SitesBLAST
Comparing WP_047092224.1 NCBI__GCF_001013305.1:WP_047092224.1 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)
5uqeD Multidomain structure of human kidney-type glutaminase(kga/gls) (see paper)
43% identity, 94% coverage: 17:516/530 of query aligns to 4:507/507 of 5uqeD
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- binding N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide): K184 (≠ E194), L185 (= L195), D191 (≠ G201), Y258 (≠ F268)
D3Z7P3 Glutaminase kidney isoform, mitochondrial; GLS; EC 3.5.1.2 from Mus musculus (Mouse) (see 3 papers)
43% identity, 95% coverage: 17:517/530 of query aligns to 145:649/674 of D3Z7P3
- K202 (≠ E70) mutation to E: Increased stimulation of enzyme activity by phosphate.
- K207 (≠ S75) mutation to E: Increased stimulation of enzyme activity by phosphate.
- Y254 (= Y123) mutation to F: Increased enzyme activity in the absence of phosphate. No effect on stimulation of enzyme activity by phosphate.
- S291 (= S160) binding substrate
- K316 (≠ R185) mutation to Q: Forms dimers with full, phosphate-independent activity; when associated with A-325 and K-391.
- G320 (= G189) mutation to P: Loss of enzyme activity.
- 320:327 (vs. 189:196, 50% identical) Highly mobile activation loop
- K325 (≠ E194) 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 (= N209) binding substrate
- E386 (= E255) binding substrate
- D391 (= D260) 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 (= N262) binding substrate
- F394 (= F263) mutation to S: Impairs tetramerization and promotes formation of homodimers. Impairs activation by phosphate.
- Y419 (= Y288) binding substrate
- Y471 (= Y340) binding substrate
- V489 (= V358) binding substrate
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, 95% coverage: 17:517/530 of query aligns to 3:501/501 of 8gwrB
P13264 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Rattus norvegicus (Rat) (see paper)
43% identity, 95% coverage: 17:517/530 of query aligns to 145:649/674 of P13264
Sites not aligning to the query:
O94925 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Homo sapiens (Human) (see 5 papers)
42% identity, 97% coverage: 5:517/530 of query aligns to 121:644/669 of O94925
- Y249 (= Y123) mutation to A: Loss of enzyme activity.
- S286 (= S160) binding substrate; mutation to A: Loss of enzyme activity.
- K289 (= K163) mutation to A: Loss of enzyme activity.
- P313 (= P187) to L: in GDPAG; loss of enzyme activity; dbSNP:rs1558973667
- F318 (= F192) mutation to Y: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with S-322.
- L321 (= L195) mutation to A: Decreased enzyme activity.
- F322 (≠ T196) mutation to S: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with Y-318.
- L323 (= L197) mutation to A: Decreased enzyme activity.
- N335 (= N209) binding substrate
- E381 (= E255) binding substrate
- N388 (= N262) binding substrate
- Y394 (≠ F268) mutation to A: Decreased enzyme activity.; mutation to L: No effect on catalytic activity. Loss of inhibition by BPTES.
- Y414 (= Y288) binding substrate
- Y466 (= Y340) binding substrate; mutation to A: Loss of enzyme activity.
- S482 (= S356) to C: in CASGID; increased enzyme activity; dbSNP:rs1558986214
- V484 (= V358) binding substrate
8t0zA Human liver-type glutaminase (k253a) with l-gln, filamentous form (see paper)
46% identity, 72% coverage: 39:418/530 of query aligns to 27:409/409 of 8t0zA
8jubA Crystal structure of glutaminasE C in complex with compound 27 (see paper)
46% identity, 72% coverage: 36:418/530 of query aligns to 18:400/401 of 8jubA
6loxA Crystal structure of human glutaminase with macrocyclic inhibitor (see paper)
44% identity, 76% coverage: 17:418/530 of query aligns to 2:406/407 of 6loxA
- active site: S148 (= S160), K151 (= K163), Y276 (= Y288), Y328 (= Y340), V346 (= V358)
- 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 (≠ E194), L183 (= L195), F184 (≠ T196), L185 (= L197), N186 (= N198), Y256 (≠ F268)
6umdB Crystal structure of human gac in complex with inhibitor upgl00012
44% identity, 76% coverage: 17:418/530 of query aligns to 4:408/409 of 6umdB
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- 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 (≠ S191), K184 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), N188 (= N198), E189 (≠ P199), Y258 (≠ F268)
6ul9B Crystal structure of human gac in complex with inhibitor upgl00023
44% identity, 76% coverage: 17:418/530 of query aligns to 4:408/409 of 6ul9B
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- 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 (≠ S191), K184 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), N188 (= N198), E189 (≠ P199), Y258 (≠ F268)
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, 76% coverage: 17:418/530 of query aligns to 4:408/410 of 5fi7A
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- 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 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), E189 (≠ P199), Y258 (≠ F268)
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, 76% coverage: 17:418/530 of query aligns to 4:408/410 of 5fi6A
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- 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 (≠ S191), F182 (= F192), K184 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), N188 (= N198), E189 (≠ P199), Y258 (≠ F268)
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, 76% coverage: 17:418/530 of query aligns to 4:408/410 of 5fi2A
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- 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 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), Y258 (≠ F268)
5w2jB Crystal structure of dimeric form of mouse glutaminasE C (see paper)
44% identity, 76% coverage: 17:418/530 of query aligns to 5:409/411 of 5w2jB
Sites not aligning to the query:
8jueA Crystal structure of glutaminasE C in complex with compound 11 (see paper)
44% identity, 76% coverage: 17:418/530 of query aligns to 3:401/401 of 8jueA
6umfA Crystal structure of human gac in complex with inhibitor upgl00012
44% identity, 76% coverage: 17:418/530 of query aligns to 4:408/409 of 6umfA
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- binding N-(5-{[1-(5-amino-1,3,4-thiadiazol-2-yl)piperidin-4-yl]oxy}-1,3,4-thiadiazol-2-yl)-2-phenylacetamide: L185 (= L195), L187 (= L197), Y258 (≠ F268)
6umcB Crystal structure of human gac in complex with inhibitor upgl00012
44% identity, 76% coverage: 17:418/530 of query aligns to 4:408/410 of 6umcB
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- 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 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), E189 (≠ P199), Y258 (≠ F268)
6uljA Crystal structure of human gac in complex with inhibitor upgl00012
44% identity, 76% coverage: 17:418/530 of query aligns to 4:408/409 of 6uljA
6ulaA Crystal structure of human gac in complex with inhibitor upgl00012
44% identity, 76% coverage: 17:418/530 of query aligns to 4:408/409 of 6ulaA
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- binding 2-cyclopropyl-N-{5-[4-({5-[(cyclopropylacetyl)amino]-1,3,4-thiadiazol-2-yl}oxy)piperidin-1-yl]-1,3,4-thiadiazol-2-yl}acetamide: K184 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), N188 (= N198), Y258 (≠ F268)
6ukbA Crystal structure of human gac in complex with inhibitor upgl00012
44% identity, 76% coverage: 17:418/530 of query aligns to 4:408/409 of 6ukbA
- active site: S150 (= S160), K153 (= K163), Y278 (= Y288), Y330 (= Y340), V348 (= V358)
- binding N-[5-(4-{[5-(acetylamino)-1,3,4-thiadiazol-2-yl]oxy}piperidin-1-yl)-1,3,4-thiadiazol-2-yl]acetamide: K184 (≠ E194), L185 (= L195), F186 (≠ T196), L187 (= L197), Y258 (≠ F268)
Query Sequence
>WP_047092224.1 NCBI__GCF_001013305.1:WP_047092224.1
MVTLKSIAADSKGFAAKNLINSLKSEHTQAVSNAMLIRALEEMGLQRDDPRLSSLFEKLD
KMPGSGTLDEDGLRSLLGEVEASLVGRALSGSLIIPAFEEFRDQLNSIFETCRGESSGSV
ASYIPQLARVDPEKFAMAVCTIDGQRHSIGDDQDRFCVQSTCKPVNYAIAHGLSNADSIH
NHVGREPSGRSFNELTLNPAGLPHNPMINAGAIMASSLIKPRESLADRFDFVMSTWRDLG
GGVEPGFDNTVFLSEKATADRNFALAYFMRENGAFPPNTDLMETLDFYFQCCSISIDVRH
MATIAATLANGGVCPTTNQRVLDAEAVRNCLSLMYSCGMYDYSGEFAFTVGIPAKSGVSG
ALMLVIPGVCGIAIWSPRLDRCGNSVRGVRFAQELSKRYSFHSYATMVPGQELIDPTKSQ
AERVAEVASSLCSAASVGDLGELRRLVASGADILQADYDGRTALHLAASEGRVGVVRFLL
SIGADAEQKDRWGNTALADAEREGMGDAVQLLSNLKTAEPMKSRPRRKAA
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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