SitesBLAST
Comparing CCNA_00278 FitnessBrowser__Caulo:CCNA_00278 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)
P77454 Glutaminase 1; EC 3.5.1.2 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 87% coverage: 24:290/306 of query aligns to 24:292/310 of P77454
- K69 (= K69) mutation to A: Loss of activity.
- N117 (= N116) mutation to A: Loss of activity.
- S160 (= S158) mutation to A: Loss of activity.
- E161 (= E159) mutation to A: Strongly reduced activity.
- Q162 (≠ L160) mutation to A: No effect.
- N168 (= N166) mutation to A: Loss of activity.
- Y192 (= Y190) mutation to A: Loss of activity.
- Y244 (= Y242) mutation to A: Loss of activity.
- S260 (= S258) mutation to A: Reduced activity.
Sites not aligning to the query:
- 294 modified: N6-acetyllysine
3ihbA Crystal structure analysis of mglu in its tris and glutamate form (see paper)
38% identity, 96% coverage: 6:299/306 of query aligns to 5:300/450 of 3ihbA
- active site: S64 (= S66), K67 (= K69), Y191 (= Y190), Y243 (= Y242), V261 (= V260)
- binding glutamic acid: Q63 (= Q65), S64 (= S66), N114 (= N116), E160 (= E159), N167 (= N166), G260 (= G259), V261 (= V260)
5w2jB Crystal structure of dimeric form of mouse glutaminasE C (see paper)
38% identity, 91% coverage: 24:302/306 of query aligns to 109:391/411 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)
39% identity, 87% coverage: 24:290/306 of query aligns to 249:519/674 of D3Z7P3
- Y254 (= Y29) mutation to F: Increased enzyme activity in the absence of phosphate. No effect on stimulation of enzyme activity by phosphate.
- S291 (= S66) binding
- K316 (= K90) mutation to Q: Forms dimers with full, phosphate-independent activity; when associated with A-325 and K-391.
- G320 (= G94) mutation to P: Loss of enzyme activity.
- 320:327 (vs. 94:101, 50% identical) Highly mobile activation loop
- K325 (≠ H99) 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 (= N116) binding
- E386 (= E159) binding
- D391 (≠ W164) 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 (= N166) binding
- F394 (≠ R167) mutation to S: Impairs tetramerization and promotes formation of homodimers. Impairs activation by phosphate.
- Y419 (= Y190) binding
- Y471 (= Y242) binding
- V489 (= V260) 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)
39% identity, 87% coverage: 24:290/306 of query aligns to 249:519/674 of P13264
Sites not aligning to the query:
8jubA Crystal structure of glutaminasE C in complex with compound 27 (see paper)
38% identity, 91% coverage: 24:302/306 of query aligns to 100:382/401 of 8jubA
8jueA Crystal structure of glutaminasE C in complex with compound 11 (see paper)
38% identity, 91% coverage: 24:302/306 of query aligns to 101:383/401 of 8jueA
4o7dA Crystal structure of human glutaminase in complex don (see paper)
38% identity, 91% coverage: 24:302/306 of query aligns to 26:308/313 of 4o7dA
- active site: S68 (= S66), K71 (= K69), Y196 (= Y190), Y248 (= Y242), V266 (= V260)
- binding 5-oxo-l-norleucine: Y31 (= Y29), Q67 (= Q65), S68 (= S66), N117 (= N116), E163 (= E159), Y196 (= Y190), Y248 (= Y242), G265 (= G259), V266 (= V260)
8bsnA Human gls in complex with compound 27 (see paper)
38% identity, 91% coverage: 24:302/306 of query aligns to 23:305/311 of 8bsnA
6loxA Crystal structure of human glutaminase with macrocyclic inhibitor (see paper)
38% identity, 91% coverage: 24:302/306 of query aligns to 106:388/407 of 6loxA
- active site: S148 (= S66), K151 (= K69), Y276 (= Y190), Y328 (= Y242), V346 (= V260)
- 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 (≠ H99), L183 (= L100), F184 (≠ S101), L185 (= L102), N186 (≠ L103), Y256 (≠ L172)
5uqeD Multidomain structure of human kidney-type glutaminase(kga/gls) (see paper)
37% identity, 94% coverage: 2:290/306 of query aligns to 81:378/507 of 5uqeD
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- binding N,N'-[sulfanediylbis(ethane-2,1-diyl-1,3,4-thiadiazole-5,2-diyl)]bis(2-phenylacetamide): K184 (≠ H99), L185 (= L100), D191 (≠ E106), Y258 (≠ L172)
6umdB Crystal structure of human gac in complex with inhibitor upgl00012
38% identity, 91% coverage: 24:302/306 of query aligns to 108:390/409 of 6umdB
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- 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 (≠ P96), K184 (≠ H99), L185 (= L100), F186 (≠ S101), L187 (= L102), N188 (≠ L103), E189 (= E104), Y258 (≠ L172)
6ul9B Crystal structure of human gac in complex with inhibitor upgl00023
38% identity, 91% coverage: 24:302/306 of query aligns to 108:390/409 of 6ul9B
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- 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 (≠ P96), K184 (≠ H99), L185 (= L100), F186 (≠ S101), L187 (= L102), N188 (≠ L103), E189 (= E104), Y258 (≠ L172)
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)
38% identity, 91% coverage: 24:302/306 of query aligns to 108:390/410 of 5fi7A
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- 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 (≠ H99), L185 (= L100), F186 (≠ S101), L187 (= L102), E189 (= E104), Y258 (≠ L172)
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)
38% identity, 91% coverage: 24:302/306 of query aligns to 108:390/410 of 5fi6A
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- 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 (≠ P96), F182 (= F97), K184 (≠ H99), L185 (= L100), F186 (≠ S101), L187 (= L102), N188 (≠ L103), E189 (= E104), Y258 (≠ L172)
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)
38% identity, 91% coverage: 24:302/306 of query aligns to 108:390/410 of 5fi2A
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- 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 (≠ H99), L185 (= L100), F186 (≠ S101), L187 (= L102), Y258 (≠ L172)
8gwrB Near full length kidney type glutaminase in complex with 2,2-dimethyl- 2,3-dihydrobenzo[a] phenanthridin-4(1h)-one (ddp) (see paper)
39% identity, 87% coverage: 24:290/306 of query aligns to 101:371/501 of 8gwrB
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)
39% identity, 87% coverage: 24:290/306 of query aligns to 244:514/669 of O94925
- Y249 (= Y29) mutation to A: Loss of enzyme activity.
- S286 (= S66) binding ; mutation to A: Loss of enzyme activity.
- K289 (= K69) mutation to A: Loss of enzyme activity.
- P313 (= P92) to L: in GDPAG; loss of enzyme activity; dbSNP:rs1558973667
- F318 (= F97) mutation to Y: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with S-322.
- L321 (= L100) mutation to A: Decreased enzyme activity.
- F322 (≠ S101) mutation to S: No effect on catalytic activity. Loss of inhibition by BPTES; when associated with Y-318.
- L323 (= L102) mutation to A: Decreased enzyme activity.
- N335 (= N116) binding
- E381 (= E159) binding
- N388 (= N166) binding
- Y394 (≠ L172) mutation to A: Decreased enzyme activity.; mutation to L: No effect on catalytic activity. Loss of inhibition by BPTES.
- Y414 (= Y190) binding
- Y466 (= Y242) binding ; mutation to A: Loss of enzyme activity.
- S482 (= S258) to C: in CASGID; increased enzyme activity; dbSNP:rs1558986214
- V484 (= V260) binding
6umcB Crystal structure of human gac in complex with inhibitor upgl00012
37% identity, 91% coverage: 24:302/306 of query aligns to 108:390/410 of 6umcB
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- 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 (≠ H99), L185 (= L100), F186 (≠ S101), L187 (= L102), E189 (= E104), Y258 (≠ L172)
6ujgA Crystal structure of human gac in complex with inhibitor upgl00012
37% identity, 91% coverage: 24:302/306 of query aligns to 108:390/410 of 6ujgA
- active site: S150 (= S66), K153 (= K69), Y278 (= Y190), Y330 (= Y242), V348 (= V260)
- 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 (≠ H99), L185 (= L100), F186 (≠ S101), L187 (= L102), Y258 (≠ L172)
Query Sequence
>CCNA_00278 FitnessBrowser__Caulo:CCNA_00278
MKALSIPDVLAEVAVLVRPHFGKGKPADYIPQLATVPGGKFGMAVRMVDGDEHVIGDADE
GFSVQSITKVFALGLALNRLGDEIWTRVGKEPSGTPFNHLSLLEAEQGVPRNPFINAGAL
AVTDVLMDVTRDPAALVRDFGGFLCGERLEIDPAVATSELAHAWQNRAIASLMRAKGTIT
HDPEAVVAAYCRQCALSMSCRQLARAFLPLAAGGFSPIAQETVFPERLTRRLNALLLTCG
IYDSVGSFAYRVGLPAKSGVGGGIVAVVPGKATVAVWSPELDRFGTSVVGTAALEAFSQI
TNCSVL
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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