SitesBLAST
Comparing WP_012972837.1 NCBI__GCF_000010725.1:WP_012972837.1 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)
62% identity, 97% coverage: 11:409/411 of query aligns to 2:396/400 of P59846
- 6:14 (vs. 15:23, 100% identical) binding ATP
- A33 (= A42) binding ATP
- G114 (= G125) binding ATP
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
62% identity, 97% coverage: 11:408/411 of query aligns to 2:386/386 of 1j20A
- active site: D12 (= D21), R92 (= R103), D121 (= D132), S168 (= S186)
- binding adenosine monophosphate: A6 (= A15), T13 (= T22), A33 (= A42), R92 (= R103), H113 (= H124), G114 (= G125), F125 (= F136)
- binding argininosuccinate: Y84 (= Y95), T88 (= T99), A115 (= A126), T116 (= T127), G119 (= G130), N120 (= N131), D121 (= D132), R124 (= R135), S177 (= S195), E179 (= E197), E253 (= E271), Y265 (= Y283)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
62% identity, 97% coverage: 11:408/411 of query aligns to 2:386/386 of 1j1zA
- active site: D12 (= D21), R92 (= R103), D121 (= D132), S168 (= S186)
- binding aspartic acid: A115 (= A126), T116 (= T127), G119 (= G130), N120 (= N131), D121 (= D132)
- binding adenosine-5'-triphosphate: A6 (= A15), T13 (= T22), A33 (= A42), R92 (= R103), I95 (= I106), H113 (= H124), G114 (= G125), F125 (= F136)
- binding citrulline: Y84 (= Y95), T88 (= T99), R124 (= R135), S168 (= S186), M169 (≠ T187), S177 (= S195), E179 (= E197), E253 (= E271), Y265 (= Y283)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
62% identity, 97% coverage: 11:408/411 of query aligns to 2:380/380 of 1kh3A
- active site: D12 (= D21), R92 (= R103), D121 (= D132), S168 (= S186)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A15), T13 (= T22), T32 (= T41), A33 (= A42), H113 (= H124), G114 (= G125), F125 (= F136), S168 (= S186), M169 (≠ T187)
- binding arginine: Y84 (= Y95), T88 (= T99), R124 (= R135), S168 (= S186), M169 (≠ T187), D170 (= D188), S177 (= S195), E179 (= E197), E253 (= E271), Y265 (= Y283)
- binding aspartic acid: A115 (= A126), T116 (= T127), G119 (= G130), N120 (= N131), D121 (= D132)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
48% identity, 95% coverage: 12:401/411 of query aligns to 7:400/412 of P00966
- V64 (≠ L72) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y95) binding L-citrulline
- T91 (= T99) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S100) binding L-citrulline
- R95 (= R103) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P104) 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 (= G125) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (= A126) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T127) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N131) binding L-aspartate; binding L-citrulline
- D124 (= D132) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R135) 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 (= R161) 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 (≠ E169) 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 (≠ R180) 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 (≠ Y185) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S186) 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 (= S195) binding L-citrulline
- E191 (= E197) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G198) to V: in CTLN1; decreased protein abundance
- V263 (≠ I264) 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 (= R266) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E271) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R273) 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 (= G281) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y283) binding L-citrulline
- T284 (= T285) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L303) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R305) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G325) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G348) to R: in CTLN1; severe clinical course
- Y359 (≠ T360) to D: in CTLN1; mild clinical course
- G362 (= G363) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G391) 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)
48% identity, 95% coverage: 12:401/411 of query aligns to 4:395/402 of 2nz2A
- active site: D13 (= D21), R92 (= R103), D121 (= D132), S176 (= S186)
- binding aspartic acid: A115 (= A126), T116 (= T127), G119 (= G130), N120 (= N131), D121 (= D132)
- binding citrulline: Y84 (= Y95), T88 (= T99), N120 (= N131), R124 (= R135), D178 (= D188), S185 (= S195), E187 (= E197), E266 (= E271), Y278 (= Y283)
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
44% identity, 98% coverage: 7:408/411 of query aligns to 1:385/390 of 7k5zA
- active site: D15 (= D21), R95 (= R103), D124 (= D132), S176 (= S186)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A15), Y10 (= Y16), S11 (= S17), C37 (≠ A42), G117 (= G125), F128 (= F136)
- binding arginine: Y88 (= Y95), T92 (= T99), D124 (= D132), R127 (= R135), S185 (= S195), E187 (= E197), E261 (= E271), Y273 (= Y283)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
41% identity, 96% coverage: 10:404/411 of query aligns to 2:392/397 of 4xfjB
- active site: D13 (= D21), R94 (= R103), D123 (= D132), S174 (= S186)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A15), Y8 (= Y16), S9 (= S17), T14 (= T22), I34 (≠ A42), G116 (= G125), C117 (≠ A126), F127 (= F136)
- binding arginine: Y86 (= Y95), S90 (≠ T99), R126 (= R135), A183 (≠ S195), E185 (= E197), E259 (= E271), E269 (≠ G281), Y271 (= Y283)
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
27% identity, 90% coverage: 10:380/411 of query aligns to 11:390/438 of 6e5yA
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
27% identity, 90% coverage: 10:380/411 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)
27% identity, 95% coverage: 10:400/411 of query aligns to 12:412/447 of P0A6E4
- 17:25 (vs. 15:23, 89% identical) binding ATP
- A43 (= A42) binding ATP
- Y99 (= Y95) binding L-citrulline
- G129 (= G125) binding ATP
- T131 (= T127) binding ATP; binding L-aspartate
- N135 (= N131) binding L-aspartate; binding L-citrulline
- D136 (= D132) binding ATP; binding L-aspartate
- R139 (= R135) binding L-citrulline
- S192 (= S186) binding L-citrulline
- D194 (= D188) binding ATP
- T201 (≠ S195) binding L-citrulline
- E203 (= E197) binding L-citrulline
- E280 (= E271) 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)
27% identity, 92% coverage: 10:386/411 of query aligns to 11:396/439 of 1kp3A
- active site: D22 (= D21), R106 (= R103), D135 (= D132), S191 (= S186)
- binding adenosine-5'-triphosphate: A16 (= A15), S18 (= S17), G20 (= G19), D22 (= D21), T23 (= T22), T41 (= T41), A42 (= A42), D127 (≠ H124), G128 (= G125), S129 (≠ A126), F139 (= F136), D193 (= D188)
- binding citrulline: Y98 (= Y95), T102 (= T99), P103 (≠ S100), T130 (= T127), G133 (= G130), N134 (= N131), D135 (= D132), R138 (= R135), D193 (= D188), T200 (≠ S195), E202 (= E197), E202 (= E197), E279 (= E271), S287 (= S279), Y291 (= Y283)
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
26% identity, 95% coverage: 10:400/411 of query aligns to 11:403/432 of 1k97A
- active site: D22 (= D21), R106 (= R103), D135 (= D132), S191 (= S186)
- binding aspartic acid: S129 (≠ A126), T130 (= T127), G133 (= G130), N134 (= N131), D135 (= D132)
- binding citrulline: Y98 (= Y95), T102 (= T99), P103 (≠ S100), R138 (= R135), S191 (= S186), T192 (= T187), D193 (= D188), T200 (≠ S195), E202 (= E197), E279 (= E271), Y291 (= Y283), Y331 (= Y323)
Query Sequence
>WP_012972837.1 NCBI__GCF_000010725.1:WP_012972837.1
MSGASGKQIKKVVLAYSGGLDTSVILKWLQETYSCEVVTFTADLGQGEELEPARKKAELL
GIKPENIFIDDLREEFVRDFVFPMFRANTLYEGTYLLGTSIARPLIAKRQIEIANMVGAD
AVAHGATGKGNDQVRFELGYYALRPDISVIAPWREWTLNSRTTLLDYAEKNQIPIAKDKR
GEAPYSTDANLLHISYEGKALEDPWVEPDEDMYTRSVAPEKAPDTPTYIEIEFKNGDAVA
IDGKALSPAALLTELNRLGGENGIGRLDLVENRYVGMKSRGVYETPGGSILLVAHRAMES
ITLDRGAGHLKDELMPRYAELIYCGYWWSPERLAIQALIDQTQSLVNGTVRLKLFKGNVT
VVGRKSPNSLYRMDYVTFEQDSVYNQKDAEGFIKLNALRLRLGAMAKQKLG
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