SitesBLAST
Comparing WP_012673904.1 NCBI__GCF_000021545.1:WP_012673904.1 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)
1gpmA Escherichia coli gmp synthetase complexed with amp and pyrophosphate (see paper)
51% identity, 99% coverage: 5:511/511 of query aligns to 8:501/501 of 1gpmA
- active site: G57 (= G54), C84 (= C81), Y85 (= Y82), H179 (= H168), E181 (= E170), D237 (= D226), K357 (= K367)
- binding adenosine monophosphate: G231 (≠ A220), L232 (= L221), S233 (= S222), V258 (= V247), F313 (= F302)
- binding pyrophosphate 2-: S233 (= S222), G235 (= G224), V236 (= V225), D237 (= D226), S238 (= S227), K357 (= K367)
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
52% identity, 99% coverage: 5:511/511 of query aligns to 6:490/490 of 5tw7F
2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
50% identity, 99% coverage: 5:511/511 of query aligns to 2:475/475 of 2ywcA
- active site: G51 (= G54), R53 (≠ A56), C78 (= C81), Y79 (= Y82), H164 (= H168), E166 (= E170), D221 (= D226), K343 (= K367)
- binding xanthosine-5'-monophosphate: R288 (= R295), P366 (= P390), G367 (= G391), P368 (= P392), Q408 (= Q432), K467 (= K503), T471 (= T507), I472 (= I508), E473 (= E509)
Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
45% identity, 100% coverage: 2:511/511 of query aligns to 6:555/555 of Q8IJR9
- Y18 (= Y14) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- H20 (≠ Q16) mutation to A: Slight decrease in affinity for glutamine. 1.8-fold increase in affinity for ATP. Slight increase in affinity for XMP. Moderate reduction in glutaminase activity.
- K24 (≠ R20) mutation to L: 50 percent decrease in glutaminase activity. 5.3-fold decrease in affinity for glutamine. 1.7-fold increase in affinity for ATP. 2.8-fold decrease in affinity for XMP.
- R25 (= R21) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- C89 (= C81) mutation to A: Loss of glutaminase activity, however, glutamine binding is not affected. In presence of exogenous ammonia, the amination of XMP to produce GMP is normal. 2.3-fold decrease in affinity for ATP and 1.8-fold decrease in affinity for XMP. 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-113.
- Q93 (= Q85) binding L-glutamine
- C113 (≠ R105) mutation to A: 2.9-fold decrease in affinity for ATP and 1.9-fold decrease in affinity for XMP; when associated with A-89.
- K160 (vs. gap) mutation to L: No effect on glutaminase activity. 1.2-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
- W167 (= W127) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ S129) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (= D132) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H168) binding L-glutamine
- Y212 (≠ S172) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ H173) mutation to A: 40 percent decrease in glutaminase activity. 1.4-fold decrease in affinity for glutamine. 1.3-fold decrease in affinity for ATP. 1.8-fold decrease in affinity for XMP.
- R336 (= R295) binding XMP
- D371 (= D327) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- E374 (= E330) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- K376 (≠ V332) mutation to L: 20 percent decrease in glutaminase activity. 4.4-fold decrease in affinity for glutamine. 1.8-fold decrease in affinity for XMP.
- K386 (= K342) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- T387 (= T343) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- H388 (= H344) Important for ATPPase activity; mutation to A: Moderate decrease in ATP pyrophosphatase (ATPPase) activity. Reduces 49 percent decrease in glutaminase activity. Impaired GMP formation.
- H389 (= H345) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- N390 (= N346) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- K411 (= K367) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- D412 (= D368) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- D413 (≠ E369) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- K415 (≠ R371) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- Q476 (= Q432) binding XMP
- R539 (= R495) mutation to L: 85 percent decrease in glutaminase activity.
- K547 (= K503) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- I552 (= I508) binding XMP
- E553 (= E509) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- E555 (= E511) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.
4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
43% identity, 99% coverage: 5:511/511 of query aligns to 3:525/525 of 4wioA
- active site: G52 (= G54), A83 (≠ C81), Y84 (= Y82), H197 (= H168), E199 (= E170), D255 (= D226), K393 (= K367)
- binding glutamine: Q87 (= Q85), N158 (≠ S129), H159 (= H130), N160 (≠ A131), D161 (= D132), H197 (= H168)
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
42% identity, 100% coverage: 2:511/511 of query aligns to 1:517/517 of 3uowA
- active site: G53 (= G54), C84 (= C81), Y85 (= Y82), H198 (= H168), E200 (= E170), D255 (= D226), K381 (= K367)
- binding xanthosine-5'-monophosphate: R325 (= R295), P404 (= P390), G405 (= G391), P406 (= P392), Q446 (= Q432), K509 (= K503), T513 (= T507), I514 (= I508), E515 (= E509)
3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
43% identity, 99% coverage: 5:511/511 of query aligns to 2:477/477 of 3uowB
- active site: G47 (= G54), C67 (= C81), Y68 (= Y82), H162 (= H168), E164 (= E170), D218 (= D226), K340 (= K367)
- binding xanthosine-5'-monophosphate: R288 (= R295), P363 (= P390), G364 (= G391), P365 (= P392), Q405 (= Q432), K469 (= K503), T473 (= T507), I474 (= I508), E475 (= E509)
6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
61% identity, 61% coverage: 199:511/511 of query aligns to 6:298/298 of 6jp9A
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
40% identity, 97% coverage: 4:498/511 of query aligns to 27:562/693 of P49915
- C104 (= C81) active site, For GATase activity
- H190 (= H168) active site, For GATase activity
- E192 (= E170) active site, For GATase activity
- R337 (= R295) binding XMP
- D522 (= D448) binding XMP
Sites not aligning to the query:
- 610 binding XMP
- 685 binding XMP
- 691 binding XMP
2vxoB Human gmp synthetase in complex with xmp (see paper)
41% identity, 97% coverage: 4:498/511 of query aligns to 5:527/658 of 2vxoB
- active site: G55 (= G54), C82 (= C81), Y83 (= Y82), H165 (= H168), E167 (= E170), D223 (= D226), K381 (= K367)
- binding xanthosine-5'-monophosphate: R302 (= R295), G348 (= G336), K349 (≠ P337), P404 (= P390), G405 (= G391), P406 (= P392), R489 (= R450)
Sites not aligning to the query:
7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
44% identity, 37% coverage: 5:192/511 of query aligns to 2:181/183 of 7yc6A
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
36% identity, 29% coverage: 37:184/511 of query aligns to 44:187/673 of 8hx8A
Sites not aligning to the query:
- binding magnesium ion: 521, 655, 658
- binding tryptophan: 231, 232, 233, 241, 243, 458, 459, 460, 614
Q42565 Anthranilate synthase beta subunit 1, chloroplastic; Anthranilate synthase component 2-1; Anthranilate synthase, glutamine amidotransferase component 2-1; Protein TRYPTOPHAN BIOSYNTHESIS 4; Protein WEAK ETHYLENE INSENSITIVE 7; EC 4.1.3.27 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
31% identity, 36% coverage: 2:184/511 of query aligns to 72:263/276 of Q42565
- G150 (= G79) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
- G176 (= G104) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.
P00903 Aminodeoxychorismate synthase component 2; ADC synthase; ADCS; 4-amino-4-deoxychorismate synthase component 2; Aminodeoxychorismate synthase, glutamine amidotransferase component; EC 2.6.1.85 from Escherichia coli (strain K12) (see paper)
34% identity, 28% coverage: 46:187/511 of query aligns to 44:187/187 of P00903
- C79 (= C81) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H168) mutation to Q: Loss of activity.
- E170 (= E170) mutation to A: 150-fold decrease in catalytic efficiency.; mutation to D: 4-fold decrease in catalytic efficiency.; mutation E->K,Q: Loss of activity.
Q9LVW7 Carbamoyl phosphate synthase small chain, chloroplastic; Carbamoyl phosphate synthetase glutamine chain; Protein VENOSA 6; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 33% coverage: 5:172/511 of query aligns to 244:406/430 of Q9LVW7
Sites not aligning to the query:
- 410 H→Y: In ven6-1; reticulate leaf phenotype.
1i7qB Anthranilate synthase from s. Marcescens (see paper)
27% identity, 35% coverage: 5:183/511 of query aligns to 3:184/192 of 1i7qB
- active site: G58 (≠ A56), C83 (= C81), L84 (≠ Y82), H169 (= H168), E171 (= E170)
- binding glutamic acid: P55 (≠ G53), G56 (= G54), G58 (≠ A56), C83 (= C81), L84 (≠ Y82), Q87 (= Q85), H132 (= H130), S133 (≠ A131), L134 (≠ D132)
P00900 Anthranilate synthase component 2; AS; ASII; Anthranilate synthase, GATase component; Anthranilate synthase, glutamine amidotransferase component; EC 4.1.3.27 from Serratia marcescens (see 3 papers)
27% identity, 35% coverage: 5:183/511 of query aligns to 4:185/193 of P00900
- C84 (= C81) active site, Nucleophile; for GATase activity
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
P0A6F1 Carbamoyl phosphate synthase small chain; Carbamoyl phosphate synthetase glutamine chain; EC 6.3.5.5 from Escherichia coli (strain K12) (see paper)
28% identity, 33% coverage: 5:172/511 of query aligns to 194:357/382 of P0A6F1
- G241 (= G54) binding L-glutamine
- G243 (≠ A56) binding L-glutamine
- L270 (≠ Y82) binding L-glutamine
- Q273 (= Q85) binding L-glutamine
- N311 (≠ W127) binding L-glutamine
- G313 (≠ S129) binding L-glutamine
- F314 (≠ H130) binding L-glutamine
Sites not aligning to the query:
1ce8B Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
28% identity, 33% coverage: 5:172/511 of query aligns to 193:356/379 of 1ce8B
Sites not aligning to the query:
1c3oB Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
27% identity, 33% coverage: 5:172/511 of query aligns to 193:356/379 of 1c3oB
- active site: K201 (≠ Q13), S268 (≠ C81), H352 (= H168), E354 (= E170)
- binding glutamine: N239 (≠ G53), G240 (= G54), G242 (≠ A56), S268 (≠ C81), L269 (≠ Y82), N310 (≠ W127), H311 (≠ M128), G312 (≠ S129), F313 (≠ H130)
Sites not aligning to the query:
Query Sequence
>WP_012673904.1 NCBI__GCF_000021545.1:WP_012673904.1
MHQGIVILDFGSQYTQLIARRIRELHIYSEILPYNTPVEEILKHNPKGIIFSGGPASVYE
KDAPKPDERVYDLGLPILGICYGLQLITHHFGGEVVKADKHEYGRAEIQVLNHEDLFYEI
PEFTHVWMSHADKVVKLPQGFEVLARSFNAPYAAVRNKEKKIWGVQFHPEVSHTLLGKEI
LKNFAVRICGCKQDWTMGNFLMEEIVKIRQTVGNKKAICALSGGVDSSVAAVLVHNAIGD
NLTCIFVDNGLLRKGEREQVEKTFRDNFHIPLIVVDARERFLNALKGITDPEQKRKIIGN
LFIEVFEEEAKKLKDVEFLVQGTLYPDVIESVSVKGPSAVIKTHHNVGGLPERMNLKLIE
PLRELFKDEVRELGKELGLPDEIIYRQPFPGPGLAIRVIGEVTQESLDILREADAIVLEE
IKKAGLYKDLWQSFAVLLPIHTVGVMGDYRTYEKVIAVRAVESSDGMTADWARLPYDLLD
TIMRRIINEVKGVNRVVYDISSKPPATIEWE
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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