SitesBLAST
Comparing WP_012757993.1 NCBI__GCF_000023185.1:WP_012757993.1 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)
61% identity, 99% coverage: 6:402/403 of query aligns to 2:397/400 of P59846
- 6:14 (vs. 10:18, 89% identical) binding ATP
- A33 (= A37) binding ATP
- G114 (= G118) binding ATP
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
61% identity, 97% coverage: 6:395/403 of query aligns to 2:379/386 of 1j20A
- active site: D12 (= D16), R92 (= R96), D121 (= D125), S168 (= S179)
- binding adenosine monophosphate: A6 (≠ S10), T13 (= T17), A33 (= A37), R92 (= R96), H113 (= H117), G114 (= G118), F125 (= F129)
- binding argininosuccinate: Y84 (= Y88), T88 (≠ S92), A115 (= A119), T116 (= T120), G119 (= G123), N120 (= N124), D121 (= D125), R124 (= R128), S177 (= S188), E179 (= E190), E253 (= E264), Y265 (= Y276)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
61% identity, 97% coverage: 6:395/403 of query aligns to 2:379/386 of 1j1zA
- active site: D12 (= D16), R92 (= R96), D121 (= D125), S168 (= S179)
- binding aspartic acid: A115 (= A119), T116 (= T120), G119 (= G123), N120 (= N124), D121 (= D125)
- binding adenosine-5'-triphosphate: A6 (≠ S10), T13 (= T17), A33 (= A37), R92 (= R96), I95 (= I99), H113 (= H117), G114 (= G118), F125 (= F129)
- binding citrulline: Y84 (= Y88), T88 (≠ S92), R124 (= R128), S168 (= S179), M169 (≠ I180), S177 (= S188), E179 (= E190), E253 (= E264), Y265 (= Y276)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
60% identity, 97% coverage: 6:395/403 of query aligns to 2:373/380 of 1kh3A
- active site: D12 (= D16), R92 (= R96), D121 (= D125), S168 (= S179)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (≠ S10), T13 (= T17), T32 (= T36), A33 (= A37), H113 (= H117), G114 (= G118), F125 (= F129), S168 (= S179), M169 (≠ I180)
- binding arginine: Y84 (= Y88), T88 (≠ S92), R124 (= R128), S168 (= S179), M169 (≠ I180), D170 (= D181), S177 (= S188), E179 (= E190), E253 (= E264), Y265 (= Y276)
- binding aspartic acid: A115 (= A119), T116 (= T120), G119 (= G123), N120 (= N124), D121 (= D125)
2nz2A Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline (see paper)
48% identity, 97% coverage: 7:397/403 of query aligns to 4:397/402 of 2nz2A
- active site: D13 (= D16), R92 (= R96), D121 (= D125), S176 (= S179)
- binding aspartic acid: A115 (= A119), T116 (= T120), G119 (= G123), N120 (= N124), D121 (= D125)
- binding citrulline: Y84 (= Y88), T88 (≠ S92), N120 (= N124), R124 (= R128), D178 (= D181), S185 (= S188), E187 (= E190), E266 (= E264), Y278 (= Y276)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
48% identity, 99% coverage: 1:397/403 of query aligns to 1:402/412 of P00966
- V64 (≠ L65) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y88) binding L-citrulline
- T91 (≠ S92) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S93) binding L-citrulline
- R95 (= R96) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P97) 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 (= G118) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (= A119) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T120) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N124) binding L-aspartate; binding L-citrulline
- D124 (= D125) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R128) 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 (= R154) 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 (≠ E162) 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 (≠ R173) 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 (≠ F178) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S179) 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 (= S188) binding L-citrulline
- E191 (= E190) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G191) to V: in CTLN1; decreased protein abundance
- V263 (≠ I257) 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 (= R259) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E264) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R266) 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 (= G274) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y276) binding L-citrulline
- T284 (= T278) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L296) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R298) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G318) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G341) to R: in CTLN1; severe clinical course
- Y359 (≠ S353) to D: in CTLN1; mild clinical course
- G362 (≠ S356) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G385) to R: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908641
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
44% identity, 99% coverage: 4:403/403 of query aligns to 3:388/390 of 7k5zA
- active site: D15 (= D16), R95 (= R96), D124 (= D125), S176 (= S179)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (≠ S10), Y10 (= Y11), S11 (= S12), C37 (≠ A37), G117 (= G118), F128 (= F129)
- binding arginine: Y88 (= Y88), T92 (≠ S92), D124 (= D125), R127 (= R128), S185 (= S188), E187 (= E190), E261 (= E264), Y273 (= Y276)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
43% identity, 96% coverage: 5:392/403 of query aligns to 2:386/397 of 4xfjB
- active site: D13 (= D16), R94 (= R96), D123 (= D125), S174 (= S179)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (≠ S10), Y8 (= Y11), S9 (= S12), T14 (= T17), I34 (≠ A37), G116 (= G118), C117 (≠ A119), F127 (= F129)
- binding arginine: Y86 (= Y88), S90 (= S92), R126 (= R128), A183 (≠ S188), E185 (= E190), E259 (= E264), E269 (≠ G274), Y271 (= Y276)
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
31% identity, 92% coverage: 5:373/403 of query aligns to 11:390/438 of 6e5yA
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
31% identity, 92% coverage: 5:373/403 of query aligns to 15:394/445 of 5us8A
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
29% identity, 96% coverage: 5:392/403 of query aligns to 12:410/447 of P0A6E4
- 17:25 (vs. 10:18, 78% identical) binding ATP
- A43 (= A37) binding ATP
- Y99 (= Y88) binding L-citrulline
- G129 (= G118) binding ATP
- T131 (= T120) binding ATP; binding L-aspartate
- N135 (= N124) binding L-aspartate; binding L-citrulline
- D136 (= D125) binding ATP; binding L-aspartate
- R139 (= R128) binding L-citrulline
- S192 (= S179) binding L-citrulline
- D194 (= D181) binding ATP
- T201 (≠ S188) binding L-citrulline
- E203 (= E190) binding L-citrulline
- E280 (= E264) binding L-citrulline
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
30% identity, 90% coverage: 5:367/403 of query aligns to 11:390/432 of 1k97A
- active site: D22 (= D16), R106 (= R96), D135 (= D125), S191 (= S179)
- binding aspartic acid: S129 (≠ A119), T130 (= T120), G133 (= G123), N134 (= N124), D135 (= D125)
- binding citrulline: Y98 (= Y88), T102 (≠ S92), P103 (≠ S93), R138 (= R128), S191 (= S179), T192 (≠ I180), D193 (= D181), T200 (≠ S188), E202 (= E190), E279 (= E264), Y291 (= Y276), Y331 (= Y316)
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
30% identity, 91% coverage: 5:371/403 of query aligns to 11:388/439 of 1kp3A
- active site: D22 (= D16), R106 (= R96), D135 (= D125), S191 (= S179)
- binding adenosine-5'-triphosphate: A16 (≠ S10), S18 (= S12), G20 (= G14), D22 (= D16), T23 (= T17), T41 (= T36), A42 (= A37), D127 (≠ H117), G128 (= G118), S129 (≠ A119), F139 (= F129), D193 (= D181)
- binding citrulline: Y98 (= Y88), T102 (≠ S92), P103 (≠ S93), T130 (= T120), G133 (= G123), N134 (= N124), D135 (= D125), R138 (= R128), D193 (= D181), T200 (≠ S188), E202 (= E190), E202 (= E190), E279 (= E264), S287 (= S272), Y291 (= Y276)
Query Sequence
>WP_012757993.1 NCBI__GCF_000023185.1:WP_012757993.1
MTKIEKIVLSYSGGLDTSIILKWLQETYGCEVVTFTADLGQGEELEPARANAEMVGVKDI
RIVDLREEFVSDFVFPMLRANALYEGQYLLGSSIARPLIAKHLVGIAREVGADAVAHGAT
GKGNDQIRFELAVNALDPSIKVIAPWRQWNIRSRMQLLEYAEKHHIPVPSDKRGEAPFSI
DANLLHTSTEGKILENPAEVAPDHVYQRTVDPVDAPDTPEIVTIGFDWGDPVSVNGKSMT
PAALLTELNGLGGRHGIGRLDLVENRFIGMKSRGIYETPGGTILLTAHRGIESITLDRAA
AHLKDEIMPRYAELIYNGFWFAPEREMLQALIDHSQAFVSGEVTLRLYKGSASVISRASP
CSLYSADLVTFEESTIAFDHHDAEGFIRLNGLRLRSWVARNGR
Or try a new SitesBLAST search
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