SitesBLAST
Comparing WP_010960394.1 NCBI__GCF_000008325.1:WP_010960394.1 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)
65% identity, 96% coverage: 8:399/408 of query aligns to 2:389/400 of P59846
- 6:14 (vs. 12:20, 100% identical) binding ATP
- A33 (= A39) binding ATP
- G114 (= G120) binding ATP
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
64% identity, 96% coverage: 8:399/408 of query aligns to 2:380/386 of 1j20A
- active site: D12 (= D18), R92 (= R98), D121 (= D127), S168 (= S181)
- binding adenosine monophosphate: A6 (= A12), T13 (= T19), A33 (= A39), R92 (= R98), H113 (= H119), G114 (= G120), F125 (= F131)
- binding argininosuccinate: Y84 (= Y90), T88 (= T94), A115 (= A121), T116 (= T122), G119 (= G125), N120 (= N126), D121 (= D127), R124 (= R130), S177 (= S190), E179 (= E192), E253 (= E266), Y265 (= Y278)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
64% identity, 96% coverage: 8:399/408 of query aligns to 2:380/386 of 1j1zA
- active site: D12 (= D18), R92 (= R98), D121 (= D127), S168 (= S181)
- binding aspartic acid: A115 (= A121), T116 (= T122), G119 (= G125), N120 (= N126), D121 (= D127)
- binding adenosine-5'-triphosphate: A6 (= A12), T13 (= T19), A33 (= A39), R92 (= R98), I95 (= I101), H113 (= H119), G114 (= G120), F125 (= F131)
- binding citrulline: Y84 (= Y90), T88 (= T94), R124 (= R130), S168 (= S181), M169 (= M182), S177 (= S190), E179 (= E192), E253 (= E266), Y265 (= Y278)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
65% identity, 96% coverage: 8:399/408 of query aligns to 2:374/380 of 1kh3A
- active site: D12 (= D18), R92 (= R98), D121 (= D127), S168 (= S181)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A12), T13 (= T19), T32 (= T38), A33 (= A39), H113 (= H119), G114 (= G120), F125 (= F131), S168 (= S181), M169 (= M182)
- binding arginine: Y84 (= Y90), T88 (= T94), R124 (= R130), S168 (= S181), M169 (= M182), D170 (= D183), S177 (= S190), E179 (= E192), E253 (= E266), Y265 (= Y278)
- binding aspartic acid: A115 (= A121), T116 (= T122), G119 (= G125), N120 (= N126), D121 (= D127)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
46% identity, 96% coverage: 9:398/408 of query aligns to 7:400/412 of P00966
- V64 (≠ L67) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y90) binding L-citrulline
- T91 (= T94) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S95) binding L-citrulline
- R95 (= R98) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P99) 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 (= G120) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (= A121) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T122) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N126) binding L-aspartate; binding L-citrulline
- D124 (= D127) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R130) 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 (= R156) 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 (≠ E164) 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 (≠ T177) 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 (≠ Y180) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S181) 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 (= S190) binding L-citrulline
- E191 (= E192) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G193) to V: in CTLN1; decreased protein abundance
- V263 (≠ I259) 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 (= R261) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E266) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R268) 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 (= G276) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y278) binding L-citrulline
- T284 (= T280) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L298) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R300) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G320) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G343) to R: in CTLN1; severe clinical course
- Y359 (≠ S355) to D: in CTLN1; mild clinical course
- G362 (= G358) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G388) 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)
46% identity, 96% coverage: 9:398/408 of query aligns to 4:395/402 of 2nz2A
- active site: D13 (= D18), R92 (= R98), D121 (= D127), S176 (= S181)
- binding aspartic acid: A115 (= A121), T116 (= T122), G119 (= G125), N120 (= N126), D121 (= D127)
- binding citrulline: Y84 (= Y90), T88 (= T94), N120 (= N126), R124 (= R130), D178 (= D183), S185 (= S190), E187 (= E192), E266 (= E266), Y278 (= Y278)
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
43% identity, 97% coverage: 6:399/408 of query aligns to 3:379/390 of 7k5zA
- active site: D15 (= D18), R95 (= R98), D124 (= D127), S176 (= S181)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A12), Y10 (= Y13), S11 (= S14), C37 (≠ A39), G117 (= G120), F128 (= F131)
- binding arginine: Y88 (= Y90), T92 (= T94), D124 (= D127), R127 (= R130), S185 (= S190), E187 (= E192), E261 (= E266), Y273 (= Y278)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
41% identity, 97% coverage: 7:403/408 of query aligns to 2:394/397 of 4xfjB
- active site: D13 (= D18), R94 (= R98), D123 (= D127), S174 (= S181)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A12), Y8 (= Y13), S9 (= S14), T14 (= T19), I34 (≠ A39), G116 (= G120), C117 (≠ A121), F127 (= F131)
- binding arginine: Y86 (= Y90), S90 (≠ T94), R126 (= R130), A183 (≠ S190), E185 (= E192), E259 (= E266), E269 (≠ G276), Y271 (= Y278)
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
29% identity, 85% coverage: 7:353/408 of query aligns to 15:371/445 of 5us8A
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
29% identity, 85% coverage: 7:353/408 of query aligns to 11:367/438 of 6e5yA
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
26% identity, 96% coverage: 7:397/408 of query aligns to 11:404/439 of 1kp3A
- active site: D22 (= D18), R106 (= R98), D135 (= D127), S191 (= S181)
- binding adenosine-5'-triphosphate: A16 (= A12), S18 (= S14), G20 (= G16), D22 (= D18), T23 (= T19), T41 (= T38), A42 (= A39), D127 (≠ H119), G128 (= G120), S129 (≠ A121), F139 (= F131), D193 (= D183)
- binding citrulline: Y98 (= Y90), T102 (= T94), P103 (≠ S95), T130 (= T122), G133 (= G125), N134 (= N126), D135 (= D127), R138 (= R130), D193 (= D183), T200 (≠ S190), E202 (= E192), E202 (= E192), E279 (= E266), S287 (= S274), Y291 (= Y278)
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
27% identity, 88% coverage: 7:363/408 of query aligns to 11:378/432 of 1k97A
- active site: D22 (= D18), R106 (= R98), D135 (= D127), S191 (= S181)
- binding aspartic acid: S129 (≠ A121), T130 (= T122), G133 (= G125), N134 (= N126), D135 (= D127)
- binding citrulline: Y98 (= Y90), T102 (= T94), P103 (≠ S95), R138 (= R130), S191 (= S181), T192 (≠ M182), D193 (= D183), T200 (≠ S190), E202 (= E192), E279 (= E266), Y291 (= Y278), Y331 (= Y318)
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
27% identity, 88% coverage: 7:363/408 of query aligns to 12:379/447 of P0A6E4
- 17:25 (vs. 12:20, 89% identical) binding ATP
- A43 (= A39) binding ATP
- Y99 (= Y90) binding L-citrulline
- G129 (= G120) binding ATP
- T131 (= T122) binding ATP; binding L-aspartate
- N135 (= N126) binding L-aspartate; binding L-citrulline
- D136 (= D127) binding ATP; binding L-aspartate
- R139 (= R130) binding L-citrulline
- S192 (= S181) binding L-citrulline
- D194 (= D183) binding ATP
- T201 (≠ S190) binding L-citrulline
- E203 (= E192) binding L-citrulline
- E280 (= E266) binding L-citrulline
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_010960394.1 NCBI__GCF_000008325.1:WP_010960394.1
MSSSNVKKVALAYSGGLDTSVILKWLQETYGCEVVTFTADLGQGEEVEPARAKAQAMGVK
EIYIDDLREEFSRDFVFPMFRANAIYEGEYLLGTSIARPLIAKRLIEIANETGADAIAHG
ATGKGNDQVRFELGAYALRPDIRVIAPWREWELTSRETLLAYAESRGIPIEMKRGKTSPY
SMDANLLHISYEGGILEDPWAEPEETMWRWSVSPENAPDRPTYVELTYEHGDIVAIDGER
MTAAAVLARLNQLGGANGIGRLDIVENRYVGMKSRGCYETPGGTIMLKAHRAIESITLDR
EVAHLKDELMPRYASLIYNGYWWSPERRMLQQMIDASQATVNGVVRVKLYKGNVSVVGRK
SESNSLFDMNIATFEDDRGAYDQKDAEGFIKLNALRLRIAGRKGASFA
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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