SitesBLAST

Comparing WP_009126907.1 NCBI__GCF_000195635.1:WP_009126907.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Found 20 (the maximum) hits to proteins with known functional sites

P77454 Glutaminase 1; EC 3.5.1.2 from Escherichia coli (strain K12) (see 2 papers)
45% identity, 97% coverage: 5:314/321 of query aligns to 2:310/310 of P77454

• K69 (= K72) mutation to A: Loss of activity.
• N117 (= N120) mutation to A: Loss of activity.
• S160 (= S164) mutation to A: Loss of activity.
• E161 (= E165) mutation to A: Strongly reduced activity.
• Q162 (≠ T166) mutation to A: No effect.
• N168 (= N172) mutation to A: Loss of activity.
• Y192 (= Y196) mutation to A: Loss of activity.
• Y244 (= Y248) mutation to A: Loss of activity.
• S260 (= S264) mutation to A: Reduced activity.
• K294 (≠ L298) modified: N6-acetyllysine

5w2jB Crystal structure of dimeric form of mouse glutaminasE C (see paper)
35% identity, 94% coverage: 16:317/321 of query aligns to 98:398/411 of 5w2jB

• active site: S151 (= S69), K154 (= K72), Y279 (= Y196), Y331 (= Y248), V349 (= V266)

Sites not aligning to the query:

• binding : 2, 4, 81, 83

D3Z7P3 Glutaminase kidney isoform, mitochondrial; GLS; EC 3.5.1.2 from Mus musculus (Mouse) (see 3 papers)
35% identity, 94% coverage: 16:317/321 of query aligns to 238:538/674 of D3Z7P3

• Y254 (= Y32) mutation to F: Increased enzyme activity in the absence of phosphate. No effect on stimulation of enzyme activity by phosphate.
• S291 (= S69) binding substrate
• K316 (≠ A94) mutation to Q: Forms dimers with full, phosphate-independent activity; when associated with A-325 and K-391.
• G320 (= G98) mutation to P: Loss of enzyme activity.
• 320:327 (vs. 98:105, 50% identical) Highly mobile activation loop
• K325 (≠ S103) 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 (= N120) binding substrate
• E386 (= E165) binding substrate
• D391 (≠ F170) 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 (= N172) binding substrate
• F394 (≠ R173) mutation to S: Impairs tetramerization and promotes formation of homodimers. Impairs activation by phosphate.
• Y419 (= Y196) binding substrate
• Y471 (= Y248) binding substrate
• V489 (= V266) 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)
35% identity, 94% coverage: 16:317/321 of query aligns to 238:538/674 of P13264

Sites not aligning to the query:

• 72:73 Cleavage; MPP

8gwrB Near full length kidney type glutaminase in complex with 2,2-dimethyl- 2,3-dihydrobenzo[a] phenanthridin-4(1h)-one (ddp) (see paper)
34% identity, 94% coverage: 16:317/321 of query aligns to 90:390/501 of 8gwrB

• binding 2,2-dimethyl-1,3-dihydrobenzo[a]phenanthridin-4-one: H332 (≠ T257), H376 (≠ M304)

5uqeD Multidomain structure of human kidney-type glutaminase(kga/gls) (see paper)
34% identity, 94% coverage: 16:317/321 of query aligns to 97:397/507 of 5uqeD

• active site: S150 (= S69), K153 (= K72), Y278 (= Y196), Y330 (= Y248), V348 (= V266)
• binding N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide): K184 (≠ S103), L185 (≠ I104), D191 (= D112), Y258 (≠ L178)

6umdB Crystal structure of human gac in complex with inhibitor upgl00012
34% identity, 94% coverage: 16:317/321 of query aligns to 97:397/409 of 6umdB

• active site: S150 (= S69), K153 (= K72), Y278 (= Y196), Y330 (= Y248), V348 (= V266)
• 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 (≠ P100), K184 (≠ S103), L185 (≠ I104), F186 (≠ I105), L187 (= L108), N188 (≠ L109), E189 (= E110), Y258 (≠ L178)

6ul9B Crystal structure of human gac in complex with inhibitor upgl00023
34% identity, 94% coverage: 16:317/321 of query aligns to 97:397/409 of 6ul9B

• active site: S150 (= S69), K153 (= K72), Y278 (= Y196), Y330 (= Y248), V348 (= V266)
• 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 (≠ P100), K184 (≠ S103), L185 (≠ I104), F186 (≠ I105), L187 (= L108), N188 (≠ L109), E189 (= E110), Y258 (≠ L178)

6loxA Crystal structure of human glutaminase with macrocyclic inhibitor (see paper)
34% identity, 94% coverage: 16:317/321 of query aligns to 95:395/407 of 6loxA

• active site: S148 (= S69), K151 (= K72), Y276 (= Y196), Y328 (= Y248), V346 (= V266)
• 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 (≠ S103), L183 (≠ I104), F184 (≠ I105), L185 (= L108), N186 (≠ L109), Y256 (≠ L178)

8jueA Crystal structure of glutaminasE C in complex with compound 11 (see paper)
34% identity, 94% coverage: 16:317/321 of query aligns to 90:390/401 of 8jueA

• binding 2-(3-phenoxyphenyl)-N-[5-[[(3R)-1-pyridazin-3-ylpyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2-yl]ethanamide: K177 (≠ S103), L178 (≠ I104), F179 (≠ I105), L180 (= L108), E182 (= E110), Y251 (≠ L178)

8jubA Crystal structure of glutaminasE C in complex with compound 27 (see paper)
34% identity, 94% coverage: 16:317/321 of query aligns to 89:389/401 of 8jubA

• binding 3-[2-oxidanylidene-2-[[5-[[(3R)-1-pyridazin-3-ylpyrrolidin-3-yl]amino]-1,3,4-thiadiazol-2-yl]amino]ethyl]benzoic acid: R173 (≠ P100), K176 (≠ S103), L177 (≠ I104), F178 (≠ I105), L179 (= L108), Y250 (≠ L178)

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)
34% identity, 94% coverage: 16:317/321 of query aligns to 97:397/410 of 5fi7A

• active site: S150 (= S69), K153 (= K72), Y278 (= Y196), Y330 (= Y248), V348 (= V266)
• 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 (≠ S103), L185 (≠ I104), F186 (≠ I105), L187 (= L108), E189 (= E110), Y258 (≠ L178)

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)
34% identity, 94% coverage: 16:317/321 of query aligns to 97:397/410 of 5fi6A

• active site: S150 (= S69), K153 (= K72), Y278 (= Y196), Y330 (= Y248), V348 (= V266)
• 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 (≠ P100), F182 (= F101), K184 (≠ S103), L185 (≠ I104), F186 (≠ I105), L187 (= L108), N188 (≠ L109), E189 (= E110), Y258 (≠ L178)

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)
34% identity, 94% coverage: 16:317/321 of query aligns to 97:397/410 of 5fi2A

• active site: S150 (= S69), K153 (= K72), Y278 (= Y196), Y330 (= Y248), V348 (= V266)
• 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 (≠ S103), L185 (≠ I104), F186 (≠ I105), L187 (= L108), Y258 (≠ L178)

O94925 Glutaminase kidney isoform, mitochondrial; GLS; K-glutaminase; L-glutamine amidohydrolase; EC 3.5.1.2 from Homo sapiens (Human) (see 5 papers)
34% identity, 94% coverage: 16:317/321 of query aligns to 233:533/669 of O94925