SitesBLAST
Comparing WP_008806631.1 NCBI__GCF_000025465.1:WP_008806631.1 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)
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
95% identity, 100% coverage: 1:447/447 of query aligns to 1:447/447 of P0A6E4
- M1 (= M1) modified: Initiator methionine, Removed
- 17:25 (vs. 17:25, 100% identical) binding ATP
- A43 (= A43) binding ATP
- Y99 (= Y99) binding L-citrulline
- G129 (= G129) binding ATP
- T131 (= T131) binding ATP; binding L-aspartate
- N135 (= N135) binding L-aspartate; binding L-citrulline
- D136 (= D136) binding ATP; binding L-aspartate
- R139 (= R139) binding L-citrulline
- S192 (= S192) binding L-citrulline
- D194 (= D194) binding ATP
- T201 (= T201) binding L-citrulline
- E203 (= E203) binding L-citrulline
- E280 (= E280) binding L-citrulline
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
94% identity, 100% coverage: 2:447/447 of query aligns to 1:439/439 of 1kp3A
- active site: D22 (= D23), R106 (= R107), D135 (= D136), S191 (= S192)
- binding adenosine-5'-triphosphate: A16 (= A17), S18 (= S19), G20 (= G21), D22 (= D23), T23 (= T24), T41 (= T42), A42 (= A43), D127 (= D128), G128 (= G129), S129 (= S130), F139 (= F140), D193 (= D194)
- binding citrulline: Y98 (= Y99), T102 (= T103), P103 (= P104), T130 (= T131), G133 (= G134), N134 (= N135), D135 (= D136), R138 (= R139), D193 (= D194), T200 (= T201), E202 (= E203), E202 (= E203), E279 (= E280), S287 (= S288), Y291 (= Y292)
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
94% identity, 98% coverage: 2:441/447 of query aligns to 1:432/432 of 1k97A
- active site: D22 (= D23), R106 (= R107), D135 (= D136), S191 (= S192)
- binding aspartic acid: S129 (= S130), T130 (= T131), G133 (= G134), N134 (= N135), D135 (= D136)
- binding citrulline: Y98 (= Y99), T102 (= T103), P103 (= P104), R138 (= R139), S191 (= S192), T192 (= T193), D193 (= D194), T200 (= T201), E202 (= E203), E279 (= E280), Y291 (= Y292), Y331 (= Y332)
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
79% identity, 99% coverage: 1:441/447 of query aligns to 4:445/445 of 5us8A
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
79% identity, 98% coverage: 2:441/447 of query aligns to 1:438/438 of 6e5yA
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
30% identity, 80% coverage: 10:368/447 of query aligns to 2:348/390 of 7k5zA
- active site: D15 (= D23), R95 (= R107), D124 (= D136), S176 (= S192)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A17), Y10 (≠ F18), S11 (= S19), C37 (≠ A43), G117 (= G129), F128 (= F140)
- binding arginine: Y88 (= Y99), T92 (= T103), D124 (= D136), R127 (= R139), S185 (≠ T201), E187 (= E203), E261 (= E280), Y273 (= Y292)
P59846 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
30% identity, 82% coverage: 13:380/447 of query aligns to 2:357/400 of P59846
- 6:14 (vs. 17:25, 89% identical) binding ATP
- A33 (= A43) binding ATP
- G114 (= G129) binding ATP
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
27% identity, 90% coverage: 14:414/447 of query aligns to 7:401/412 of P00966
- V64 (≠ C73) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y99) binding L-citrulline
- T91 (= T103) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (≠ P104) binding L-citrulline
- R95 (= R107) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (≠ A108) 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 (= G129) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (≠ S130) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T131) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N135) binding L-aspartate; binding L-citrulline
- D124 (= D136) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R139) 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 (= R169) 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 (≠ I177) 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 (≠ E188) 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 (≠ Y191) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S192) 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 (≠ T201) binding L-citrulline
- E191 (= E203) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (= A204) to V: in CTLN1; decreased protein abundance
- V263 (≠ L273) 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 (≠ M275) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E280) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R282) 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 (= G290) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y292) binding L-citrulline
- T284 (≠ A294) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ H312) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (≠ E314) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G334) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G358) to R: in CTLN1; severe clinical course
- Y359 (= Y370) to D: in CTLN1; mild clinical course
- G362 (≠ N374) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G403) 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)
26% identity, 90% coverage: 14:414/447 of query aligns to 4:396/402 of 2nz2A
- active site: D13 (= D23), R92 (= R107), D121 (= D136), S176 (= S192)
- binding aspartic acid: A115 (≠ S130), T116 (= T131), G119 (= G134), N120 (= N135), D121 (= D136)
- binding citrulline: Y84 (= Y99), T88 (= T103), N120 (= N135), R124 (= R139), D178 (= D194), S185 (≠ T201), E187 (= E203), E266 (= E280), Y278 (= Y292)
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
29% identity, 82% coverage: 13:380/447 of query aligns to 2:352/386 of 1j20A
- active site: D12 (= D23), R92 (= R107), D121 (= D136), S168 (= S192)
- binding adenosine monophosphate: A6 (= A17), T13 (= T24), A33 (= A43), R92 (= R107), H113 (≠ D128), G114 (= G129), F125 (= F140)
- binding argininosuccinate: Y84 (= Y99), T88 (= T103), A115 (≠ S130), T116 (= T131), G119 (= G134), N120 (= N135), D121 (= D136), R124 (= R139), S177 (≠ T201), E179 (= E203), E253 (= E280), Y265 (= Y292)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
29% identity, 82% coverage: 13:380/447 of query aligns to 2:352/386 of 1j1zA
- active site: D12 (= D23), R92 (= R107), D121 (= D136), S168 (= S192)
- binding aspartic acid: A115 (≠ S130), T116 (= T131), G119 (= G134), N120 (= N135), D121 (= D136)
- binding adenosine-5'-triphosphate: A6 (= A17), T13 (= T24), A33 (= A43), R92 (= R107), I95 (≠ T110), H113 (≠ D128), G114 (= G129), F125 (= F140)
- binding citrulline: Y84 (= Y99), T88 (= T103), R124 (= R139), S168 (= S192), M169 (≠ T193), S177 (≠ T201), E179 (= E203), E253 (= E280), Y265 (= Y292)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
29% identity, 82% coverage: 13:380/447 of query aligns to 2:352/380 of 1kh3A
- active site: D12 (= D23), R92 (= R107), D121 (= D136), S168 (= S192)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A17), T13 (= T24), T32 (= T42), A33 (= A43), H113 (≠ D128), G114 (= G129), F125 (= F140), S168 (= S192), M169 (≠ T193)
- binding arginine: Y84 (= Y99), T88 (= T103), R124 (= R139), S168 (= S192), M169 (≠ T193), D170 (= D194), S177 (≠ T201), E179 (= E203), E253 (= E280), Y265 (= Y292)
- binding aspartic acid: A115 (≠ S130), T116 (= T131), G119 (= G134), N120 (= N135), D121 (= D136)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
29% identity, 86% coverage: 12:395/447 of query aligns to 2:372/397 of 4xfjB
- active site: D13 (= D23), R94 (= R107), D123 (= D136), S174 (= S192)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A17), Y8 (≠ F18), S9 (= S19), T14 (= T24), I34 (≠ A43), G116 (= G129), C117 (≠ S130), F127 (= F140)
- binding arginine: Y86 (= Y99), S90 (≠ T103), R126 (= R139), A183 (≠ T201), E185 (= E203), E259 (= E280), E269 (≠ G290), Y271 (= Y292)
Query Sequence
>WP_008806631.1 NCBI__GCF_000025465.1:WP_008806631.1
MTTILKHLPVGQRIGIAFSGGLDTSAALLWMRKKGAVPYAYTANLGQPDEDDYDAIPRRA
KEYGAEGARLIDCRKQLVAEGIAAIQCGAFHNTTGGLTYFNTTPLGRAVTGTMLVAAMKE
DGVNIWGDGSTYKGNDIERFYRYGLLTNAELQIYKPWLDSDFIDELGGRHEMSEFMIACG
FDYKMSVEKAYSTDSNMLGATHEAKDLEFLNSSVKIVNPIMGVKFWDENVKIPAEEVTVR
FEQGHPVALNGKTFADDVEMMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALL
HIAYERLLTGIHNEDTIEQYHAHGRQLGRLLYQGRWFDSQALMLRDSLQRWVASQITGEV
TLELRRGNDYSILNTVSDNLTYKAERLTMEKGDSMFTAEDRIGQLTMRNLDITDTREKLF
GYAQSGLLSASSATGLPQVENLENKGK
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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