SitesBLAST
Comparing WP_012590417.1 NCBI__GCF_000021745.1:WP_012590417.1 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)
63% identity, 94% coverage: 10:402/416 of query aligns to 2:389/400 of P59846
- 6:14 (vs. 14:22, 100% identical) binding ATP
- A33 (= A41) binding ATP
- G114 (= G124) binding ATP
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
63% identity, 94% coverage: 10:402/416 of query aligns to 2:380/386 of 1j20A
- active site: D12 (= D20), R92 (= R102), D121 (= D131), S168 (= S185)
- binding adenosine monophosphate: A6 (= A14), T13 (= T21), A33 (= A41), R92 (= R102), H113 (= H123), G114 (= G124), F125 (= F135)
- binding argininosuccinate: Y84 (= Y94), T88 (= T98), A115 (= A125), T116 (= T126), G119 (= G129), N120 (= N130), D121 (= D131), R124 (= R134), S177 (= S194), E179 (= E196), E253 (= E270), Y265 (= Y282)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
63% identity, 94% coverage: 10:402/416 of query aligns to 2:380/386 of 1j1zA
- active site: D12 (= D20), R92 (= R102), D121 (= D131), S168 (= S185)
- binding aspartic acid: A115 (= A125), T116 (= T126), G119 (= G129), N120 (= N130), D121 (= D131)
- binding adenosine-5'-triphosphate: A6 (= A14), T13 (= T21), A33 (= A41), R92 (= R102), I95 (= I105), H113 (= H123), G114 (= G124), F125 (= F135)
- binding citrulline: Y84 (= Y94), T88 (= T98), R124 (= R134), S168 (= S185), M169 (≠ V186), S177 (= S194), E179 (= E196), E253 (= E270), Y265 (= Y282)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
62% identity, 94% coverage: 10:402/416 of query aligns to 2:374/380 of 1kh3A
- active site: D12 (= D20), R92 (= R102), D121 (= D131), S168 (= S185)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A14), T13 (= T21), T32 (= T40), A33 (= A41), H113 (= H123), G114 (= G124), F125 (= F135), S168 (= S185), M169 (≠ V186)
- binding arginine: Y84 (= Y94), T88 (= T98), R124 (= R134), S168 (= S185), M169 (≠ V186), D170 (= D187), S177 (= S194), E179 (= E196), E253 (= E270), Y265 (= Y282)
- binding aspartic acid: A115 (= A125), T116 (= T126), G119 (= G129), N120 (= N130), D121 (= D131)
2nz2A Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline (see paper)
51% identity, 94% coverage: 11:401/416 of query aligns to 4:395/402 of 2nz2A
- active site: D13 (= D20), R92 (= R102), D121 (= D131), S176 (= S185)
- binding aspartic acid: A115 (= A125), T116 (= T126), G119 (= G129), N120 (= N130), D121 (= D131)
- binding citrulline: Y84 (= Y94), T88 (= T98), N120 (= N130), R124 (= R134), D178 (= D187), S185 (= S194), E187 (= E196), E266 (= E270), Y278 (= Y282)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
49% identity, 99% coverage: 1:412/416 of query aligns to 1:411/412 of P00966
- V64 (≠ L71) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y94) binding L-citrulline
- T91 (= T98) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S99) binding L-citrulline
- R95 (= R102) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P103) 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 (= G124) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (= A125) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T126) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N130) binding L-aspartate; binding L-citrulline
- D124 (= D131) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R134) 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 (vs. gap) 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 (≠ E168) 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 (≠ R179) 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 (≠ F184) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S185) 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 (= S194) binding L-citrulline
- E191 (= E196) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G197) to V: in CTLN1; decreased protein abundance
- V263 (= V263) 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 (= R265) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E270) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R272) 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 (= G280) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y282) binding L-citrulline
- T284 (= T284) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L302) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R304) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G324) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G347) to R: in CTLN1; severe clinical course
- Y359 (≠ V359) to D: in CTLN1; mild clinical course
- G362 (= G362) 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
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
45% identity, 95% coverage: 8:401/416 of query aligns to 3:378/390 of 7k5zA
- active site: D15 (= D20), R95 (= R102), D124 (= D131), S176 (= S185)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A14), Y10 (= Y15), S11 (= S16), C37 (≠ A41), G117 (= G124), F128 (= F135)
- binding arginine: Y88 (= Y94), T92 (= T98), D124 (= D131), R127 (= R134), S185 (= S194), E187 (= E196), E261 (= E270), Y273 (= Y282)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
43% identity, 96% coverage: 9:406/416 of query aligns to 2:394/397 of 4xfjB
- active site: D13 (= D20), R94 (= R102), D123 (= D131), S174 (= S185)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A14), Y8 (= Y15), S9 (= S16), T14 (= T21), I34 (≠ A41), G116 (= G124), C117 (≠ A125), F127 (= F135)
- binding arginine: Y86 (= Y94), S90 (≠ T98), R126 (= R134), A183 (≠ S194), E185 (= E196), E259 (= E270), E269 (≠ G280), Y271 (= Y282)
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
29% identity, 84% coverage: 9:357/416 of query aligns to 11:367/438 of 6e5yA
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
29% identity, 84% coverage: 9:357/416 of query aligns to 15:371/445 of 5us8A
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 94% coverage: 9:398/416 of query aligns to 12:410/447 of P0A6E4
- 17:25 (vs. 14:22, 89% identical) binding ATP
- A43 (= A41) binding ATP
- Y99 (= Y94) binding L-citrulline
- G129 (= G124) binding ATP
- T131 (= T126) binding ATP; binding L-aspartate
- N135 (= N130) binding L-aspartate; binding L-citrulline
- D136 (= D131) binding ATP; binding L-aspartate
- R139 (= R134) binding L-citrulline
- S192 (= S185) binding L-citrulline
- D194 (= D187) binding ATP
- T201 (≠ S194) binding L-citrulline
- E203 (= E196) binding L-citrulline
- E280 (= E270) 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)
28% identity, 84% coverage: 9:357/416 of query aligns to 11:367/432 of 1k97A
- active site: D22 (= D20), R106 (= R102), D135 (= D131), S191 (= S185)
- binding aspartic acid: S129 (≠ A125), T130 (= T126), G133 (= G129), N134 (= N130), D135 (= D131)
- binding citrulline: Y98 (= Y94), T102 (= T98), P103 (≠ S99), R138 (= R134), S191 (= S185), T192 (≠ V186), D193 (= D187), T200 (≠ S194), E202 (= E196), E279 (= E270), Y291 (= Y282), Y331 (= Y322)
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
28% identity, 84% coverage: 9:357/416 of query aligns to 11:367/439 of 1kp3A
- active site: D22 (= D20), R106 (= R102), D135 (= D131), S191 (= S185)
- binding adenosine-5'-triphosphate: A16 (= A14), S18 (= S16), G20 (= G18), D22 (= D20), T23 (= T21), T41 (= T40), A42 (= A41), D127 (≠ H123), G128 (= G124), S129 (≠ A125), F139 (= F135), D193 (= D187)
- binding citrulline: Y98 (= Y94), T102 (= T98), P103 (≠ S99), T130 (= T126), G133 (= G129), N134 (= N130), D135 (= D131), R138 (= R134), D193 (= D187), T200 (≠ S194), E202 (= E196), E202 (= E196), E279 (= E270), S287 (= S278), Y291 (= Y282)
Query Sequence
>WP_012590417.1 NCBI__GCF_000021745.1:WP_012590417.1
MPSKQSDIKKVVLAYSGGLDTSIILKWLETTYGCEVVTFTADLGQGEEIEPARQKAILLG
VKPENIFIEDLREEFVRDYVFPMFRANAQYEGLYLLGTSIARPLIAKKQIEIAKKTGADA
VAHGATGKGNDQVRFELSYYALDPDIKVIAPWREWDLTSRTALIAFAEQHQIPIAKDKRG
DAPFSVDANLLHASSEGKVLEDPAEEVPDYVYSRTVNPEDAPDKPTYIEIDFERGDPVAI
DGEALSPANLLTRLNELARVNGVGRLDLVENRFVGMKSRGMYETPGGTILYVAHRGIESI
TLDRGAAHLKDELAPKYSELIYNGFWFSPEREMLQALIDKSQEFVAGRVRVKLYKGSAVV
VGRSSPYSLYDQDLVTFEEGAVAYDHRDAAGFIKLNALRLRTLGKRARKIAAAQKA
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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