SitesBLAST
Comparing WP_012469956.1 NCBI__GCF_000020385.1:WP_012469956.1 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)
53% identity, 99% coverage: 5:517/517 of query aligns to 2:501/501 of 1gpmA
- active site: G57 (= G60), C84 (= C87), Y85 (= Y88), H179 (= H174), E181 (= E176), D237 (= D232), K357 (= K373)
- binding adenosine monophosphate: G231 (≠ A226), L232 (= L227), S233 (= S228), V258 (= V253), F313 (= F308)
- binding pyrophosphate 2-: S233 (= S228), G235 (= G230), V236 (= V231), D237 (= D232), S238 (= S233), K357 (= K373)
5tw7F Crystal structure of a gmp synthase (glutamine-hydrolyzing) from neisseria gonorrhoeae
53% identity, 98% coverage: 10:517/517 of query aligns to 5:490/490 of 5tw7F
Q8IJR9 GMP synthase [glutamine-hydrolyzing]; PfGMPS; Glutamine amidotransferase; Guanosine monophosphate synthetase; EC 6.3.5.2 from Plasmodium falciparum (isolate 3D7) (see 3 papers)
43% identity, 98% coverage: 10:517/517 of query aligns to 8:555/555 of Q8IJR9
- Y18 (≠ V20) mutation to F: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- H20 (≠ Q22) 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 (≠ R26) 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 (= R27) mutation to L: No effect on glutaminase activity. 1.4-fold decrease in affinity for glutamine.
- C89 (= C87) 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 (= Q91) binding L-glutamine
- C113 (≠ R111) 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 (= W133) mutation to F: Slight decrease in affinity for glutamine. Slight increase in glutaminase activity.
- N169 (≠ S135) binding L-glutamine; mutation to S: Slight increase in affinity for glutamine. No defect in glutaminase activity.
- D172 (= D138) binding L-glutamine; mutation to A: 172-fold decrease in affinity for glutamine. Severe loss of glutaminase activity.
- H208 (= H174) binding L-glutamine
- Y212 (≠ V178) mutation to W: 2.7-fold decrease in affinity for glutamine. No defect in glutaminase activity.
- E213 (≠ H179) 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 (= R301) binding XMP
- D371 (= D333) Important for ATPPase activity; mutation to A: Impaired formation of adenyl-XMP intermediate. Slight increase in glutaminase activity.
- E374 (= E336) mutation to L: 8.9-fold decrease in affinity for ammonia. Severe loss of glutaminase activity.
- K376 (≠ V338) 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 (= K348) mutation to L: Severe loss of ATP pyrophosphatase (ATPPase) activity. 80 percent decrease in glutaminase activity. Impaired GMP formation.
- T387 (≠ S349) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. 20 percent decrease in glutaminase activity. No effect on GMP formation.
- H388 (= H350) 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 (= H351) Important for ATPPase activity; mutation to A: Loss of ATP pyrophosphatase (ATPPase) activity. 67 percent decrease in glutaminase activity. Impaired GMP formation.
- N390 (= N352) mutation to A: No effect on ATP pyrophosphatase (ATPPase) activity. Increases glutaminase activity. Loss of GMP formation.
- K411 (= K373) mutation to L: 70 percent decrease in glutaminase activity. Loss of GMP formation.
- D412 (= D374) mutation to A: 30 percent decrease in glutaminase activity. 7.9-fold decrease in affinity for glutamine.
- D413 (≠ E375) mutation to A: 35 percent decrease in glutaminase activity. 3.6-fold decrease in affinity for glutamine.
- K415 (≠ R377) mutation to L: Increases glutaminase activity. 4.2-fold decrease in affinity for ATP.
- Q476 (= Q438) binding XMP
- R539 (= R501) mutation to L: 85 percent decrease in glutaminase activity.
- K547 (= K509) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- I552 (= I514) binding XMP
- E553 (= E515) binding XMP; mutation to L: 85 percent decrease in glutaminase activity.
- E555 (= E517) mutation to L: 20 percent decrease in glutaminase activity. No effect on GMP formation.
2ywcA Crystal structure of gmp synthetase from thermus thermophilus in complex with xmp
48% identity, 98% coverage: 11:517/517 of query aligns to 2:475/475 of 2ywcA
- active site: G51 (= G60), R53 (≠ S62), C78 (= C87), Y79 (= Y88), H164 (= H174), E166 (= E176), D221 (= D232), K343 (= K373)
- binding xanthosine-5'-monophosphate: R288 (= R301), P366 (= P396), G367 (= G397), P368 (= P398), Q408 (= Q438), K467 (= K509), T471 (= T513), I472 (= I514), E473 (= E515)
4wioA Crystal structure of the c89a gmp synthetase inactive mutant from plasmodium falciparum in complex with glutamine (see paper)
40% identity, 98% coverage: 10:517/517 of query aligns to 2:525/525 of 4wioA
- active site: G52 (= G60), A83 (≠ C87), Y84 (= Y88), H197 (= H174), E199 (= E176), D255 (= D232), K393 (= K373)
- binding glutamine: Q87 (= Q91), N158 (≠ S135), H159 (= H136), N160 (≠ G137), D161 (= D138), H197 (= H174)
3uowA Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
40% identity, 98% coverage: 10:517/517 of query aligns to 3:517/517 of 3uowA
- active site: G53 (= G60), C84 (= C87), Y85 (= Y88), H198 (= H174), E200 (= E176), D255 (= D232), K381 (= K373)
- binding xanthosine-5'-monophosphate: R325 (= R301), P404 (= P396), G405 (= G397), P406 (= P398), Q446 (= Q438), K509 (= K509), T513 (= T513), I514 (= I514), E515 (= E515)
3uowB Crystal structure of pf10_0123, a gmp synthetase from plasmodium falciparum
40% identity, 98% coverage: 10:517/517 of query aligns to 1:477/477 of 3uowB
- active site: G47 (= G60), C67 (= C87), Y68 (= Y88), H162 (= H174), E164 (= E176), D218 (= D232), K340 (= K373)
- binding xanthosine-5'-monophosphate: R288 (= R301), P363 (= P396), G364 (= G397), P365 (= P398), Q405 (= Q438), K469 (= K509), T473 (= T513), I474 (= I514), E475 (= E515)
P49915 GMP synthase [glutamine-hydrolyzing]; GMP synthetase; Glutamine amidotransferase; EC 6.3.5.2 from Homo sapiens (Human) (see paper)
36% identity, 97% coverage: 11:514/517 of query aligns to 28:575/693 of P49915
- C104 (= C87) active site, For GATase activity
- H190 (= H174) active site, For GATase activity
- E192 (= E176) active site, For GATase activity
- R337 (= R301) binding XMP
- D522 (= D454) 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)
36% identity, 97% coverage: 11:514/517 of query aligns to 6:540/658 of 2vxoB
- active site: G55 (= G60), C82 (= C87), Y83 (= Y88), H165 (= H174), E167 (= E176), D223 (= D232), K381 (= K373)
- binding xanthosine-5'-monophosphate: R302 (= R301), G348 (= G342), K349 (≠ P343), P404 (= P396), G405 (= G397), P406 (= P398), R489 (= R456)
Sites not aligning to the query:
6jp9A Crsytal structure of a xmp complexed atppase subunit of m. Jannaschii gmp synthetase (see paper)
51% identity, 61% coverage: 205:517/517 of query aligns to 6:298/298 of 6jp9A
7yc6A Crystal structure of d110p mutant of gatase subunit of methanocaldococcus jannaschii gmp synthetase
38% identity, 36% coverage: 11:196/517 of query aligns to 2:179/183 of 7yc6A
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)
30% identity, 29% coverage: 42:191/517 of query aligns to 34:185/187 of P00903
- C79 (= C87) mutation to S: 10000-fold decrease in catalytic efficiency.
- H168 (= H174) mutation to Q: Loss of activity.
- E170 (= E176) 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.
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)
30% identity, 35% coverage: 11:191/517 of query aligns to 75:264/276 of Q42565
- G150 (= G85) mutation to D: In trp4-1; no visible phenotype under normal growth conditions.
- G176 (= G110) mutation to E: In wei7-2; insensitive to inhibition of root elongation by ethylene.
8hx8A Crystal structure of 4-amino-4-deoxychorismate synthase from streptomyces venezuelae co-crystallized with chorismate (see paper)
28% identity, 26% coverage: 55:190/517 of query aligns to 51:187/673 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
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)
25% identity, 34% coverage: 11:187/517 of query aligns to 4:183/193 of P00900
- C84 (= C87) active site, Nucleophile; for GATase activity
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1i7qB Anthranilate synthase from s. Marcescens (see paper)
25% identity, 34% coverage: 11:187/517 of query aligns to 3:182/192 of 1i7qB
- active site: G58 (≠ S62), C83 (= C87), L84 (≠ Y88), H169 (= H174), E171 (= E176)
- binding glutamic acid: P55 (≠ G59), G56 (= G60), G58 (≠ S62), C83 (= C87), L84 (≠ Y88), Q87 (= Q91), H132 (= H136), S133 (≠ G137), L134 (≠ D138)
7d54A Crstal structure msgatase with gln (see paper)
34% identity, 19% coverage: 78:177/517 of query aligns to 92:182/242 of 7d54A
Sites not aligning to the query:
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)
26% identity, 36% coverage: 2:185/517 of query aligns to 235:413/430 of Q9LVW7
- H410 (≠ K182) mutation to Y: In ven6-1; reticulate leaf phenotype.
O25096 NH(3)-dependent NAD(+) synthetase; EC 6.3.1.5 from Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (see paper)
25% identity, 38% coverage: 200:394/517 of query aligns to 9:182/260 of O25096
- 31:38 (vs. 226:233, 75% identical) binding ATP
- T132 (= T321) binding ATP
- K161 (= K373) binding ATP
1xngB Crystal structure of nh3-dependent NAD+ synthetase from helicobacter pylori (see paper)
25% identity, 38% coverage: 200:394/517 of query aligns to 7:180/262 of 1xngB
- active site: D35 (= D232), E135 (vs. gap)
- binding adenosine-5'-triphosphate: G29 (≠ A226), L30 (= L227), S31 (= S228), G33 (= G230), L34 (≠ V231), D35 (= D232), S36 (= S233), M56 (≠ V253), R112 (vs. gap), T130 (= T321), E135 (vs. gap), K159 (= K373)
- binding nicotinic acid adenine dinucleotide: R21 (≠ V218), F23 (≠ N220), N106 (= N306), Y117 (= Y310), S120 (vs. gap), L121 (vs. gap), L126 (≠ K317), Y140 (≠ Q327), G141 (= G328), T142 (= T329), D146 (= D333), A150 (≠ S337)
Sites not aligning to the query:
Query Sequence
>WP_012469956.1 NCBI__GCF_000020385.1:WP_012469956.1
MSSTDIHSQKILILDFGSQVTQLIARRIREQSVYCEIHPYNMGLEKIKAFAPQGIILSGG
PSSVYDADAPHSDAGVYELGVPVLGICYGMQLMTSQLGGKVERSDKREFGRAAMTIDDTT
DLFSGLSGKEEVWMSHGDKIEQMPKGFSAIAHTDNTPAAAMKDEKRRLYAVQFHPEVVHT
PKGAEMLGNFVFTVCGCQPIWTMANFIETEIAAIREKVGNGKVICALSGGVDSSVVAVLL
HKAIGDQLQCIFVNNGLLRKGEAEKVVNLFTRHFKINLDYVEASSRFLDKLKGITDPEQK
RKIIGNEFIYLFEDEAKKIGTVDWLAQGTLYPDVIESVSTKGPSAVIKSHHNVGGLPDRM
KMKLIEPVRELFKDEVRLLGKELGLPDEVIHRQPFPGPGLAIRCIGEITADRLEILRESD
AIVLDEIRKAGLYREIWQSFAVLLPVRSVGVMGDARTYDYTIALRAVNSLDGMTADWVKL
PYEVMGSISSRIINEVKGVNRVVYDISQKPPATIEWE
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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