SitesBLAST
Comparing WP_011445295.1 NCBI__GCF_000013325.1:WP_011445295.1 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)
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
65% identity, 98% coverage: 7:384/387 of query aligns to 6:375/377 of 4ktoA
- active site: M130 (= M131), S131 (= S132), E239 (= E248), A360 (= A369), R372 (= R381)
- binding flavin-adenine dinucleotide: L128 (= L129), M130 (= M131), S131 (= S132), M155 (≠ F161), W156 (= W162), T158 (= T164), R265 (= R274), F268 (= F277), I272 (= I281), F275 (= F284), M278 (= M287), Q333 (= Q342), A334 (= A343), G337 (= G346), L355 (= L364), G359 (= G368), T362 (= T371), E364 (= E373)
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
58% identity, 96% coverage: 10:381/387 of query aligns to 7:382/387 of 1ivhA
- active site: M130 (= M131), S131 (= S132), E249 (= E248), A370 (= A369), R382 (= R381)
- binding coenzyme a persulfide: S137 (= S138), S185 (= S184), R186 (= R185), V239 (= V238), Y240 (≠ G239), M243 (= M242), E249 (= E248), R250 (= R249), G369 (= G368), A370 (= A369), G371 (= G370), V375 (≠ I374)
- binding flavin-adenine dinucleotide: L128 (= L129), M130 (= M131), S131 (= S132), G136 (= G137), S137 (= S138), W161 (= W162), T163 (= T164), R275 (= R274), F278 (= F277), F285 (= F284), M288 (= M287), Q343 (= Q342), C344 (≠ A343), G347 (= G346), T372 (= T371), E374 (= E373)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
58% identity, 96% coverage: 10:381/387 of query aligns to 11:386/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (= S132), G140 (= G137), S141 (= S138), W165 (= W162), T167 (= T164), R279 (= R274), F282 (= F277), I286 (= I281), F289 (= F284), Q347 (= Q342), C348 (≠ A343), G351 (= G346), L369 (= L364), G375 (= G370), T376 (= T371), L382 (≠ M377)
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)
58% identity, 96% coverage: 10:381/387 of query aligns to 44:419/426 of P26440
- 165:174 (vs. 129:138, 80% identical) binding FAD
- S174 (= S138) binding substrate
- WIT 198:200 (= WIT 162:164) binding FAD
- SR 222:223 (= SR 184:185) binding substrate
- G250 (= G212) to A: in IVA; uncertain significance
- Y277 (≠ G239) binding substrate
- DLER 284:287 (≠ DYER 246:249) binding substrate
- E286 (= E248) 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 (= A253) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R274) binding FAD
- Q323 (= Q285) binding FAD
- I379 (≠ V341) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QALGG 342:346) binding FAD
- R398 (= R360) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ L365) to N: in IVA; uncertain significance
- A407 (= A369) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (= AG 369:370) binding substrate
- TSE 409:411 (≠ TNE 371:373) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
5ol2F The electron transferring flavoprotein/butyryl-coa dehydrogenase complex from clostridium difficile (see paper)
43% identity, 95% coverage: 17:384/387 of query aligns to 10:377/378 of 5ol2F
- active site: L124 (≠ M131), T125 (≠ S132), G241 (≠ E248), G374 (≠ R381)
- binding calcium ion: E29 (= E36), E33 (≠ N40), R35 (= R42)
- binding coenzyme a persulfide: L238 (= L245), R242 (= R249), E362 (≠ A369), G363 (= G370)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), T125 (≠ S132), P127 (≠ A134), T131 (≠ S138), F155 (≠ W162), I156 (= I163), T157 (= T164), E198 (≠ I205), R267 (= R274), F270 (= F277), L274 (≠ I281), F277 (= F284), Q335 (= Q342), L336 (≠ A343), G338 (= G345), G339 (= G346), Y361 (≠ G368), T364 (= T371), E366 (= E373)
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
42% identity, 97% coverage: 8:384/387 of query aligns to 2:378/380 of 4l1fA
- active site: L125 (≠ M131), T126 (≠ S132), G242 (≠ E248), E363 (≠ A369), R375 (= R381)
- binding coenzyme a persulfide: T132 (≠ S138), H179 (≠ R185), F232 (≠ V238), M236 (= M242), E237 (≠ S243), L239 (= L245), D240 (= D246), R243 (= R249), Y362 (≠ G368), E363 (≠ A369), G364 (= G370), R375 (= R381)
- binding flavin-adenine dinucleotide: F123 (≠ L129), L125 (≠ M131), T126 (≠ S132), G131 (= G137), T132 (≠ S138), F156 (≠ W162), I157 (= I163), T158 (= T164), R268 (= R274), Q270 (= Q276), F271 (= F277), I275 (= I281), F278 (= F284), L281 (≠ M287), Q336 (= Q342), I337 (≠ A343), G340 (= G346), I358 (≠ L364), Y362 (≠ G368), T365 (= T371), Q367 (≠ E373)
- binding 1,3-propandiol: L5 (= L11), Q10 (≠ L16)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
41% identity, 97% coverage: 12:385/387 of query aligns to 3:374/374 of 5lnxD
- active site: L122 (≠ M131), T123 (≠ S132), G239 (≠ E248), E358 (≠ A369), K370 (≠ R381)
- binding flavin-adenine dinucleotide: L122 (≠ M131), T123 (≠ S132), G128 (= G137), S129 (= S138), F153 (≠ W162), T155 (= T164), R265 (= R274), Q267 (= Q276), F268 (= F277), I272 (= I281), N275 (≠ F284), I278 (≠ M287), Q331 (= Q342), I332 (≠ A343), G335 (= G346), Y357 (≠ G368), T360 (= T371), E362 (= E373)
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)
38% identity, 96% coverage: 11:383/387 of query aligns to 57:428/432 of P45954
- V137 (≠ L91) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (≠ S92) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 129:138, 70% identical) binding in other chain
- S183 (= S138) binding substrate
- WIS 207:209 (≠ WIT 162:164) binding in other chain
- S210 (≠ N165) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ S184) binding substrate
- L255 (= L210) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ V238) binding substrate
- NEGR 291:294 (≠ DYER 246:249) binding substrate
- I316 (≠ V271) to V: in dbSNP:rs1131430
- R319 (= R274) binding FAD
- Q330 (= Q285) binding FAD
- EWMGG 387:391 (≠ QALGG 342:346) binding FAD
- A416 (≠ T371) mutation to T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- ASN 416:418 (≠ TNE 371:373) 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)
38% identity, 96% coverage: 11:383/387 of query aligns to 6:377/381 of 2jifA
- active site: L125 (≠ M131), S126 (= S132), G242 (≠ E248), E363 (≠ A369), K375 (≠ R381)
- binding coenzyme a persulfide: S132 (= S138), S134 (≠ V140), Y178 (≠ S184), Y232 (≠ V238), I236 (≠ M242), L239 (= L245), N240 (≠ D246), R243 (= R249), Y362 (≠ G368), E363 (≠ A369), G364 (= G370), I368 (= I374)
- binding flavin-adenine dinucleotide: F123 (≠ L129), L125 (≠ M131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), S158 (≠ T164), K201 (= K207), T209 (= T215), R268 (= R274), F271 (= F277), L275 (≠ I281), F278 (= F284), L281 (≠ M287), E336 (≠ Q342), W337 (≠ A343), G340 (= G346), N367 (≠ E373), I368 (= I374)
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
39% identity, 97% coverage: 11:384/387 of query aligns to 7:380/384 of 1jqiA
- active site: G377 (≠ R381)
- binding acetoacetyl-coenzyme a: L95 (= L99), F125 (≠ L129), S134 (= S138), F234 (≠ V238), M238 (= M242), Q239 (≠ S243), L241 (= L245), D242 (= D246), R245 (= R249), Y364 (≠ G368), E365 (≠ A369), G366 (= G370)
- binding flavin-adenine dinucleotide: F125 (≠ L129), L127 (≠ M131), S128 (= S132), G133 (= G137), S134 (= S138), W158 (= W162), T160 (= T164), R270 (= R274), F273 (= F277), L280 (≠ F284), Q338 (= Q342), I339 (≠ A343), G342 (= G346), I360 (≠ L364), T367 (= T371), E369 (= E373), I370 (= I374)
P15651 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Rattus norvegicus (Rat) (see 2 papers)
39% identity, 97% coverage: 11:384/387 of query aligns to 34:407/412 of P15651
- 152:161 (vs. 129:138, 60% identical) binding FAD
- S161 (= S138) binding substrate
- WIT 185:187 (= WIT 162:164) binding FAD
- DMGR 269:272 (≠ DYER 246:249) binding substrate
- R297 (= R274) binding FAD
- QILGG 365:369 (≠ QALGG 342:346) binding FAD
- E392 (≠ A369) active site, Proton acceptor
- TSE 394:396 (≠ TNE 371:373) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
39% identity, 97% coverage: 11:384/387 of query aligns to 34:407/412 of P16219
- G90 (= G67) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (= E81) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 129:138, 60% identical) binding in other chain
- R171 (≠ D148) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (= WIT 162:164) binding in other chain
- A192 (= A169) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G186) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R274) binding FAD
- Q308 (= Q285) binding in other chain
- R325 (= R302) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (= S330) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QALGG 342:346) binding FAD
- R380 (= R357) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
- TSE 394:396 (≠ TNE 371:373) binding in other chain
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
39% identity, 97% coverage: 11:384/387 of query aligns to 4:377/381 of 8sgsA
- binding coenzyme a: S131 (= S138), A133 (≠ V140), N177 (≠ S184), F231 (≠ V238), M235 (= M242), L238 (= L245), I312 (≠ R319), E362 (≠ A369), G363 (= G370)
- binding flavin-adenine dinucleotide: F122 (≠ L129), L124 (≠ M131), S125 (= S132), G130 (= G137), S131 (= S138), W155 (= W162), T157 (= T164), R267 (= R274), F270 (= F277), L274 (≠ I281), L277 (≠ F284), Q335 (= Q342), I336 (≠ A343), G338 (= G345), G339 (= G346), I357 (≠ L364), I360 (= I367), Y361 (≠ G368), T364 (= T371), E366 (= E373)
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
39% identity, 97% coverage: 11:384/387 of query aligns to 7:380/385 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 (≠ A347), T347 (≠ K351), E348 (≠ D352)
- binding flavin-adenine dinucleotide: F125 (≠ L129), L127 (≠ M131), S128 (= S132), G133 (= G137), S134 (= S138), W158 (= W162), T160 (= T164), R270 (= R274), F273 (= F277), L280 (≠ F284), V282 (≠ L286), Q338 (= Q342), I339 (≠ A343), G342 (= G346), I360 (≠ L364), Y364 (≠ G368), T367 (= T371), E369 (= E373), I370 (= I374), L373 (≠ M377)
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
39% identity, 97% coverage: 11:384/387 of query aligns to 10:383/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L129), L130 (≠ M131), S131 (= S132), G136 (= G137), S137 (= S138), W161 (= W162), T163 (= T164), T214 (= T215), R273 (= R274), F276 (= F277), L280 (≠ I281), L283 (≠ F284), V285 (≠ L286), Q341 (= Q342), I342 (≠ A343), G345 (= G346), I363 (≠ L364), Y367 (≠ G368), T370 (= T371), E372 (= E373), L376 (≠ M377)
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)
41% identity, 95% coverage: 16:384/387 of query aligns to 2:368/369 of 3pfdC
- active site: L116 (≠ M131), S117 (= S132), T233 (≠ E248), E353 (≠ A369), R365 (= R381)
- binding dihydroflavine-adenine dinucleotide: Y114 (≠ L129), L116 (≠ M131), S117 (= S132), G122 (= G137), S123 (= S138), W147 (= W162), I148 (= I163), T149 (= T164), R259 (= R274), F262 (= F277), V266 (≠ I281), N269 (≠ F284), Q326 (= Q342), L327 (≠ A343), G330 (= G346), I348 (≠ L364), Y352 (≠ G368), T355 (= T371), Q357 (≠ E373)
7w0jE Acyl-coa dehydrogenase, tfu_1647
42% identity, 98% coverage: 6:384/387 of query aligns to 1:381/382 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 (= S132), W157 (= W162), R270 (= R274), Q272 (= Q276), F273 (= F277), I277 (= I281), F280 (= F284), I283 (≠ M287), Q339 (= Q342), L340 (≠ A343), G343 (= G346), Y365 (≠ G368), E366 (≠ A369), T368 (= T371), Q370 (≠ E373), I371 (= I374)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
40% identity, 96% coverage: 12:383/387 of query aligns to 7:378/378 of 4n5fA
- active site: L126 (≠ M131), T127 (≠ S132), G243 (≠ E248), E364 (≠ A369), R376 (= R381)
- binding dihydroflavine-adenine dinucleotide: L126 (≠ M131), T127 (≠ S132), G132 (= G137), S133 (= S138), F157 (≠ W162), T159 (= T164), T210 (= T215), Y363 (≠ G368), T366 (= T371), E368 (= E373), M372 (= M377)
8i4rA Crystal structure of acyl-coa dehydrogenase complexed with acetyl-coa from thermobifida fusca
42% identity, 96% coverage: 12:384/387 of query aligns to 7:380/381 of 8i4rA
- binding acetyl coenzyme *a: S132 (= S138), T134 (≠ V140), R180 (vs. gap), R234 (≠ G239), L237 (≠ M242), R238 (≠ S243), L240 (= L245), D241 (= D246), R244 (= R249), E365 (≠ A369), G366 (= G370), R377 (= R381)
- binding flavin-adenine dinucleotide: Y123 (≠ L129), L125 (≠ M131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), T158 (= T164), I360 (≠ L364), T367 (= T371), Q369 (≠ E373)
8i4pA Crystal structure of acyl-coa dehydrogenase from thermobifida fusca
42% identity, 96% coverage: 12:384/387 of query aligns to 7:380/381 of 8i4pA
- binding flavin-adenine dinucleotide: Y123 (≠ L129), L125 (≠ M131), S126 (= S132), G131 (= G137), S132 (= S138), W156 (= W162), I157 (= I163), T158 (= T164), I360 (≠ L364), Y364 (≠ G368), T367 (= T371), Q369 (≠ E373)
Query Sequence
>WP_011445295.1 NCBI__GCF_000013325.1:WP_011445295.1
MRATPDFDFGLTESALMIREAAGRFADEQIAPLAAEIDRNDRFPRELWEPMGALGLHGIT
VEEEFGGLGLGYLDHVIAVEEVSRASGSVGLSYGAHSNLCVNQIRRWGNDEQKAKYLPKL
ISGEHVGSLAMSEAGAGSDVVSMKLRADAVAGGFRLNGTKFWITNGTYADTLVVYAKTSP
EAGSRGISAFLIEKDMPGFSIGQKIDKMGLRGSPTCELVFDDCFVPEENVMGPLHGGVGV
LMSGLDYERVVLAGMQIGIMQACLDTVIPYVRERKQFGQPIGTFQLMQAKVADMYVAIQS
ARAYVYAVAKACDAGQTTRFDAAGAILLASENAFRVSGEAVQALGGAGYTKDWPVERYLR
DAKLLDIGAGTNEIRRMLIGRELIGAR
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