SitesBLAST
Comparing WP_079646508.1 NCBI__GCF_900167915.1:WP_079646508.1 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)
6cxtB Crystal structure of fad-dependent dehydrogenase (see paper)
30% identity, 92% coverage: 1:347/376 of query aligns to 1:346/372 of 6cxtB
- active site: I117 (≠ H125), S118 (≠ D126), E234 (≠ A234)
- binding flavin-adenine dinucleotide: N115 (≠ L123), I117 (≠ H125), S118 (≠ D126), G123 (≠ A131), S124 (≠ R132), Y148 (≠ A156), T150 (≠ I158), L201 (≠ V201)
- binding S-[2-({N-[(2R)-2-hydroxy-4-{[(R)-hydroxy(oxo)-lambda~5~-phosphanyl]oxy}-3,3-dimethylbutanoyl]-beta-alanyl}amino)ethyl] 1H-pyrrole-2-carbothioate: A81 (≠ F88), N115 (≠ L123), S124 (≠ R132), F227 (≠ L227), M231 (≠ F231), E234 (≠ A234), R235 (= R235)
Sites not aligning to the query:
6wy8C Tcur3481-tcur3483 steroid acad (see paper)
35% identity, 98% coverage: 1:369/376 of query aligns to 1:357/364 of 6wy8C
6wy9B Tcur3481-tcur3483 steroid acad g363a variant (see paper)
37% identity, 87% coverage: 44:369/376 of query aligns to 41:354/361 of 6wy9B
6cy8B Crystal structure of fad-dependent dehydrogenase (see paper)
30% identity, 92% coverage: 1:347/376 of query aligns to 1:344/370 of 6cy8B
- active site: I115 (≠ L123), S116 (≠ A124), E232 (≠ A234)
- binding flavin-adenine dinucleotide: N113 (≠ L121), I115 (≠ L123), S116 (≠ A124), G121 (= G129), S122 (≠ Q130), Y146 (≠ A156), T148 (≠ I158), L199 (≠ V201)
- binding 4'-phosphopantetheine: S122 (≠ Q130), F225 (≠ L227), A226 (≠ D228), R233 (= R235)
Sites not aligning to the query:
6af6A Piga with fad and proline (see paper)
27% identity, 90% coverage: 1:339/376 of query aligns to 1:348/383 of 6af6A
- active site: A127 (≠ H125), T128 (≠ D126), A244 (= A234)
- binding flavin-adenine dinucleotide: N125 (≠ L123), A127 (≠ H125), T128 (≠ D126), G133 (≠ A131), S134 (≠ R132), F158 (≠ A156), I159 (≠ V157), T160 (≠ I158), W211 (≠ V201)
- binding 1,4,7,10,13,16-hexaoxacyclooctadecane: L41 (≠ A43), K44 (≠ A46), K275 (≠ V265), F280 (= F270)
- binding proline: G133 (≠ A131), I136 (≠ T134), F237 (≠ L227), M241 (≠ F231)
Sites not aligning to the query:
4l1fA Electron transferring flavoprotein of acidaminococcus fermentans: towards a mechanism of flavin-based electron bifurcation (see paper)
28% identity, 90% coverage: 1:340/376 of query aligns to 1:347/380 of 4l1fA
- active site: L125 (≠ H125), T126 (≠ D126), G242 (≠ A234)
- binding coenzyme a persulfide: T132 (≠ R132), H179 (vs. gap), F232 (≠ A224), M236 (≠ D228), E237 (≠ R229), L239 (≠ F231), D240 (= D232), R243 (= R235)
- binding flavin-adenine dinucleotide: F123 (≠ L123), L125 (≠ H125), T126 (≠ D126), G131 (≠ A131), T132 (≠ R132), F156 (≠ A156), I157 (≠ V157), T158 (≠ I158), R268 (= R260), Q270 (= Q262), F271 (= F263), I275 (= I267), F278 (= F270), L281 (= L273), Q336 (= Q329), I337 (≠ M330), G340 (≠ A333)
- binding 1,3-propandiol: L5 (= L5), Q10 (≠ K10)
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)
26% identity, 91% coverage: 5:346/376 of query aligns to 53:402/430 of P51174
- K318 (≠ Q261) modified: N6-acetyllysine; mutation to R: Reduces activity by 37%; reduces activity by 80% when associated with R-322.
- K322 (≠ V265) 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.
8sgsA Human liver mitochondrial short-chain specific acyl-coa dehydrogenase (see paper)
26% identity, 93% coverage: 4:352/376 of query aligns to 3:360/381 of 8sgsA
- binding coenzyme a: S131 (≠ R132), A133 (≠ T134), N177 (≠ G173), F231 (≠ A224), M235 (≠ D228), L238 (≠ F231), I312 (≠ R306)
- binding flavin-adenine dinucleotide: F122 (≠ L123), L124 (≠ H125), S125 (≠ D126), G130 (≠ A131), S131 (≠ R132), W155 (≠ A156), T157 (≠ I158), R267 (= R260), F270 (= F263), L274 (≠ I267), L277 (≠ F270), Q335 (= Q329), I336 (≠ M330), G338 (= G332), G339 (≠ A333), I357 (≠ L349), I360 (= I352)
Sites not aligning to the query:
P16219 Short-chain specific acyl-CoA dehydrogenase, mitochondrial; SCAD; Butyryl-CoA dehydrogenase; EC 1.3.8.1 from Homo sapiens (Human) (see 3 papers)
26% identity, 93% coverage: 4:352/376 of query aligns to 33:390/412 of P16219
- G90 (= G63) to S: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908005
- E104 (≠ A77) natural variant: Missing (in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs387906308)
- 152:161 (vs. 123:132, 30% identical) binding in other chain
- R171 (= R142) to W: 69% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1800556
- WIT 185:187 (≠ AVI 156:158) binding in other chain
- A192 (= A163) to V: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940874
- G209 (= G175) to S: 86% of wild-type acyl-CoA dehydrogenase activity; confers susceptibility to ethylmalonicaciduria; dbSNP:rs1799958
- R297 (= R260) binding FAD
- Q308 (= Q271) binding in other chain
- R325 (= R288) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs121908006
- S353 (≠ G317) to L: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28941773
- QILGG 365:369 (≠ QMHGA 329:333) binding FAD
- R380 (≠ H344) to W: in ACADSD; loss of acyl-CoA dehydrogenase activity; dbSNP:rs28940875
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 394:396 binding in other chain
7y0aC Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 93% coverage: 4:352/376 of query aligns to 9:366/387 of 7y0aC
- binding flavin-adenine dinucleotide: F128 (≠ L123), L130 (≠ H125), S131 (≠ D126), G136 (≠ A131), S137 (≠ R132), W161 (≠ A156), T163 (≠ I158), T214 (≠ V201), R273 (= R260), F276 (= F263), L280 (≠ I267), L283 (≠ F270), V285 (≠ A272), Q341 (= Q329), I342 (≠ M330), G345 (≠ A333), I363 (≠ L349)
Sites not aligning to the query:
7y0bA Crystal structure of human short-chain acyl-coa dehydrogenase
26% identity, 93% coverage: 4:352/376 of query aligns to 6:363/385 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 (≠ I334), T347 (≠ A338), E348 (= E339)
- binding flavin-adenine dinucleotide: F125 (≠ L123), L127 (≠ H125), S128 (≠ D126), G133 (≠ A131), S134 (≠ R132), W158 (≠ A156), T160 (≠ I158), R270 (= R260), F273 (= F263), L280 (≠ F270), V282 (≠ A272), Q338 (= Q329), I339 (≠ M330), G342 (≠ A333), I360 (≠ L349)
Sites not aligning to the query:
8sgrA Human liver mitochondrial isovaleryl-coa dehydrogenase (see paper)
26% identity, 90% coverage: 5:343/376 of query aligns to 12:361/393 of 8sgrA
- binding flavin-adenine dinucleotide: S135 (≠ D126), G140 (≠ A131), S141 (≠ R132), W165 (≠ A156), T167 (≠ I158), R279 (= R260), F282 (= F263), I286 (= I267), F289 (= F270), Q347 (= Q329), C348 (≠ M330), G351 (≠ A333)
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)
26% identity, 90% coverage: 5:343/376 of query aligns to 45:394/426 of P26440
- 165:174 (vs. 123:132, 30% identical) binding FAD
- S174 (≠ R132) binding substrate
- WIT 198:200 (≠ AVI 156:158) binding FAD
- SR 222:223 (≠ GE 173:174) binding substrate
- G250 (= G198) to A: in IVA; uncertain significance
- Y277 (≠ A225) binding substrate
- DLER 284:287 (≠ DEAR 232:235) binding substrate
- E286 (≠ A234) 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 (≠ V239) to V: in IVA; uncertain significance; dbSNP:rs886042098
- R312 (= R260) binding FAD
- Q323 (= Q271) binding FAD
- I379 (≠ V328) to T: in IVA; uncertain significance
- QCFGG 380:384 (≠ QMHGA 329:333) binding FAD
Sites not aligning to the query:
- 1:32 modified: transit peptide, Mitochondrion
- 398 R → Q: in IVA; uncertain significance; dbSNP:rs1477527791
- 403 Y → N: in IVA; uncertain significance
- 407 A→E: Does not affect isovaleryl-CoA dehydrogenase activity; when associated with 286-D.
- 407:408 binding substrate
- 409:411 binding FAD
1ivhA Structure of human isovaleryl-coa dehydrogenase at 2.6 angstroms resolution: structural basis for substrate specificity (see paper)
26% identity, 90% coverage: 5:343/376 of query aligns to 8:357/387 of 1ivhA
- active site: M130 (≠ H125), S131 (≠ D126), E249 (≠ A234)
- binding coenzyme a persulfide: S137 (≠ R132), S185 (≠ G173), R186 (≠ E174), V239 (≠ A224), Y240 (≠ A225), M243 (≠ D228), E249 (≠ A234), R250 (= R235)
- binding flavin-adenine dinucleotide: L128 (= L123), M130 (≠ H125), S131 (≠ D126), G136 (≠ A131), S137 (≠ R132), W161 (≠ A156), T163 (≠ I158), R275 (= R260), F278 (= F263), F285 (= F270), M288 (≠ L273), Q343 (= Q329), C344 (≠ M330), G347 (≠ A333)
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)
25% identity, 91% coverage: 5:347/376 of query aligns to 57:405/432 of P45954
- V137 (≠ Y87) mutation to L: Decreased acyl-CoA dehydrogenase activity.
- F138 (= F88) mutation to L: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 174:183 (vs. 123:132, 30% identical) binding in other chain
- S183 (≠ R132) binding substrate
- WIS 207:209 (≠ AVI 156:158) binding in other chain
- S210 (≠ H159) mutation to N: Increased acyl-CoA dehydrogenase activity. Changed substrate specificity.
- Y229 (≠ L178) binding substrate
- L255 (≠ Y196) to F: in SBCADD; loss of protein expression; loss of 2-methylbutyryl-CoA dehydrogenase activity; dbSNP:rs137852649
- Y283 (≠ A224) binding substrate
- NEGR 291:294 (≠ DEAR 232:235) binding substrate
- I316 (≠ L257) to V: in dbSNP:rs1131430
- R319 (= R260) binding FAD
- Q330 (= Q271) binding FAD
- EWMGG 387:391 (≠ QMHGA 329:333) binding FAD
Sites not aligning to the query:
- 1:33 modified: transit peptide, Mitochondrion
- 13 R → K: in dbSNP:rs12263012
- 416 A→T: Increased acyl-CoA dehydrogenase activity. No effect on substrate specificity.
- 416:418 binding in other chain
2jifA Structure of human short-branched chain acyl-coa dehydrogenase (acadsb)
25% identity, 91% coverage: 5:347/376 of query aligns to 6:354/381 of 2jifA
- active site: L125 (≠ H125), S126 (≠ D126), G242 (≠ A234)
- binding coenzyme a persulfide: S132 (≠ R132), S134 (≠ T134), Y178 (≠ L178), Y232 (≠ A224), I236 (≠ D228), L239 (≠ F231), N240 (≠ D232), R243 (= R235)
- binding flavin-adenine dinucleotide: F123 (≠ L123), L125 (≠ H125), S126 (≠ D126), G131 (≠ A131), S132 (≠ R132), W156 (≠ A156), I157 (≠ V157), S158 (≠ I158), K201 (≠ T193), T209 (≠ V201), R268 (= R260), F271 (= F263), L275 (≠ I267), F278 (= F270), L281 (= L273), E336 (≠ Q329), W337 (≠ M330), G340 (≠ A333)
Sites not aligning to the query:
2vigB Crystal structure of human short-chain acyl coa dehydrogenase
27% identity, 81% coverage: 50:352/376 of query aligns to 44:350/371 of 2vigB
- active site: L121 (≠ H125), S122 (≠ D126), G231 (≠ A234)
- binding coenzyme a persulfide: S128 (≠ R132), F221 (≠ A224), M225 (≠ D228), Q226 (≠ R229), L228 (≠ F231), D229 (= D232), R232 (= R235)
- binding flavin-adenine dinucleotide: L121 (≠ H125), S122 (≠ D126), G127 (≠ A131), S128 (≠ R132), W152 (≠ A156), T154 (≠ I158), R257 (= R260), F260 (= F263), L264 (≠ I267), L267 (≠ F270), Q325 (= Q329), I326 (≠ M330), G329 (≠ A333), I347 (≠ L349)
Sites not aligning to the query:
1jqiA Crystal structure of rat short chain acyl-coa dehydrogenase complexed with acetoacetyl-coa (see paper)
25% identity, 93% coverage: 4:352/376 of query aligns to 6:363/384 of 1jqiA
- binding acetoacetyl-coenzyme a: L95 (≠ V92), F125 (≠ L123), S134 (≠ R132), F234 (≠ A224), M238 (≠ D228), Q239 (≠ R229), L241 (≠ F231), D242 (= D232), R245 (= R235)
- binding flavin-adenine dinucleotide: F125 (≠ L123), L127 (≠ H125), S128 (≠ D126), G133 (≠ A131), S134 (≠ R132), W158 (≠ A156), T160 (≠ I158), R270 (= R260), F273 (= F263), L280 (≠ F270), Q338 (= Q329), I339 (≠ M330), G342 (≠ A333), I360 (≠ L349)
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)
25% identity, 93% coverage: 4:352/376 of query aligns to 33:390/412 of P15651
- 152:161 (vs. 123:132, 30% identical) binding FAD
- S161 (≠ R132) binding substrate
- WIT 185:187 (≠ AVI 156:158) binding FAD
- DMGR 269:272 (≠ DEAR 232:235) binding substrate
- R297 (= R260) binding FAD
- QILGG 365:369 (≠ QMHGA 329:333) binding FAD
Sites not aligning to the query:
- 1:24 modified: transit peptide, Mitochondrion
- 392 active site, Proton acceptor
- 394:396 binding FAD
4ktoA Crystal structure of a putative isovaleryl-coa dehydrogenase (psi- nysgrc-012251) from sinorhizobium meliloti 1021
27% identity, 92% coverage: 1:347/376 of query aligns to 6:351/377 of 4ktoA
- active site: M130 (≠ H125), S131 (≠ D126), E239 (≠ A234)
- binding flavin-adenine dinucleotide: L128 (= L123), M130 (≠ H125), S131 (≠ D126), M155 (≠ I155), W156 (≠ A156), T158 (≠ I158), R265 (= R260), F268 (= F263), I272 (= I267), F275 (= F270), M278 (≠ L273), Q333 (= Q329), A334 (≠ M330), G337 (≠ A333)
Sites not aligning to the query:
Query Sequence
>WP_079646508.1 NCBI__GCF_900167915.1:WP_079646508.1
MDFELTDEQKMLSETVTRFVAETYDFSKREHALRSADGWSREAWAALAEMGLLGLPFAEE
DGGFGGSGVEMMLIMEALGRGLMVEPYFATVVLAGGVLRHGASAAQRAAIVPGVIAGERI
LALAHDEAGQARHTLAARTTARPAGDGWIIDGAKIAVIHGQSAGTLIVSATTGEGLGLFL
VDARADGVSIEATRGYDGVPVASVRLAGVAVGADALIGEAGTGAAILDRSFDEARAALVA
EAVGAMAETFDITVDYLKTRQQFGVAIGSFQALQHRAVDMLMQLELSRSMAVLAALSLDG
DADQRRRNIAAAKAQIGKSGRMVGQEAVQMHGAIGITAEYKVGHAFKRLTAIDALLGDRD
HHLARLVELGGVYPAE
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