126), G241 (≠ A238)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (≠ Y125), T125 (≠ A126), R152 (≠ H153), F155 (≠ V156), T157 (≠ V158), E198 (≠ R197), R267 (= R264), Q269 (= Q266), F270 (= F267), I274 (= I271), F277 (= F274), Q335 (= Q333), I336 (= I334), G339 (= G337), Y361 (≠ I356)
Sites not aligning to the query:
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
28% identity, 93% coverage: 1:351/379 of query aligns to 1:353/379 of 1ukwB
- active site: L124 (≠ Y125), S125 (≠ A126), T241 (≠ A238)
- binding cobalt (ii) ion: D145 (≠ S146), H146 (≠ G147)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (≠ Y125), S125 (≠ A126), G130 (≠ R131), S131 (≠ Y132), W155 (≠ V156), S157 (≠ V158), K200 (≠ V202)
Sites not aligning to the query:
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
28% identity, 93% coverage: 1:351/379 of query aligns to 1:353/379 of 1ukwA
Sites not aligning to the query:
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 81% coverage: 51:357/379 of query aligns to 53:365/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (= F123), L130 (≠ Y125), S131 (≠ A126), G136 (≠ R131), S137 (≠ Y132), W161 (≠ V156), T163 (≠ V158), T214 (≠ A207), R273 (= R264), F276 (= F267), L280 (≠ I271), L283 (≠ F274), V285 (= V276), Q341 (= Q333), I342 (= I334), G345 (= G337), I363 (≠ M355)
Sites not aligning to the query:
8sgsA Short-chain specific acyl-CoA dehydrogenase, mitochondrial (see paper)
26% identity, 81% coverage: 51:357/379 of query aligns to 47:359/381 of 8sgsA
- binding coenzyme a: S131 (≠ Y132), A133 (≠ W134), N177 (≠ D178), F231 (vs. gap), M235 (≠ E232), L238 (≠ M235), I312 (≠ A310)
- binding flavin-adenine dinucleotide: F122 (= F123), L124 (≠ Y125), S125 (≠ A126), G130 (≠ R131), S131 (≠ Y132), W155 (≠ V156), T157 (≠ V158), R267 (= R264), F270 (= F267), L274 (≠ I271), L277 (≠ F274), Q335 (= Q333), I336 (= I334), G338 (= G336), G339 (= G337), I357 (≠ M355)
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)
26% identity, 85% coverage: 50:372/379 of query aligns to 76:412/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
27% identity, 94% coverage: 1:357/379 of query aligns to 1:360/380 of 4l1fA
- active site: L125 (≠ Y125), T126 (≠ A126), G242 (≠ A238)
- binding coenzyme a persulfide: T132 (≠ Y132), H179 (≠ G180), F232 (≠ L228), M236 (≠ E232), E237 (≠ Q233), L239 (≠ M235), D240 (= D236), R243 (≠ I239)
- binding flavin-adenine dinucleotide: F123 (= F123), L125 (≠ Y125), T126 (≠ A126), G131 (≠ R131), T132 (≠ Y132), F156 (≠ V156), I157 (≠ V157), T158 (≠ V158), R268 (= R264), Q270 (= Q266), F271 (= F267), I275 (= I271), F278 (= F274), L281 (= L277), Q336 (= Q333), I337 (= I334), G340 (= G337), I358 (≠ M355)
- binding 1,3-propandiol: L5 (≠ F5), Q10 (≠ S10)
Sites not aligning to the query:
7w0jE Acyl-coa dehydrogenase, tfu_1647
25% identity, 94% coverage: 2:357/379 of query aligns to 1:363/382 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 (≠ A126), W157 (≠ V156), R270 (= R264), Q272 (= Q266), F273 (= F267), I277 (= I271), F280 (= F274), I283 (≠ L277), Q339 (= Q333), L340 (≠ I334), G343 (= G337)
Sites not aligning to the query:
- 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: 365, 366, 368, 370, 371
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
25% identity, 94% coverage: 3:357/379 of query aligns to 4:362/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (≠ Y132), T134 (≠ W134), R180 (≠ G180), R234 (≠ A229), L237 (≠ E232), R238 (≠ Q233), L240 (≠ M235), D241 (= D236), R244 (≠ I239)
- binding flavin-adenine dinucleotide: Y123 (≠ F123), L125 (≠ Y125), S126 (≠ A126), G131 (≠ R131), S132 (≠ Y132), W156 (≠ V156), I157 (≠ V157), T158 (≠ V158), I360 (≠ M355)
Sites not aligning to the query:
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
25% identity, 94% coverage: 3:357/379 of query aligns to 4:362/381 of 8i4pA
Sites not aligning to the query:
Query Sequence
>CCNA_01369 FitnessBrowser__Caulo:CCNA_01369
MDFNFTEEQSMVRDSVASFLQDKYDFDTRRKIVSSDAGWRADYWKAFAEELGILGASFSE
ELGGLGGGAIDNMIIMEEFGKALVIEPYLGTVVIGGGFMKHSGYAGAASVIEGIVGGSTT
IAFAYAEPQARYTWQDLKTTAKKDGSGWVLNGHKAVVVGAPFATHLIVTARTGGAQRDAG
GVGVFIIDKSLPGVVTRDYPTVDGNRASEVYFENVSIPAEALISESGLALVEQVMDEAIA
AVGAEAVGVLRKLHEGTLDYAKQRKQFGTAIANFQVLQHRMVDMFIEVEQSVSMTYMATI
KVGESAAERAKAVSAMKVRIGRACKFVGQSAIQIHGGMGMTDELAIGHYFKRATMIEGLF
GSVDHHLKRYESLSFDAAA
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