SitesBLAST
Comparing WP_012471178.1 NCBI__GCF_000020385.1:WP_012471178.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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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)
62% identity, 97% coverage: 9:402/405 of query aligns to 2:394/400 of P59846
- 6:14 (vs. 13:21, 100% identical) binding ATP
- A33 (= A40) binding ATP
- G114 (= G121) binding ATP
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
62% identity, 97% coverage: 9:402/405 of query aligns to 2:385/386 of 1j20A
- active site: D12 (= D19), R92 (= R99), D121 (= D128), S168 (= S180)
- binding adenosine monophosphate: A6 (= A13), T13 (= T20), A33 (= A40), R92 (= R99), H113 (= H120), G114 (= G121), F125 (= F132)
- binding argininosuccinate: Y84 (= Y91), T88 (= T95), A115 (= A122), T116 (= T123), G119 (= G126), N120 (= N127), D121 (= D128), R124 (= R131), S177 (= S189), E179 (= E191), E253 (= E265), Y265 (= Y277)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
62% identity, 97% coverage: 9:402/405 of query aligns to 2:385/386 of 1j1zA
- active site: D12 (= D19), R92 (= R99), D121 (= D128), S168 (= S180)
- binding aspartic acid: A115 (= A122), T116 (= T123), G119 (= G126), N120 (= N127), D121 (= D128)
- binding adenosine-5'-triphosphate: A6 (= A13), T13 (= T20), A33 (= A40), R92 (= R99), I95 (= I102), H113 (= H120), G114 (= G121), F125 (= F132)
- binding citrulline: Y84 (= Y91), T88 (= T95), R124 (= R131), S168 (= S180), M169 (≠ S181), S177 (= S189), E179 (= E191), E253 (= E265), Y265 (= Y277)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
62% identity, 97% coverage: 9:402/405 of query aligns to 2:379/380 of 1kh3A
- active site: D12 (= D19), R92 (= R99), D121 (= D128), S168 (= S180)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A13), T13 (= T20), T32 (≠ S39), A33 (= A40), H113 (= H120), G114 (= G121), F125 (= F132), S168 (= S180), M169 (≠ S181)
- binding arginine: Y84 (= Y91), T88 (= T95), R124 (= R131), S168 (= S180), M169 (≠ S181), D170 (= D182), S177 (= S189), E179 (= E191), E253 (= E265), Y265 (= Y277)
- binding aspartic acid: A115 (= A122), T116 (= T123), G119 (= G126), N120 (= N127), D121 (= D128)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
50% identity, 98% coverage: 10:404/405 of query aligns to 7:408/412 of P00966
- V64 (≠ L68) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y91) binding L-citrulline
- T91 (= T95) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S96) binding L-citrulline
- R95 (= R99) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P100) 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 (= G121) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (= A122) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T123) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N127) binding L-aspartate; binding L-citrulline
- D124 (= D128) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R131) 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 (= R157) 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 (= K165) 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 (= K176) 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 (= W179) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S180) 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 (= S189) binding L-citrulline
- E191 (= E191) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G192) to V: in CTLN1; decreased protein abundance
- V263 (= V258) 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 (= R260) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E265) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R267) 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 (= G275) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y277) binding L-citrulline
- T284 (= T279) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (= M297) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R299) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G319) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G342) to R: in CTLN1; severe clinical course
- Y359 (≠ R354) to D: in CTLN1; mild clinical course
- G362 (= G357) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G386) 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)
51% identity, 96% coverage: 10:396/405 of query aligns to 4:395/402 of 2nz2A
- active site: D13 (= D19), R92 (= R99), D121 (= D128), S176 (= S180)
- binding aspartic acid: A115 (= A122), T116 (= T123), G119 (= G126), N120 (= N127), D121 (= D128)
- binding citrulline: Y84 (= Y91), T88 (= T95), N120 (= N127), R124 (= R131), D178 (= D182), S185 (= S189), E187 (= E191), E266 (= E265), Y278 (= Y277)
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
43% identity, 97% coverage: 7:399/405 of query aligns to 3:381/390 of 7k5zA
- active site: D15 (= D19), R95 (= R99), D124 (= D128), S176 (= S180)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A13), Y10 (= Y14), S11 (= S15), C37 (≠ A40), G117 (= G121), F128 (= F132)
- binding arginine: Y88 (= Y91), T92 (= T95), D124 (= D128), R127 (= R131), S185 (= S189), E187 (= E191), E261 (= E265), Y273 (= Y277)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
40% identity, 97% coverage: 8:399/405 of query aligns to 2:392/397 of 4xfjB
- active site: D13 (= D19), R94 (= R99), D123 (= D128), S174 (= S180)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A13), Y8 (= Y14), S9 (= S15), T14 (= T20), I34 (≠ A40), G116 (= G121), C117 (≠ A122), F127 (= F132)
- binding arginine: Y86 (= Y91), S90 (≠ T95), R126 (= R131), A183 (≠ S189), E185 (= E191), E259 (= E265), E269 (≠ G275), Y271 (= Y277)
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
28% identity, 95% coverage: 8:393/405 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.
28% identity, 95% coverage: 8:393/405 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)
25% identity, 96% coverage: 8:395/405 of query aligns to 12:412/447 of P0A6E4
- 17:25 (vs. 13:21, 89% identical) binding ATP
- A43 (= A40) binding ATP
- Y99 (= Y91) binding L-citrulline
- G129 (= G121) binding ATP
- T131 (= T123) binding ATP; binding L-aspartate
- N135 (= N127) binding L-aspartate; binding L-citrulline
- D136 (= D128) binding ATP; binding L-aspartate
- R139 (= R131) binding L-citrulline
- S192 (= S180) binding L-citrulline
- D194 (= D182) binding ATP
- T201 (≠ S189) binding L-citrulline
- E203 (= E191) binding L-citrulline
- E280 (= E265) binding L-citrulline
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
25% identity, 92% coverage: 8:381/405 of query aligns to 11:396/439 of 1kp3A
- active site: D22 (= D19), R106 (= R99), D135 (= D128), S191 (= S180)
- binding adenosine-5'-triphosphate: A16 (= A13), S18 (= S15), G20 (= G17), D22 (= D19), T23 (= T20), T41 (≠ S39), A42 (= A40), D127 (≠ H120), G128 (= G121), S129 (≠ A122), F139 (= F132), D193 (= D182)
- binding citrulline: Y98 (= Y91), T102 (= T95), P103 (≠ S96), T130 (= T123), G133 (= G126), N134 (= N127), D135 (= D128), R138 (= R131), D193 (= D182), T200 (≠ S189), E202 (= E191), E202 (= E191), E279 (= E265), S287 (= S273), Y291 (= Y277)
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
25% identity, 96% coverage: 8:395/405 of query aligns to 11:403/432 of 1k97A
- active site: D22 (= D19), R106 (= R99), D135 (= D128), S191 (= S180)
- binding aspartic acid: S129 (≠ A122), T130 (= T123), G133 (= G126), N134 (= N127), D135 (= D128)
- binding citrulline: Y98 (= Y91), T102 (= T95), P103 (≠ S96), R138 (= R131), S191 (= S180), T192 (≠ S181), D193 (= D182), T200 (≠ S189), E202 (= E191), E279 (= E265), Y291 (= Y277), Y331 (= Y317)
Query Sequence
>WP_012471178.1 NCBI__GCF_000020385.1:WP_012471178.1
MAKKQEVKKIVLAYSGGLDTSIILKWLKNEYGAEIVAFSADLGQGDELAPVREKALKTGA
STVYIDDLREEFVRDFVYPMFRANAIYEGHYLLGTSIARPLIAKRQMEIAKLEGCDAVSH
GATGKGNDQVRFELAYYHFDPSISVIAPWREWKLNSRKALIAYAKKNDIPIPITKKRPWS
SDRNLLHISFEGGILEDTWAEAPEEMYVLTCKPEKAPNKPQYVEIEFEQGNAVAVDGVRM
TPAQLLAHLNTIGGLHGVGRVDLLENRSVGMKSRGVYETPGGTILREAHSAVEQITMDRE
VMRIRDSLIPEYARQVYAGYWFSPEREMLQTLIDESQKTVNGVARVKLYKGHCRTVGRKS
ETNSLFNLDFATFEKDKVYNQADAEGFIKINSLRLRIRSLMQGKK
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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