SitesBLAST
Comparing GFF2618 FitnessBrowser__psRCH2:GFF2618 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
7p9aA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1,5-diene-1-carboxyl-coa (see paper)
33% identity, 98% coverage: 6:384/387 of query aligns to 5:380/380 of 7p9aA
- binding 1,5 Dienoyl-CoA: S131 (≠ T131), L133 (≠ T133), K178 (≠ E182), F231 (= F235), M235 (≠ L239), L238 (= L242), N241 (≠ E245), R242 (= R246), Y362 (≠ A365), T363 (≠ I367), G364 (≠ S368), R375 (≠ H379)
- binding flavin-adenine dinucleotide: L122 (≠ M122), A124 (≠ V124), T125 (= T125), G130 (= G130), S131 (≠ T131), F155 (≠ W155), I156 (= I156), T157 (≠ S157), K200 (≠ I204), N208 (≠ T212), L358 (= L361), T365 (= T369), Q367 (≠ L371), I368 (= I372)
Q39QF5 Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase; CHeneCoA dehydrogenase; EC 1.3.8.10 from Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15) (see paper)
33% identity, 98% coverage: 6:384/387 of query aligns to 5:380/380 of Q39QF5
- D91 (≠ Y91) mutation to E: Retains minor activity.; mutation to N: Loss of activity. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with D-241.
- L122 (≠ M122) binding FAD
- A124 (≠ V124) binding FAD
- T125 (= T125) binding FAD
- S131 (≠ T131) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; binding FAD
- T157 (≠ S157) binding FAD
- K178 (≠ E182) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- N241 (≠ E245) mutation to D: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation. Gains a low but significant C1,C2-dehydrogenation activity, but the C3,C6- and C3,C4-dehydrogenating activities are largely diminished; when associated with N-91.
- R242 (= R246) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
- T363 (≠ I367) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA; mutation to V: Shows decreased activity, with a shift towards C3,C4- versus C3,C6-dehydrogenation.
- T365 (= T369) binding FAD
- Q367 (≠ L371) binding FAD
- R375 (≠ H379) binding cyclohex-1-ene-1-carbonyl-CoA; binding cyclohexa-1,5-diene-1-carbonyl-CoA
7p9xA Structure of cyclohex-1-ene-1-carboxyl-coa dehydrogenase complexed with cyclohex-1-ene-1-carboxyl-coa (see paper)
33% identity, 98% coverage: 6:384/387 of query aligns to 3:378/378 of 7p9xA
- binding 1-monoenoyl-CoA: L82 (≠ G84), D89 (≠ Y91), S129 (≠ T131), L131 (≠ T133), K176 (≠ E182), F229 (= F235), M233 (≠ L239), L236 (= L242), R240 (= R246), Y360 (≠ A365), T361 (≠ I367), G362 (≠ S368), R373 (≠ H379)
- binding flavin-adenine dinucleotide: A122 (≠ V124), T123 (= T125), G128 (= G130), S129 (≠ T131), F153 (≠ W155), I154 (= I156), T155 (≠ S157), N206 (≠ T212), L356 (= L361), Y360 (≠ A365), T363 (= T369), Q365 (≠ L371), I366 (= I372)
4iv6B X-ray crystal structure of an isovaleryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
34% identity, 91% coverage: 29:381/387 of query aligns to 26:376/383 of 4iv6B
- active site: L121 (≠ V124), T122 (= T125), G240 (≠ E245), E361 (≠ P366), K373 (≠ E378)
- binding dihydroflavine-adenine dinucleotide: L121 (≠ V124), T122 (= T125), G126 (≠ T129), G127 (= G130), S128 (≠ T131), W152 (= W155), I153 (= I156), S154 (= S157), R266 (= R271), S268 (≠ V273), F269 (= F274), I273 (= I278), H276 (≠ N281), V279 (= V284), R334 (≠ Q339), V335 (≠ T340), G338 (= G343), L356 (= L361), G360 (≠ A365), T363 (≠ S368), E365 (≠ N370), I366 (≠ L371)
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
33% identity, 86% coverage: 31:364/387 of query aligns to 30:360/378 of 5ol2F
- active site: L124 (≠ V124), T125 (= T125), G241 (≠ E245)
- binding calcium ion: E33 (= E34), R35 (≠ G36)
- binding coenzyme a persulfide: L238 (= L242), R242 (= R246)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), T125 (= T125), P127 (= P127), T131 (= T131), F155 (≠ W155), I156 (= I156), T157 (≠ S157), E198 (≠ Q202), R267 (= R271), F270 (= F274), L274 (≠ I278), F277 (≠ N281), Q335 (= Q339), L336 (≠ T340), G338 (= G342), G339 (= G343)
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)
33% identity, 91% coverage: 12:364/387 of query aligns to 4:351/369 of 3pfdC
- active site: L116 (≠ V124), S117 (≠ T125), T233 (≠ E245)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ M122), L116 (≠ V124), S117 (≠ T125), G122 (= G130), S123 (≠ T131), W147 (= W155), I148 (= I156), T149 (≠ S157), R259 (= R271), F262 (= F274), V266 (≠ I278), N269 (= N281), Q326 (= Q339), L327 (≠ T340), G330 (= G343), I348 (≠ L361)
Sites not aligning to the query:
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
34% identity, 88% coverage: 25:364/387 of query aligns to 25:356/374 of 5lnxD
- active site: L122 (≠ V124), T123 (= T125), G239 (≠ E245)
- binding flavin-adenine dinucleotide: L122 (≠ V124), T123 (= T125), G128 (= G130), S129 (≠ T131), F153 (≠ W155), T155 (≠ S157), R265 (= R271), Q267 (≠ V273), F268 (= F274), I272 (= I278), N275 (= N281), I278 (≠ V284), Q331 (= Q339), I332 (≠ T340), G335 (= G343)
Sites not aligning to the query:
1ukwB Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 97% coverage: 6:381/387 of query aligns to 6:377/379 of 1ukwB
- active site: L124 (≠ V124), S125 (≠ T125), T241 (≠ E245), E362 (≠ P366), R374 (≠ E378)
- binding cobalt (ii) ion: D145 (= D145), H146 (≠ K146)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), S125 (≠ T125), G130 (= G130), S131 (≠ T131), W155 (= W155), S157 (= S157), K200 (≠ I204), L357 (= L361), Y361 (≠ A365), E362 (≠ P366), T364 (≠ S368), E366 (≠ N370), L370 (≠ S374)
1ukwA Crystal structure of medium-chain acyl-coa dehydrogenase from thermus thermophilus hb8
30% identity, 97% coverage: 6:381/387 of query aligns to 6:377/379 of 1ukwA
- active site: L124 (≠ V124), S125 (≠ T125), T241 (≠ E245), E362 (≠ P366), R374 (≠ E378)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), S125 (≠ T125), G130 (= G130), S131 (≠ T131), W155 (= W155), S157 (= S157), L357 (= L361), Y361 (≠ A365), E362 (≠ P366), T364 (≠ S368), E366 (≠ N370), L370 (≠ S374)
2pg0A Crystal structure of acyl-coa dehydrogenase from geobacillus kaustophilus
30% identity, 97% coverage: 7:380/387 of query aligns to 7:378/380 of 2pg0A
- active site: M124 (≠ V124), T125 (= T125), E243 (= E245), A364 (≠ P366), R376 (≠ E378)
- binding flavin-adenine dinucleotide: I122 (≠ M122), M124 (≠ V124), T125 (= T125), G130 (= G130), S131 (≠ T131), F155 (≠ W155), I156 (= I156), T157 (≠ S157), R269 (= R271), F272 (= F274), F279 (≠ N281), Q337 (= Q339), L338 (≠ T340), G340 (= G342), G341 (= G343), V359 (≠ L361), I362 (≠ V364), Y363 (≠ A365), T366 (≠ S368), E368 (≠ N370), M369 (≠ L371)
C3UVB0 Glutaryl-CoA dehydrogenase; GDH(Des); EC 1.3.99.32 from Desulfococcus multivorans (see paper)
33% identity, 97% coverage: 1:377/387 of query aligns to 1:378/389 of C3UVB0
- A80 (≠ N77) mutation to E: Loses the FAD cofactor and dehydrogenase activity.
- R87 (≠ H87) binding substrate
- V88 (≠ G88) mutation to S: A residual dehydrogenase activity is observed.
- N91 (= N92) binding substrate
- FGIT 126:129 (≠ MGVT 122:125) binding FAD
- S135 (≠ T131) binding FAD; binding substrate
- WIS 159:161 (= WIS 155:157) binding FAD
- S181 (= S181) binding substrate
- R271 (= R271) binding FAD
- FQMN 281:284 (≠ NQGV 281:284) binding FAD
- R340 (≠ Q339) binding FAD
- A344 (≠ G343) binding FAD
- V366 (≠ A365) mutation to Y: Loses the FAD cofactor but a residual dehydrogenase activity is observed.
- EGSAN 367:371 (≠ PISTN 366:370) binding FAD
Sites not aligning to the query:
3mpjB Structure of the glutaryl-coenzyme a dehydrogenase (see paper)
33% identity, 97% coverage: 1:377/387 of query aligns to 1:378/393 of 3mpjB
- active site: I128 (≠ V124), T129 (= T125), T245 (≠ E245), E367 (≠ P366)
- binding flavin-adenine dinucleotide: F126 (≠ M122), I128 (≠ V124), T129 (= T125), G134 (= G130), S135 (≠ T131), W159 (= W155), I160 (= I156), S161 (= S157), V366 (≠ A365), S369 (= S368), N371 (= N370), M375 (≠ S374)
- binding : H36 (≠ G36), F37 (= F37), Y39 (vs. gap), A164 (≠ Q160), Q165 (≠ H161), D167 (= D163), N193 (≠ E193)
Sites not aligning to the query:
3mpiC Structure of the glutaryl-coenzyme a dehydrogenase glutaryl-coa complex (see paper)
33% identity, 97% coverage: 1:377/387 of query aligns to 1:378/395 of 3mpiC
- active site: I128 (≠ V124), T129 (= T125), T245 (≠ E245), E367 (≠ P366)
- binding flavin-adenine dinucleotide: I128 (≠ V124), T129 (= T125), G134 (= G130), S135 (≠ T131), W159 (= W155), I160 (= I156), S161 (= S157), M365 (≠ V364), V366 (≠ A365), S369 (= S368), N371 (= N370), M375 (≠ S374)
- binding glutaryl-coenzyme A: R87 (≠ H87), F126 (≠ M122), S135 (≠ T131), V137 (≠ T133), S181 (= S181), F239 (≠ L239), R246 (= R246), N315 (= N314), V366 (≠ A365), E367 (≠ P366), G368 (≠ I367), I376 (≠ Y375)
Sites not aligning to the query:
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
30% identity, 97% coverage: 6:382/387 of query aligns to 7:381/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (≠ T131), T134 (= T133), R180 (≠ E182), R234 (= R236), L237 (= L239), R238 (≠ D240), L240 (= L242), D241 (≠ N243), R244 (= R246), E365 (≠ P366), G366 (≠ I367), R377 (≠ E378)
- binding flavin-adenine dinucleotide: Y123 (≠ M122), L125 (≠ V124), S126 (≠ T125), G131 (= G130), S132 (≠ T131), W156 (= W155), I157 (= I156), T158 (≠ S157), I360 (≠ L361), T367 (≠ S368), Q369 (≠ N370)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
30% identity, 97% coverage: 6:382/387 of query aligns to 7:381/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ M122), L125 (≠ V124), S126 (≠ T125), G131 (= G130), S132 (≠ T131), W156 (= W155), I157 (= I156), T158 (≠ S157), I360 (≠ L361), Y364 (≠ A365), T367 (≠ S368), Q369 (≠ N370)
7w0jE Acyl-coa dehydrogenase, tfu_1647
31% identity, 97% coverage: 6:382/387 of query aligns to 8:382/382 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 (≠ T125), W157 (= W155), R270 (= R271), Q272 (≠ V273), F273 (= F274), I277 (= I278), F280 (≠ N281), I283 (≠ V284), Q339 (= Q339), L340 (≠ T340), G343 (= G343), Y365 (≠ A365), E366 (≠ P366), T368 (≠ S368), Q370 (≠ N370), I371 (≠ L371)
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)
29% identity, 97% coverage: 6:380/387 of query aligns to 58:428/432 of P45954
- V137 (≠ T85) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (vs. gap) 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 (≠ T131) binding substrate
- WIS 207:209 (= WIS 155:157) binding in other chain
- S210 (≠ R158) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ S181) binding substrate
- L255 (vs. gap) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ F235) binding substrate
- NEGR 291:294 (≠ NAER 243:246) binding substrate
- I316 (≠ A268) to V: in dbSNP:rs1131430
- R319 (= R271) binding FAD
- Q330 (= Q282) binding FAD
- EWMGG 387:391 (≠ QTHGG 339:343) binding FAD
- A416 (≠ S368) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ STN 368:370) binding in other chain
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
29% identity, 97% coverage: 6:380/387 of query aligns to 7:377/381 of 2jifA
- active site: L125 (≠ V124), S126 (≠ T125), G242 (≠ E245), E363 (≠ P366), K375 (≠ E378)
- binding coenzyme a persulfide: S132 (≠ T131), S134 (≠ T133), Y178 (≠ S181), Y232 (≠ F235), I236 (≠ L239), L239 (= L242), N240 (= N243), R243 (= R246), Y362 (≠ A365), E363 (≠ P366), G364 (≠ I367), I368 (≠ L371)
- binding flavin-adenine dinucleotide: F123 (≠ M122), L125 (≠ V124), S126 (≠ T125), G131 (= G130), S132 (≠ T131), W156 (= W155), I157 (= I156), S158 (= S157), K201 (≠ M207), T209 (= T212), R268 (= R271), F271 (= F274), L275 (≠ I278), F278 (≠ N281), L281 (≠ V284), E336 (≠ Q339), W337 (≠ T340), G340 (= G343), N367 (= N370), I368 (≠ L371)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
30% identity, 98% coverage: 1:381/387 of query aligns to 1:377/380 of 4l1fA
- active site: L125 (≠ V124), T126 (= T125), G242 (≠ E245), E363 (≠ P366), R375 (≠ H379)
- binding coenzyme a persulfide: T132 (= T131), H179 (≠ E182), F232 (= F235), M236 (≠ L239), E237 (≠ D240), L239 (= L242), D240 (≠ N243), R243 (= R246), Y362 (≠ A365), E363 (≠ P366), G364 (≠ S368), R375 (≠ H379)
- binding flavin-adenine dinucleotide: F123 (≠ M122), L125 (≠ V124), T126 (= T125), G131 (= G130), T132 (= T131), F156 (≠ W155), I157 (= I156), T158 (≠ S157), R268 (= R271), Q270 (≠ V273), F271 (= F274), I275 (= I278), F278 (≠ N281), L281 (≠ V284), Q336 (= Q339), I337 (≠ T340), G340 (= G343), I358 (≠ L361), Y362 (≠ A365), T365 (= T369), Q367 (≠ L371)
- binding 1,3-propandiol: L5 (≠ K5), Q10 (≠ N10)
6fahD Molecular basis of the flavin-based electron-bifurcating caffeyl-coa reductase reaction (see paper)
29% identity, 93% coverage: 6:364/387 of query aligns to 4:360/379 of 6fahD
- active site: L124 (≠ V124), T125 (= T125), G241 (≠ E245)
- binding flavin-adenine dinucleotide: F122 (≠ M122), L124 (≠ V124), T125 (= T125), R152 (≠ Q152), F155 (≠ W155), T157 (≠ S157), E198 (≠ V201), R267 (= R271), Q269 (≠ V273), F270 (= F274), I274 (= I278), F277 (≠ N281), Q335 (= Q339), I336 (≠ T340), G339 (= G343)
Sites not aligning to the query:
Query Sequence
>GFF2618 FitnessBrowser__psRCH2:GFF2618
MNPNKTEELNFIREGVRALCAEFPAEYWRRIDEEKGFPEAFVTAMTEAGWLSAMIPEEYG
GSGLGLAEASVILEEVNHCGGNSGTIHGQMYNMFTLLRNGSEEQKRYYLPKLASGELRLQ
SMGVTEPTTGTDTTKIKTTAVRQGDKYVINGQKVWISRIQHSDLMILLARTTPLGEVQRK
SEGMSIFLVDLREAIGNGLTVQPIANMVNHETNELFFDNLEIPASSLIGEEGKGFRYILD
GLNAERTLIAAECIGDGRWFVEKSAQYARDRVVFGRPIGQNQGVQFPIAEAHIEIEAADL
MRWRACEEYDSGRNAGAAANMAKYLAAKASWEAANACLQTHGGFGFANEYDVERKFRETR
LYQVAPISTNLILSYVAEHLLELPRSF
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