SitesBLAST
Comparing WP_085984486.1 NCBI__GCF_000019365.1:WP_085984486.1 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)
3gqtC Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment (1,4-dimethyl-1,2,3,4- tetrahydroquinoxalin-6-yl)methylamine (see paper)
67% identity, 97% coverage: 14:401/402 of query aligns to 3:385/385 of 3gqtC
- active site: L135 (= L146), T136 (= T147), A250 (= A260), E365 (= E381), R377 (= R393)
- binding 1-(1,4-dimethyl-1,2,3,4-tetrahydroquinoxalin-6-yl)methanamine: W166 (= W177), K210 (= K220), L213 (= L223), T218 (= T228), Y364 (= Y380)
3gncA Crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei with fragment 6421 (see paper)
67% identity, 96% coverage: 14:400/402 of query aligns to 4:380/380 of 3gncA
2r0nA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
67% identity, 97% coverage: 14:401/402 of query aligns to 2:388/390 of 2r0nA
- active site: L133 (= L146), T134 (= T147), A247 (= A260), E368 (= E381), R380 (= R393)
- binding flavin-adenine dinucleotide: F131 (= F144), L133 (= L146), T134 (= T147), G139 (= G152), S140 (= S153), W166 (= W177), I167 (= I178), T168 (≠ S179), Y367 (= Y380), T370 (= T383), D372 (= D385)
- binding 3-thiaglutaryl-CoA: R92 (= R105), S93 (= S106), V97 (= V110), P142 (= P155), G238 (≠ K251), F241 (= F254), L244 (= L257), N245 (= N258), P318 (= P331), Y367 (= Y380), E368 (= E381), I377 (= I390)
1sirA The crystal structure and mechanism of human glutaryl-coa dehydrogenase (see paper)
67% identity, 97% coverage: 14:401/402 of query aligns to 2:388/390 of 1sirA
- active site: L133 (= L146), T134 (= T147), A247 (= A260), E368 (= E381), R380 (= R393)
- binding flavin-adenine dinucleotide: F131 (= F144), L133 (= L146), T134 (= T147), G139 (= G152), S140 (= S153), W166 (= W177), I167 (= I178), T168 (≠ S179), Y367 (= Y380), T370 (= T383)
- binding s-4-nitrobutyryl-coa: S93 (= S106), S140 (= S153), F241 (= F254), G242 (= G255), L244 (= L257), N245 (= N258), R248 (= R261), P318 (= P331), Y367 (= Y380), E368 (= E381), R380 (= R393)
3eonC 2.55a crystal structure of native glutaryl-coa dehydrogenase from burkholderia pseudomallei in complex with a small molecule (see paper)
67% identity, 96% coverage: 14:400/402 of query aligns to 3:382/382 of 3eonC
2r0mA The effect of a glu370asp mutation in glutaryl-coa dehydrogenase on proton transfer to the dienolate intermediate (see paper)
67% identity, 97% coverage: 14:401/402 of query aligns to 2:388/390 of 2r0mA
- active site: L133 (= L146), T134 (= T147), A247 (= A260), D368 (≠ E381), R380 (= R393)
- binding 4-nitrobutanoic acid: L101 (= L114), Y367 (= Y380), D368 (≠ E381)
- binding flavin-adenine dinucleotide: F131 (= F144), L133 (= L146), T134 (= T147), G139 (= G152), S140 (= S153), W166 (= W177), I167 (= I178), T168 (≠ S179), L210 (= L223), Y367 (= Y380), T370 (= T383)
3d6bC 2.2 a crystal structure of glutaryl-coa dehydrogenase from burkholderia pseudomallei (see paper)
65% identity, 96% coverage: 14:400/402 of query aligns to 3:377/377 of 3d6bC
3sf6A Crystal structure of glutaryl-coa dehydrogenase from mycobacterium smegmatis (see paper)
53% identity, 96% coverage: 17:401/402 of query aligns to 5:386/387 of 3sf6A
- active site: L134 (= L146), T135 (= T147), A245 (= A260), E366 (= E381), Q378 (≠ R393)
- binding dihydroflavine-adenine dinucleotide: F132 (= F144), L134 (= L146), T135 (= T147), G140 (= G152), S141 (= S153), W165 (= W177), I166 (= I178), T167 (≠ S179), S361 (≠ T376), T364 (= T379), Y365 (= Y380), T368 (= T383), E370 (≠ D385), M371 (≠ V386)
2ebaA Crystal structure of the putative glutaryl-coa dehydrogenase from thermus thermophilus
53% identity, 96% coverage: 18:401/402 of query aligns to 3:380/380 of 2ebaA
- active site: L131 (= L146), T132 (= T147), A239 (= A260), E360 (= E381), R372 (= R393)
- binding flavin-adenine dinucleotide: L131 (= L146), T132 (= T147), G136 (≠ A151), G137 (= G152), S138 (= S153), W161 (= W177), T163 (≠ S179), R265 (= R286), L272 (= L293), K275 (≠ T296), D333 (= D354), I334 (≠ M355), G337 (= G358), T355 (= T376), T358 (= T379), Y359 (= Y380), T362 (= T383)
3swoA Crystal structure of a glutaryl-coa dehydrogenase from mycobacterium smegmatis in complex with fadh2 (see paper)
49% identity, 94% coverage: 24:401/402 of query aligns to 13:387/388 of 3swoA
- active site: L135 (= L146), T136 (= T147), A246 (= A260), E367 (= E381), K379 (≠ R393)
- binding dihydroflavine-adenine dinucleotide: F133 (= F144), L135 (= L146), T136 (= T147), G141 (= G152), S142 (= S153), W166 (= W177), I167 (= I178), T168 (≠ S179), R272 (= R286), V274 (≠ Q288), F275 (= F289), L279 (= L293), Y282 (≠ T296), T340 (≠ D354), L341 (≠ M355), G344 (= G358), I347 (= I361), T365 (= T379), Y366 (= Y380), T369 (= T383), E371 (≠ D385), M372 (≠ V386)
2ix5A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 in complex with acetoacetyl-coa (see paper)
34% identity, 100% coverage: 1:401/402 of query aligns to 12:412/415 of 2ix5A
- active site: L158 (= L146), T159 (= T147), S271 (≠ A260), E392 (= E381), R404 (= R393)
- binding acetoacetyl-coenzyme a: S165 (= S153), A167 (≠ P155), S168 (≠ A156), F261 (≠ L250), L268 (= L257), R272 (= R261), E392 (= E381), G393 (= G382), R404 (= R393)
- binding flavin-adenine dinucleotide: L158 (= L146), T159 (= T147), G164 (= G152), S165 (= S153), W189 (= W177), N239 (≠ T228), R297 (= R286), F300 (= F289), L304 (= L293), F307 (≠ T296), L309 (= L298), N310 (≠ V299), E365 (≠ D354), L366 (≠ M355), G368 (= G357), G369 (= G358), Y391 (= Y380), T394 (= T383), D396 (= D385), I397 (≠ V386)
2ix6A Short chain specific acyl-coa oxidase from arabidopsis thaliana, acx4 (see paper)
34% identity, 100% coverage: 1:401/402 of query aligns to 12:412/416 of 2ix6A
- active site: L158 (= L146), T159 (= T147), S271 (≠ A260), E392 (= E381), R404 (= R393)
- binding flavin-adenine dinucleotide: T159 (= T147), G164 (= G152), S165 (= S153), W189 (= W177), N239 (≠ T228), R297 (= R286), F300 (= F289), L304 (= L293), F307 (≠ T296), N310 (≠ V299), E365 (≠ D354), L366 (≠ M355), G369 (= G358), I372 (= I361), Y391 (= Y380), T394 (= T383), D396 (= D385)
Q96329 Acyl-coenzyme A oxidase 4, peroxisomal; AOX 4; G6p; Short-chain acyl-CoA oxidase; AtCX4; AtG6; SAOX; EC 1.3.3.6 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 100% coverage: 1:401/402 of query aligns to 28:428/436 of Q96329
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
35% identity, 93% coverage: 22:394/402 of query aligns to 1:376/380 of 4l1fA
- active site: L125 (= L146), T126 (= T147), G242 (≠ A260), E363 (= E381), R375 (= R393)
- binding coenzyme a persulfide: T132 (≠ S153), H179 (≠ N198), F232 (≠ L250), M236 (≠ F254), E237 (≠ G255), L239 (= L257), D240 (≠ N258), R243 (= R261), Y362 (= Y380), E363 (= E381), G364 (= G382), R375 (= R393)
- binding flavin-adenine dinucleotide: F123 (= F144), L125 (= L146), T126 (= T147), G131 (= G152), T132 (≠ S153), F156 (≠ W177), I157 (= I178), T158 (≠ S179), R268 (= R286), Q270 (= Q288), F271 (= F289), I275 (≠ L293), F278 (≠ T296), L281 (≠ V299), Q336 (≠ D354), I337 (≠ M355), G340 (= G358), I358 (≠ T376), Y362 (= Y380), T365 (= T383), Q367 (≠ D385)
- binding 1,3-propandiol: L5 (= L26), Q10 (≠ R31)
5lnxD Crystal structure of mmgc, an acyl-coa dehydrogenase from bacillus subtilis.
34% identity, 91% coverage: 27:393/402 of query aligns to 3:370/374 of 5lnxD
- active site: L122 (= L146), T123 (= T147), G239 (≠ A260), E358 (= E381), K370 (≠ R393)
- binding flavin-adenine dinucleotide: L122 (= L146), T123 (= T147), G128 (= G152), S129 (= S153), F153 (≠ W177), T155 (≠ S179), R265 (= R286), Q267 (= Q288), F268 (= F289), I272 (≠ L293), N275 (≠ T296), I278 (≠ V299), Q331 (≠ D354), I332 (≠ M355), G335 (= G358), Y357 (= Y380), T360 (= T383), E362 (≠ D385)
4n5fA Crystal structure of a putative acyl-coa dehydrogenase with bound fadh2 from burkholderia cenocepacia j2315
35% identity, 93% coverage: 22:393/402 of query aligns to 2:376/378 of 4n5fA
- active site: L126 (= L146), T127 (= T147), G243 (≠ A260), E364 (= E381), R376 (= R393)
- binding dihydroflavine-adenine dinucleotide: L126 (= L146), T127 (= T147), G132 (= G152), S133 (= S153), F157 (≠ W177), T159 (≠ S179), T210 (= T228), Y363 (= Y380), T366 (= T383), E368 (≠ D385), M372 (≠ L389)
2dvlA Crystal structure of project tt0160 from thermus thermophilus hb8
36% identity, 92% coverage: 26:393/402 of query aligns to 1:366/370 of 2dvlA
- active site: L121 (= L146), T122 (= T147), G233 (≠ A260), E354 (= E381), R366 (= R393)
- binding flavin-adenine dinucleotide: L121 (= L146), T122 (= T147), G127 (= G152), S128 (= S153), W152 (= W177), I153 (= I178), T154 (≠ S179), T356 (= T383), E358 (≠ D385)
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
33% identity, 92% coverage: 26:394/402 of query aligns to 12:387/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ T147), G140 (= G152), S141 (= S153), W165 (= W177), T167 (≠ S179), R279 (= R286), F282 (= F289), I286 (≠ L293), F289 (≠ T296), Q347 (≠ D354), C348 (≠ M355), G351 (= G358), L369 (≠ T376), G375 (= G382), T376 (= T383), L382 (= L389)
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)
33% identity, 92% coverage: 26:394/402 of query aligns to 45:420/426 of P26440
- 165:174 (vs. 144:153, 50% identical) binding FAD
- S174 (= S153) binding substrate
- WIT 198:200 (≠ WIS 177:179) binding FAD
- SR 222:223 (≠ DN 197:198) binding substrate
- G250 (≠ A225) to A: in IVA; uncertain significance
- Y277 (≠ K251) binding substrate
- DLER 284:287 (≠ NRAR 258:261) binding substrate
- E286 (≠ A260) 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 (≠ S265) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R286) binding FAD
- Q323 (= Q297) binding FAD
- I379 (≠ R353) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ DMHGG 354:358) binding FAD
- R398 (≠ Q372) to Q: in IVA; uncertain significance; dbSNP:rs1477527791
- Y403 (≠ V377) to N: in IVA; uncertain significance
- A407 (≠ E381) mutation to E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- AG 407:408 (≠ EG 381:382) binding substrate
- TSE 409:411 (≠ THD 383:385) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
33% identity, 92% coverage: 26:394/402 of query aligns to 8:383/387 of 1ivhA
- active site: M130 (≠ L146), S131 (≠ T147), E249 (≠ A260), A370 (≠ E381), R382 (= R393)
- binding coenzyme a persulfide: S137 (= S153), S185 (≠ D197), R186 (≠ N198), V239 (≠ L250), Y240 (≠ K251), M243 (≠ F254), E249 (≠ A260), R250 (= R261), G369 (≠ Y380), A370 (≠ E381), G371 (= G382), V375 (= V386)
- binding flavin-adenine dinucleotide: L128 (≠ F144), M130 (≠ L146), S131 (≠ T147), G136 (= G152), S137 (= S153), W161 (= W177), T163 (≠ S179), R275 (= R286), F278 (= F289), F285 (≠ T296), M288 (≠ V299), Q343 (≠ D354), C344 (≠ M355), G347 (= G358), T372 (= T383), E374 (≠ D385)
Query Sequence
>WP_085984486.1 NCBI__GCF_000019365.1:WP_085984486.1
MSAAKPHEGSKGAFRWDDPFLLEDQLTDEERLIRDTARGFAQERLLPGIVEAYAEERTDR
SLFNAMGELGLLGVTLPEEYGCAGASYVAYGLVAREVERIDSGYRSMMSVQSSLVMYPIY
AYGDEAQRRTYLPKLATGEFVGCFGLTEPDAGSDPAGMRTRAEKIDGGYRLSGAKTWISN
APIADVFVVWAKSPAHDNQIRGFVLEKGMKGLSAPKIKGKLSLRASVTGEIVMDGVEVPE
SALLPHVSGLKGPFGCLNRARYGISWGALGAAEDCWHRARQYTLDRTQFGRPLAQTQLVQ
RKLADMQTEIALGLQASLRVGRLFDEGRVAPEMISIVKRNNCGKALEIARTARDMHGGNG
IMGEYHVMRHAQNLETVNTYEGTHDVHALILGRAQTGLQAFF
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