SitesBLAST
Comparing HSERO_RS04140 FitnessBrowser__HerbieS:HSERO_RS04140 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)
3ihbA Crystal structure analysis of mglu in its tris and glutamate form (see paper)
40% identity, 89% coverage: 21:291/305 of query aligns to 22:294/450 of 3ihbA
- active site: S64 (= S63), K67 (= K66), Y191 (= Y188), Y243 (= Y240), V261 (= V258)
- binding glutamic acid: Q63 (= Q62), S64 (= S63), N114 (= N113), E160 (= E157), N167 (≠ H164), G260 (= G257), V261 (= V258)
P77454 Glutaminase 1; EC 3.5.1.2 from Escherichia coli (strain K12) (see 2 papers)
37% identity, 93% coverage: 21:304/305 of query aligns to 24:308/310 of P77454
- K69 (= K66) mutation to A: Loss of activity.
- N117 (= N113) mutation to A: Loss of activity.
- S160 (= S156) mutation to A: Loss of activity.
- E161 (= E157) mutation to A: Strongly reduced activity.
- Q162 (≠ L158) mutation to A: No effect.
- N168 (≠ H164) mutation to A: Loss of activity.
- Y192 (= Y188) mutation to A: Loss of activity.
- Y244 (= Y240) mutation to A: Loss of activity.
- S260 (= S256) mutation to A: Reduced activity.
- K294 (= K290) modified: N6-acetyllysine
5w2jB Crystal structure of dimeric form of mouse glutaminasE C (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 102:380/411 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)
35% identity, 90% coverage: 14:289/305 of query aligns to 242:520/674 of D3Z7P3
- Y254 (= Y26) mutation to F: Increased enzyme activity in the absence of phosphate. No effect on stimulation of enzyme activity by phosphate.
- S291 (= S63) binding
- K316 (≠ Q87) mutation to Q: Forms dimers with full, phosphate-independent activity; when associated with A-325 and K-391.
- G320 (≠ T91) mutation to P: Loss of enzyme activity.
- 320:327 (vs. 91:98, 38% identical) Highly mobile activation loop
- K325 (≠ S96) 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 (= N113) binding
- E386 (= E157) binding
- D391 (≠ S162) 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 (≠ H164) binding
- F394 (≠ H165) mutation to S: Impairs tetramerization and promotes formation of homodimers. Impairs activation by phosphate.
- Y419 (= Y188) binding
- Y471 (= Y240) binding
- V489 (= V258) binding
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)
35% identity, 90% coverage: 14:289/305 of query aligns to 242:520/674 of P13264
Sites not aligning to the query:
6loxA Crystal structure of human glutaminase with macrocyclic inhibitor (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 99:377/407 of 6loxA
- active site: S148 (= S63), K151 (= K66), Y276 (= Y188), Y328 (= Y240), V346 (= V258)
- 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 (≠ S96), L183 (= L97), F184 (≠ I98), L185 (≠ E99), N186 (≠ L100), Y256 (≠ L170)
6umdB Crystal structure of human gac in complex with inhibitor upgl00012
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/409 of 6umdB
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- 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 (≠ P93), K184 (≠ S96), L185 (= L97), F186 (≠ I98), L187 (≠ E99), N188 (≠ L100), E189 (= E101), Y258 (≠ L170)
6ul9B Crystal structure of human gac in complex with inhibitor upgl00023
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/409 of 6ul9B
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- 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 (≠ P93), K184 (≠ S96), L185 (= L97), F186 (≠ I98), L187 (≠ E99), N188 (≠ L100), E189 (= E101), Y258 (≠ L170)
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)
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/410 of 5fi7A
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- 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 (≠ S96), L185 (= L97), F186 (≠ I98), L187 (≠ E99), E189 (= E101), Y258 (≠ L170)
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)
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/410 of 5fi6A
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- 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 (≠ P93), F182 (= F94), K184 (≠ S96), L185 (= L97), F186 (≠ I98), L187 (≠ E99), N188 (≠ L100), E189 (= E101), Y258 (≠ L170)
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)
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/410 of 5fi2A
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- 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 (≠ S96), L185 (= L97), F186 (≠ I98), L187 (≠ E99), Y258 (≠ L170)
4o7dA Crystal structure of human glutaminase in complex don (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 19:297/313 of 4o7dA
- active site: S68 (= S63), K71 (= K66), Y196 (= Y188), Y248 (= Y240), V266 (= V258)
- binding 5-oxo-l-norleucine: Y31 (= Y26), Q67 (= Q62), S68 (= S63), N117 (= N113), E163 (= E157), Y196 (= Y188), Y248 (= Y240), G265 (= G257), V266 (= V258)
O94925 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Homo sapiens (Human) (see 5 papers)
35% identity, 90% coverage: 14:289/305 of query aligns to 237:515/669 of O94925
- Y249 (= Y26) mutation to A: Loss of enzyme activity.
- S286 (= S63) binding ; mutation to A: Loss of enzyme activity.
- K289 (= K66) mutation to A: Loss of enzyme activity.
- P313 (= P89) to L: in GDPAG; loss of enzyme activity; dbSNP:rs1558973667
- F318 (= F94) mutation to Y: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with S-322.
- L321 (= L97) mutation to A: Decreased enzyme activity.
- F322 (≠ I98) mutation to S: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with Y-318.
- L323 (≠ E99) mutation to A: Decreased enzyme activity.
- N335 (= N113) binding
- E381 (= E157) binding
- N388 (≠ H164) binding
- Y394 (≠ L170) mutation to A: Decreased enzyme activity.; mutation to L: No effect on catalytic activity. Loss of inhibition by BPTES.
- Y414 (= Y188) binding
- Y466 (= Y240) binding ; mutation to A: Loss of enzyme activity.
- S482 (= S256) to C: in CASGID; increased enzyme activity; dbSNP:rs1558986214
- V484 (= V258) binding
5uqeD Multidomain structure of human kidney-type glutaminase(kga/gls) (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/507 of 5uqeD
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- binding N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide): K184 (≠ S96), L185 (= L97), D191 (≠ E103), Y258 (≠ L170)
8bsnA Human gls in complex with compound 27 (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 16:294/311 of 8bsnA
8jubA Crystal structure of glutaminasE C in complex with compound 27 (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 93:371/401 of 8jubA
8gwrB Near full length kidney type glutaminase in complex with 2,2-dimethyl- 2,3-dihydrobenzo[a] phenanthridin-4(1h)-one (ddp) (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 94:372/501 of 8gwrB
Sites not aligning to the query:
8jueA Crystal structure of glutaminasE C in complex with compound 11 (see paper)
35% identity, 90% coverage: 14:289/305 of query aligns to 94:372/401 of 8jueA
6umcB Crystal structure of human gac in complex with inhibitor upgl00012
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/410 of 6umcB
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- 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 (≠ S96), L185 (= L97), F186 (≠ I98), L187 (≠ E99), E189 (= E101), Y258 (≠ L170)
6ujgA Crystal structure of human gac in complex with inhibitor upgl00012
35% identity, 90% coverage: 14:289/305 of query aligns to 101:379/410 of 6ujgA
- active site: S150 (= S63), K153 (= K66), Y278 (= Y188), Y330 (= Y240), V348 (= V258)
- 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 (≠ S96), L185 (= L97), F186 (≠ I98), L187 (≠ E99), Y258 (≠ L170)
Query Sequence
>HSERO_RS04140 FitnessBrowser__HerbieS:HSERO_RS04140
LPWKQILERAAQLSAACRHEGKVADYIPALACVAPDQFGMAVATIDGGVHCVGDGETRFS
IQSISKVFLLTMAYGSYGEDLWKRVGQHPSTNPFNSLIELELERGVPRNPFLNPGALAVA
DALLSRHTHLESAMVSLMRELSGSADLNYDSEVFNSELRSSSRHHAAAYLMQSHGNFSNE
VGEVVRAYCASCAIEASCVELARAGLFLANGGRDIASGRQLLSAREAQRVCALMLTTGTY
EYSGMTAFAIGLPTKSGVGGGVLAVIPGRGCICAWSPRLDPRGNSVRAMKALELVSNTAG
LSVFA
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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