SitesBLAST
Comparing CCNA_02129 FitnessBrowser__Caulo:CCNA_02129 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)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
32% identity, 94% coverage: 4:358/377 of query aligns to 8:367/387 of 1ivhA
- active site: M130 (≠ I126), S131 (≠ D127), E249 (≠ A240)
- binding coenzyme a persulfide: S137 (≠ H132), S185 (≠ T179), R186 (≠ N180), V239 (≠ W230), Y240 (≠ A231), M243 (≠ E234), E249 (≠ A240), R250 (≠ Y241)
- binding flavin-adenine dinucleotide: L128 (= L124), M130 (≠ I126), S131 (≠ D127), G136 (≠ H131), S137 (≠ H132), W161 (≠ L156), T163 (≠ L158), R275 (= R266), F278 (= F269), F285 (= F276), M288 (≠ L279), Q343 (= Q334), C344 (≠ M335), G347 (= G338)
Sites not aligning to the query:
8sgrA Isovaleryl-CoA dehydrogenase, mitochondrial (see paper)
32% identity, 94% coverage: 4:358/377 of query aligns to 12:371/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ D127), G140 (≠ H131), S141 (≠ H132), W165 (≠ L156), T167 (≠ L158), R279 (= R266), F282 (= F269), I286 (= I273), F289 (= F276), Q347 (= Q334), C348 (≠ M335), G351 (= G338), L369 (≠ V356)
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, 94% coverage: 4:358/377 of query aligns to 45:404/426 of P26440
- 165:174 (vs. 124:132, 40% identical) binding
- S174 (≠ H132) binding
- WIT 198:200 (≠ LVL 156:158) binding
- SR 222:223 (≠ TN 179:180) binding
- G250 (= G206) to A: in IVA; uncertain significance
- Y277 (≠ A231) binding
- DLER 284:287 (≠ DRAY 238:241) binding
- E286 (≠ A240) 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 (= A245) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R266) binding
- Q323 (= Q277) binding
- I379 (≠ V333) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QMHGG 334:338) binding
- R398 (≠ K352) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ T357) 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
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
33% identity, 97% coverage: 4:368/377 of query aligns to 10:367/377 of 4ktoA
- active site: M130 (≠ I126), S131 (≠ D127), E239 (≠ A240), A360 (≠ F361)
- binding flavin-adenine dinucleotide: L128 (= L124), M130 (≠ I126), S131 (≠ D127), M155 (≠ T155), W156 (≠ L156), T158 (≠ L158), R265 (= R266), F268 (= F269), I272 (= I273), F275 (= F276), M278 (≠ L279), Q333 (= Q334), A334 (≠ M335), G337 (= G338), L355 (≠ V356), G359 (≠ L360), T362 (≠ G363), E364 (≠ S365)
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
31% identity, 97% coverage: 4:368/377 of query aligns to 5:370/380 of 4l1fA
- active site: L125 (≠ I126), T126 (≠ D127), G242 (≠ A240), E363 (≠ F361)
- binding coenzyme a persulfide: T132 (= T137), H179 (≠ N180), F232 (≠ W230), M236 (≠ E234), E237 (≠ P235), L239 (= L237), D240 (= D238), R243 (≠ Y241), Y362 (≠ L360), E363 (≠ F361), G364 (= G362)
- binding flavin-adenine dinucleotide: F123 (≠ L124), L125 (≠ I126), T126 (≠ D127), G131 (≠ R136), T132 (= T137), F156 (≠ L156), I157 (≠ V157), T158 (≠ L158), R268 (= R266), Q270 (= Q268), F271 (= F269), I275 (= I273), F278 (= F276), L281 (= L279), Q336 (= Q334), I337 (≠ M335), G340 (= G338), I358 (≠ V356), Y362 (≠ L360), T365 (≠ G363), Q367 (≠ S365)
- binding 1,3-propandiol: L5 (= L4), Q10 (≠ T9)
Sites not aligning to the query:
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
29% identity, 97% coverage: 1:365/377 of query aligns to 3:366/381 of 2jifA
- active site: L125 (≠ I126), S126 (≠ D127), G242 (≠ A240), E363 (≠ G362)
- binding coenzyme a persulfide: S132 (≠ H132), S134 (≠ P134), Y178 (≠ T179), Y232 (≠ W230), I236 (≠ E234), L239 (= L237), N240 (≠ D238), R243 (≠ Y241), Y362 (≠ F361), E363 (≠ G362), G364 (= G363)
- binding flavin-adenine dinucleotide: F123 (≠ L124), L125 (≠ I126), S126 (≠ D127), G131 (≠ H131), S132 (≠ H132), W156 (≠ L156), I157 (≠ V157), S158 (≠ L158), K201 (≠ R205), T209 (≠ A207), R268 (= R266), F271 (= F269), L275 (≠ I273), F278 (= F276), L281 (= L279), E336 (≠ Q334), W337 (≠ M335), G340 (= G338)
Sites not aligning to the query:
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)
28% identity, 99% coverage: 1:373/377 of query aligns to 54:426/432 of P45954
- V137 (≠ L88) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ L89) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 124:132, 30% identical) binding in other chain
- S183 (≠ H132) binding
- WIS 207:209 (≠ LVL 156:158) binding in other chain
- S210 (≠ D159) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ T179) binding
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ W230) binding
- NEGR 291:294 (≠ DRAY 238:241) binding
- I316 (≠ L263) to V: in dbSNP:rs1131430
- R319 (= R266) binding
- Q330 (= Q277) binding
- EWMGG 387:391 (≠ QMHGG 334:338) binding
- A416 (≠ G363) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ GAS 363:365) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
31% identity, 91% coverage: 4:346/377 of query aligns to 5:349/380 of 2pg0A
- active site: M124 (≠ I126), T125 (≠ D127), E243 (≠ A240)
- binding flavin-adenine dinucleotide: I122 (≠ L124), M124 (≠ I126), T125 (≠ D127), G130 (≠ H131), S131 (≠ H132), F155 (≠ L156), I156 (≠ V157), T157 (≠ L158), R269 (= R266), F272 (= F269), F279 (= F276), Q337 (= Q334), L338 (≠ M335), G340 (= G337), G341 (= G338)
Sites not aligning to the query:
6wy9B Tcur3481-tcur3483 steroid acad g363a variant (see paper)
34% identity, 99% coverage: 4:375/377 of query aligns to 2:355/361 of 6wy9B
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
30% identity, 99% coverage: 3:375/377 of query aligns to 5:378/378 of 4n5fA
- active site: L126 (≠ I126), T127 (≠ D127), G243 (≠ A240), E364 (≠ F361), R376 (= R373)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ I126), T127 (≠ D127), G132 (vs. gap), S133 (vs. gap), F157 (≠ L156), T159 (≠ L158), T210 (≠ A207), Y363 (≠ L360), T366 (≠ G363), E368 (≠ S365), M372 (≠ D369)
6wy8C Tcur3481-tcur3483 steroid acad (see paper)
34% identity, 99% coverage: 4:375/377 of query aligns to 5:358/364 of 6wy8C
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
28% identity, 94% coverage: 4:356/377 of query aligns to 3:357/379 of 6fahD
- active site: L124 (≠ I126), T125 (≠ D127), G241 (≠ A240)
- binding flavin-adenine dinucleotide: F122 (≠ L124), L124 (≠ I126), T125 (≠ D127), R152 (≠ T153), F155 (≠ L156), T157 (≠ L158), E198 (≠ S197), R267 (= R266), Q269 (= Q268), F270 (= F269), I274 (= I273), F277 (= F276), Q335 (= Q334), I336 (≠ M335), G339 (= G338)
Sites not aligning to the query:
P28330 Long-chain specific acyl-CoA dehydrogenase, mitochondrial; LCAD; EC 1.3.8.8 from Homo sapiens (Human) (see 2 papers)
28% identity, 85% coverage: 45:365/377 of query aligns to 90:415/430 of P28330
- E291 (≠ A240) 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 (≠ A252) to T: in dbSNP:rs1801204
- K333 (≠ R282) to Q: in dbSNP:rs2286963
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
28% identity, 97% coverage: 4:368/377 of query aligns to 34:399/412 of P15651
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
28% identity, 97% coverage: 4:368/377 of query aligns to 7:372/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (= L99), F125 (≠ L124), S134 (≠ A133), F234 (≠ W230), M238 (≠ E234), Q239 (≠ P235), L241 (= L237), D242 (= D238), R245 (≠ Y241), Y364 (≠ L360), E365 (≠ F361), G366 (= G362)
- binding flavin-adenine dinucleotide: F125 (≠ L124), L127 (≠ I126), S128 (≠ D127), G133 (≠ H132), S134 (≠ A133), W158 (≠ L156), T160 (≠ L158), R270 (= R266), F273 (= F269), L280 (≠ F276), Q338 (= Q334), I339 (≠ M335), G342 (= G338), I360 (≠ V356), T367 (≠ G363), E369 (≠ S365), I370 (≠ F366)
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, 98% coverage: 1:368/377 of query aligns to 1:370/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ H132), L133 (≠ P134), K178 (≠ N180), F231 (≠ W230), M235 (≠ E234), L238 (= L237), N241 (≠ A240), R242 (≠ Y241), Y362 (≠ L360), T363 (≠ F361), G364 (= G362)
- binding flavin-adenine dinucleotide: L122 (≠ T123), A124 (= A125), T125 (≠ I126), G130 (≠ H131), S131 (≠ H132), F155 (≠ L156), I156 (≠ V157), T157 (≠ L158), K200 (≠ L201), N208 (vs. gap), L358 (≠ V356), T365 (≠ G363), Q367 (≠ S365), I368 (≠ F366)
Sites not aligning to the query:
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
31% identity, 99% coverage: 4:377/377 of query aligns to 2:377/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (= L88), D89 (≠ A98), S129 (≠ H132), L131 (≠ P134), K176 (≠ N180), F229 (≠ W230), M233 (≠ E234), L236 (= L237), R240 (≠ Y241), Y360 (≠ L360), T361 (≠ F361), G362 (= G362), R373 (= R373)
- binding flavin-adenine dinucleotide: A122 (= A125), T123 (≠ I126), G128 (≠ H131), S129 (≠ H132), F153 (≠ L156), I154 (≠ V157), T155 (≠ L158), N206 (vs. gap), L356 (≠ V356), Y360 (≠ L360), T363 (≠ G363), Q365 (≠ S365), I366 (≠ F366)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
28% identity, 88% coverage: 36:368/377 of query aligns to 32:369/378 of 5ol2F
- active site: L124 (≠ I126), T125 (≠ D127), G241 (≠ A240)
- binding calcium ion: E33 (≠ K37), R35 (≠ T39)
- binding coenzyme a persulfide: L238 (= L237), R242 (≠ Y241), E362 (≠ F361), G363 (= G362)
- binding flavin-adenine dinucleotide: F122 (≠ L124), L124 (≠ I126), T125 (≠ D127), P127 (vs. gap), T131 (≠ H132), F155 (≠ L156), I156 (≠ V157), T157 (≠ L158), E198 (≠ R196), R267 (= R266), F270 (= F269), L274 (≠ I273), F277 (= F276), Q335 (= Q334), L336 (≠ M335), G338 (= G337), G339 (= G338), Y361 (≠ L360), T364 (≠ G363), E366 (≠ S365)
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)
28% identity, 85% coverage: 45:365/377 of query aligns to 90:415/430 of P51174
- K318 (≠ T267) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ Q271) 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.
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
29% identity, 97% coverage: 4:368/377 of query aligns to 10:375/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L124), L130 (≠ I126), S131 (≠ D127), G136 (≠ H132), S137 (≠ A133), W161 (≠ L156), T163 (≠ L158), T214 (≠ A207), R273 (= R266), F276 (= F269), L280 (≠ I273), L283 (≠ F276), V285 (≠ A278), Q341 (= Q334), I342 (≠ M335), G345 (= G338), I363 (≠ V356), Y367 (≠ L360), T370 (≠ G363), E372 (≠ S365)
Sites not aligning to the query:
Query Sequence
>CCNA_02129 FitnessBrowser__Caulo:CCNA_02129
MAVLTEEQTMLRDAAKGWASESAPVGALRKLRDSKSKQTFDPAAWAEMGQMGWAGVIVPE
AYDGSAFGYLGLGLILEETGRTLAASPLLSTAMIAASALQLGGSDAQKQAWLPKIATGEA
VATLAIDEGAHHAPARTALSATQSGAGYVLNGTKTLVLDGEAADLLIVAARTSGAPGDTN
GITLFLVAGDAAGVTRSHLSLIDSRGAAKIAFDGVEVGADAVLGEVDKGWAVLEPTLDRA
YAGLAAEMLGSASAAFDITLDYLKTRTQFGQVIGTFQALQHRAAKWFTDLETTRSCVEAA
LEALDAGADSRALAFLAKAKASELVHLASNEMVQMHGGIGMTDAHDAGLYMKRARVTEAL
FGGASFHRDRYARLMGF
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