SitesBLAST
Comparing WP_011317820.1 NCBI__GCF_000204075.1:WP_011317820.1 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)
5w2jB Crystal structure of dimeric form of mouse glutaminasE C (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 96:396/411 of 5w2jB
Sites not aligning to the query:
D3Z7P3 Glutaminase kidney isoform, mitochondrial; GLS; EC 3.5.1.2 from Mus musculus (Mouse) (see 3 papers)
43% identity, 90% coverage: 21:321/334 of query aligns to 236:539/674 of D3Z7P3
- Y254 (= Y39) mutation to F: Increased enzyme activity in the absence of phosphate. No effect on stimulation of enzyme activity by phosphate.
- S291 (= S76) binding substrate
- K316 (≠ V101) mutation to Q: Forms dimers with full, phosphate-independent activity; when associated with A-325 and K-391.
- G320 (= G105) mutation to P: Loss of enzyme activity.
- 320:327 (vs. 105:112, 38% identical) Highly mobile activation loop
- K325 (≠ S110) mutation to A: Constitutive enzyme activity that is fully active also in the absence phosphate. Forms oligomers with full, phosphate-independent activity; when associated with K-391. Forms dimers with full, phosphate-independent activity; when associated with Q-316 and K-391.
- N340 (= N126) binding substrate
- E386 (= E170) binding substrate
- D391 (≠ H175) mutation to K: Abolishes assembly of dimers into functional tetramers. Loss of enzyme activity. Forms oligomers with full, phosphate-independent activity; when associated with A-325. Forms dimers with full, phosphate-independent activity; when associated with Q-316 and A-325.
- N393 (= N177) binding substrate
- F394 (≠ R178) mutation to S: Impairs tetramerization and promotes formation of homodimers. Impairs activation by phosphate.
- Y419 (= Y201) binding substrate
- Y471 (= Y253) binding substrate
- V489 (= V271) binding substrate
Sites not aligning to the query:
- 202 K→E: Increased stimulation of enzyme activity by phosphate.
- 207 K→E: Increased stimulation of enzyme activity by phosphate.
P13264 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Rattus norvegicus (Rat) (see paper)
43% identity, 90% coverage: 21:321/334 of query aligns to 236:539/674 of P13264
Sites not aligning to the query:
6loxA Crystal structure of human glutaminase with macrocyclic inhibitor (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 93:393/407 of 6loxA
- active site: S148 (= S76), K151 (= K79), Y276 (= Y201), Y328 (= Y253), V346 (= V271)
- binding (E)-15,22-Dioxa-4,11-diaza-5(2,5)-thiadiazola-10(3,6)-pyridazina-1,14(1,3)-dibenzenacyclodocosaphan-18-ene-3,12-dione: K182 (≠ S110), L183 (≠ I111), F184 (≠ I112), L185 (= L113), N186 (≠ D114), Y256 (≠ L183)
4o7dA Crystal structure of human glutaminase in complex don (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 13:313/313 of 4o7dA
- active site: S68 (= S76), K71 (= K79), Y196 (= Y201), Y248 (= Y253), V266 (= V271)
- binding 5-oxo-l-norleucine: Y31 (= Y39), Q67 (= Q75), S68 (= S76), N117 (= N126), E163 (= E170), Y196 (= Y201), Y248 (= Y253), G265 (= G270), V266 (= V271)
O94925 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Homo sapiens (Human) (see 5 papers)
43% identity, 90% coverage: 21:321/334 of query aligns to 231:534/669 of O94925
- Y249 (= Y39) mutation to A: Loss of enzyme activity.
- S286 (= S76) binding substrate; mutation to A: Loss of enzyme activity.
- K289 (= K79) mutation to A: Loss of enzyme activity.
- P313 (= P103) to L: in GDPAG; loss of enzyme activity; dbSNP:rs1558973667
- F318 (= F108) mutation to Y: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with S-322.
- L321 (≠ I111) mutation to A: Decreased enzyme activity.
- F322 (≠ I112) mutation to S: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with Y-318.
- L323 (= L113) mutation to A: Decreased enzyme activity.
- N335 (= N126) binding substrate
- E381 (= E170) binding substrate
- N388 (= N177) binding substrate
- Y394 (≠ L183) mutation to A: Decreased enzyme activity.; mutation to L: No effect on catalytic activity. Loss of inhibition by BPTES.
- Y414 (= Y201) binding substrate
- Y466 (= Y253) binding substrate; mutation to A: Loss of enzyme activity.
- S482 (= S269) to C: in CASGID; increased enzyme activity; dbSNP:rs1558986214
- V484 (= V271) binding substrate
8jubA Crystal structure of glutaminasE C in complex with compound 27 (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 87:387/401 of 8jubA
8bsnA Human gls in complex with compound 27 (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 10:310/311 of 8bsnA
6umdB Crystal structure of human gac in complex with inhibitor upgl00012
44% identity, 89% coverage: 21:318/334 of query aligns to 95:395/409 of 6umdB
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-(pyridin-3-yl)-N-(5-{4-[(5-{[(pyridin-3-yl)acetyl]amino}-1,3,4-thiadiazol-2-yl)amino]piperidin-1-yl}-1,3,4-thiadiazol-2-yl)acetamide: R181 (≠ A107), K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), N188 (≠ D114), E189 (= E115), Y258 (≠ L183)
6ul9B Crystal structure of human gac in complex with inhibitor upgl00023
44% identity, 89% coverage: 21:318/334 of query aligns to 95:395/409 of 6ul9B
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-phenyl-N-{5-[(1-{5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}azetidin-3-yl)oxy]-1,3,4-thiadiazol-2-yl}acetamide: R181 (≠ A107), K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), N188 (≠ D114), E189 (= E115), Y258 (≠ L183)
5fi7A Crystal structure of human gac in complex with inhibitor upgl_00015: 2-phenyl-~{n}-[5-[(3~{s})-3-[[5-(2-phenylethanoylamino)-1,3,4- thiadiazol-2-yl]oxy]pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl]ethanamide (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 95:395/410 of 5fi7A
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-phenyl-~{N}-[5-[(3~{S})-3-[[5-(2-phenylethanoylamino)-1,3,4-thiadiazol-2-yl]oxy]pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl]ethanamide: K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), E189 (= E115), Y258 (≠ L183)
5fi6A Crystal structure of human gac in complex with inhibitor upgl_00011: 2-phenyl-~{n}-[5-[[(3~{s})-1-[5-(2-phenylethanoylamino)-1,3,4- thiadiazol-2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2- yl]ethanamide (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 95:395/410 of 5fi6A
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-phenyl-~{N}-[5-[[(3~{S})-1-[5-(2-phenylethanoylamino)-1,3,4-thiadiazol-2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2-yl]ethanamide: R181 (≠ A107), F182 (= F108), K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), N188 (≠ D114), E189 (= E115), Y258 (≠ L183)
5fi2A Crystal structure of human gac in complex with inhibitor upgl_00009: 2-phenyl-~{n}-[5-[[(3~{r})-1-[5-(2-phenylethanoylamino)-1,3,4- thiadiazol- 2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2- yl]ethanamide (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 95:395/410 of 5fi2A
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-phenyl-~{N}-[5-[[(3~{R})-1-[5-(2-phenylethanoylamino)-1,3,4-thiadiazol-2-yl]pyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2-yl]ethanamide: K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), Y258 (≠ L183)
8jueA Crystal structure of glutaminasE C in complex with compound 11 (see paper)
44% identity, 89% coverage: 21:318/334 of query aligns to 88:388/401 of 8jueA
5uqeD Multidomain structure of human kidney-type glutaminase(kga/gls) (see paper)
43% identity, 90% coverage: 21:321/334 of query aligns to 95:398/507 of 5uqeD
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide): K184 (≠ S110), L185 (≠ I111), D191 (≠ S117), Y258 (≠ L183)
8gwrB Near full length kidney type glutaminase in complex with 2,2-dimethyl- 2,3-dihydrobenzo[a] phenanthridin-4(1h)-one (ddp) (see paper)
43% identity, 90% coverage: 21:321/334 of query aligns to 88:391/501 of 8gwrB
6umcB Crystal structure of human gac in complex with inhibitor upgl00012
43% identity, 89% coverage: 21:318/334 of query aligns to 95:395/410 of 6umcB
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-phenyl-N-{5-[(3R)-3-({5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}oxy)pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide: K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), E189 (= E115), Y258 (≠ L183)
6ujgA Crystal structure of human gac in complex with inhibitor upgl00012
43% identity, 89% coverage: 21:318/334 of query aligns to 95:395/410 of 6ujgA
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding N-{5-[(3S)-3-{[5-(acetylamino)-1,3,4-thiadiazol-2-yl]amino}pyrrolidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide: K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), Y258 (≠ L183)
5wj6A Crystal structure of glutaminasE C in complex with inhibitor 2-phenyl- n-{5-[4-({5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}amino) piperidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide (upgl-00004) (see paper)
43% identity, 89% coverage: 21:318/334 of query aligns to 95:395/410 of 5wj6A
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-phenyl-N-{5-[4-({5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}amino)piperidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide: R181 (≠ A107), K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), L187 (= L113), N188 (≠ D114), E189 (= E115), Y258 (≠ L183)
5i94A Crystal structure of human glutaminasE C in complex with the inhibitor upgl-00019 (see paper)
43% identity, 89% coverage: 21:318/334 of query aligns to 95:395/410 of 5i94A
- active site: S150 (= S76), K153 (= K79), Y278 (= Y201), Y330 (= Y253), V348 (= V271)
- binding 2-phenyl-N-{5-[4-({5-[(phenylacetyl)amino]-1,3,4-thiadiazol-2-yl}oxy)piperidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide: R181 (≠ A107), K184 (≠ S110), L185 (≠ I111), F186 (≠ I112), Y258 (≠ L183)
Query Sequence
>WP_011317820.1 NCBI__GCF_000204075.1:WP_011317820.1
MSDQANQGDLEIRPSPLLTVINDLHSKYKSLKEGIVANYIPELAKVNPDLFSISIVTVDG
QVYQVGDYQQLFTIQSISKVFAYGLALEDHGRDYVLTRVGVEPTGEAFNSIILDEQSKRP
YNPMVNAGAIATTSLIKGAGATERLNRVLEMFRRYIGHDVFVDISVFTSERSTGHRNRAM
AHLMLNFGMIDRNLEEALDLYFQQCAVMVNCHDLAVMAATLANRGVNPVTGEQAVNSRYI
KDILSVMYTCGMYNFAGEWAYKVGIPAKSGVCGGIMAVVPNQMGIAVFSPPLDIRGNSVR
GVKVCEELSQQLGLHLFECVKVENGKWGVGNCEC
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