SitesBLAST
Comparing WP_084056568.1 NCBI__GCF_900176285.1:WP_084056568.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 13 hits to proteins with known functional sites (download)
P59846 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
68% identity, 98% coverage: 5:398/403 of query aligns to 2:395/400 of P59846
- 6:14 (vs. 9:17, 100% identical) binding ATP
- A33 (= A36) binding ATP
- G114 (= G117) binding ATP
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
66% identity, 98% coverage: 5:398/403 of query aligns to 2:386/386 of 1j20A
- active site: D12 (= D15), R92 (= R95), D121 (= D124), S168 (= S176)
- binding adenosine monophosphate: A6 (= A9), T13 (= T16), A33 (= A36), R92 (= R95), H113 (= H116), G114 (= G117), F125 (= F128)
- binding argininosuccinate: Y84 (= Y87), T88 (= T91), A115 (= A118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124), R124 (= R127), S177 (= S185), E179 (= E187), E253 (= E261), Y265 (= Y273)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
66% identity, 98% coverage: 5:398/403 of query aligns to 2:386/386 of 1j1zA
- active site: D12 (= D15), R92 (= R95), D121 (= D124), S168 (= S176)
- binding aspartic acid: A115 (= A118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124)
- binding adenosine-5'-triphosphate: A6 (= A9), T13 (= T16), A33 (= A36), R92 (= R95), I95 (= I98), H113 (= H116), G114 (= G117), F125 (= F128)
- binding citrulline: Y84 (= Y87), T88 (= T91), R124 (= R127), S168 (= S176), M169 (≠ C177), S177 (= S185), E179 (= E187), E253 (= E261), Y265 (= Y273)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
66% identity, 98% coverage: 5:398/403 of query aligns to 2:380/380 of 1kh3A
- active site: D12 (= D15), R92 (= R95), D121 (= D124), S168 (= S176)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A9), T13 (= T16), T32 (≠ A35), A33 (= A36), H113 (= H116), G114 (= G117), F125 (= F128), S168 (= S176), M169 (≠ C177)
- binding arginine: Y84 (= Y87), T88 (= T91), R124 (= R127), S168 (= S176), M169 (≠ C177), D170 (= D178), S177 (= S185), E179 (= E187), E253 (= E261), Y265 (= Y273)
- binding aspartic acid: A115 (= A118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
52% identity, 97% coverage: 6:396/403 of query aligns to 7:409/412 of P00966
- V64 (≠ L64) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y87) binding L-citrulline
- T91 (= T91) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S92) binding L-citrulline
- R95 (= R95) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P96) to H: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; to L: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; loss of argininosuccinate synthase activity; to S: in CTLN1; no effect on thermal stability; decreased argininosuccinate synthase activity
- G117 (= G117) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (= A118) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T119) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N123) binding L-aspartate; binding L-citrulline
- D124 (= D124) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R127) binding L-citrulline; to L: increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs201623252; to Q: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs201623252; to W: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs771794639
- R157 (= R153) to C: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770585183; to H: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908637
- K165 (≠ R161) modified: N6-acetyllysine; by CLOCK; mutation K->Q,R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-176 or R-176.
- K176 (≠ E172) modified: N6-acetyllysine; by CLOCK; mutation K->Q,R: Significant loss of acetylation but no decrease in enzyme activity; when associated with Q-165 or R-165.
- W179 (≠ Y175) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S176) binding L-citrulline; to I: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs121908638; to N: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908638
- S189 (= S185) binding L-citrulline
- E191 (= E187) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G188) to V: in CTLN1; decreased protein abundance
- V263 (= V254) to M: in CTLN1; mild clinical course; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs192838388
- R265 (= R256) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E261) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R263) to C: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs762387914; to H: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs768215008; to L: in CTLN1; increased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs768215008
- G280 (= G271) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y273) binding L-citrulline
- T284 (= T275) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (= M293) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R295) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G315) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G338) to R: in CTLN1; severe clinical course
- Y359 (≠ M350) to D: in CTLN1; mild clinical course
- G362 (= G353) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G381) to R: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908641
2nz2A Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline (see paper)
53% identity, 96% coverage: 6:391/403 of query aligns to 4:395/402 of 2nz2A
- active site: D13 (= D15), R92 (= R95), D121 (= D124), S176 (= S176)
- binding aspartic acid: A115 (= A118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124)
- binding citrulline: Y84 (= Y87), T88 (= T91), N120 (= N123), R124 (= R127), D178 (= D178), S185 (= S185), E187 (= E187), E266 (= E261), Y278 (= Y273)
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
49% identity, 99% coverage: 3:399/403 of query aligns to 3:386/390 of 7k5zA
- active site: D15 (= D15), R95 (= R95), D124 (= D124), S176 (= S176)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A9), Y10 (= Y10), S11 (= S11), C37 (≠ A36), G117 (= G117), F128 (= F128)
- binding arginine: Y88 (= Y87), T92 (= T91), D124 (= D124), R127 (= R127), S185 (= S185), E187 (= E187), E261 (= E261), Y273 (= Y273)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
42% identity, 97% coverage: 4:394/403 of query aligns to 2:392/397 of 4xfjB
- active site: D13 (= D15), R94 (= R95), D123 (= D124), S174 (= S176)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A9), Y8 (= Y10), S9 (= S11), T14 (= T16), I34 (≠ A36), G116 (= G117), C117 (≠ A118), F127 (= F128)
- binding arginine: Y86 (= Y87), S90 (≠ T91), R126 (= R127), A183 (≠ S185), E185 (= E187), E259 (= E261), E269 (≠ G271), Y271 (= Y273)
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
29% identity, 96% coverage: 4:388/403 of query aligns to 15:414/445 of 5us8A
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
29% identity, 96% coverage: 4:388/403 of query aligns to 11:410/438 of 6e5yA
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 96% coverage: 4:388/403 of query aligns to 12:410/447 of P0A6E4