SitesBLAST
Comparing WP_012676091.1 NCBI__GCF_000021565.1:WP_012676091.1 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)
53% identity, 98% coverage: 4:394/399 of query aligns to 2:391/400 of P59846
- 6:14 (vs. 8:16, 100% identical) binding ATP
- A33 (= A34) binding ATP
- G114 (= G115) binding ATP
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
52% identity, 98% coverage: 4:394/399 of query aligns to 2:382/386 of 1j20A
- active site: D12 (= D14), R92 (= R93), D121 (= D122), S168 (= S174)
- binding adenosine monophosphate: A6 (= A8), T13 (= T15), A33 (= A34), R92 (= R93), H113 (= H114), G114 (= G115), F125 (= F126)
- binding argininosuccinate: Y84 (= Y85), T88 (≠ S89), A115 (≠ S116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122), R124 (= R125), S177 (≠ A183), E179 (= E185), E253 (= E260), Y265 (= Y272)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
52% identity, 98% coverage: 4:394/399 of query aligns to 2:382/386 of 1j1zA
- active site: D12 (= D14), R92 (= R93), D121 (= D122), S168 (= S174)
- binding aspartic acid: A115 (≠ S116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122)
- binding adenosine-5'-triphosphate: A6 (= A8), T13 (= T15), A33 (= A34), R92 (= R93), I95 (= I96), H113 (= H114), G114 (= G115), F125 (= F126)
- binding citrulline: Y84 (= Y85), T88 (≠ S89), R124 (= R125), S168 (= S174), M169 (≠ Y175), S177 (≠ A183), E179 (= E185), E253 (= E260), Y265 (= Y272)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
52% identity, 98% coverage: 4:394/399 of query aligns to 2:376/380 of 1kh3A
- active site: D12 (= D14), R92 (= R93), D121 (= D122), S168 (= S174)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A8), T13 (= T15), T32 (= T33), A33 (= A34), H113 (= H114), G114 (= G115), F125 (= F126), S168 (= S174), M169 (≠ Y175)
- binding arginine: Y84 (= Y85), T88 (≠ S89), R124 (= R125), S168 (= S174), M169 (≠ Y175), D170 (= D176), S177 (≠ A183), E179 (= E185), E253 (= E260), Y265 (= Y272)
- binding aspartic acid: A115 (≠ S116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
46% identity, 99% coverage: 2:395/399 of query aligns to 1:393/397 of 4xfjB
- active site: D13 (= D14), R94 (= R93), D123 (= D122), S174 (= S174)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A8), Y8 (= Y9), S9 (= S10), T14 (= T15), I34 (≠ A34), G116 (= G115), C117 (≠ S116), F127 (= F126)
- binding arginine: Y86 (= Y85), S90 (= S89), R126 (= R125), A183 (= A183), E185 (= E185), E259 (= E260), E269 (= E270), Y271 (= Y272)
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
46% identity, 99% coverage: 3:398/399 of query aligns to 4:385/390 of 7k5zA
- active site: D15 (= D14), R95 (= R93), D124 (= D122), S176 (= S174)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A8), Y10 (= Y9), S11 (= S10), C37 (≠ A34), G117 (= G115), F128 (= F126)
- binding arginine: Y88 (= Y85), T92 (≠ A90), D124 (= D122), R127 (= R125), S185 (≠ A183), E187 (= E185), E261 (= E260), Y273 (= Y272)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
43% identity, 100% coverage: 2:399/399 of query aligns to 4:408/412 of P00966
- V64 (≠ I62) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y85) binding L-citrulline
- T91 (≠ S89) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (≠ A90) binding L-citrulline
- R95 (= R93) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P94) 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 (= G115) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (≠ S116) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T117) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N121) binding L-aspartate; binding L-citrulline
- D124 (= D122) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R125) 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 (= R151) 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 (≠ L159) 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 (≠ E170) 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 (≠ Y173) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S174) 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 (≠ A183) binding L-citrulline
- E191 (= E185) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (= A186) to V: in CTLN1; decreased protein abundance
- V263 (= V253) 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 (= R255) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E260) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R262) 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 (≠ E270) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y272) binding L-citrulline
- T284 (≠ S274) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L292) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R294) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G315) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G338) to R: in CTLN1; severe clinical course
- Y359 (≠ Q350) to D: in CTLN1; mild clinical course
- G362 (= G353) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (≠ M381) 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)
44% identity, 99% coverage: 2:395/399 of query aligns to 1:399/402 of 2nz2A
- active site: D13 (= D14), R92 (= R93), D121 (= D122), S176 (= S174)
- binding aspartic acid: A115 (≠ S116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122)
- binding citrulline: Y84 (= Y85), T88 (≠ S89), N120 (= N121), R124 (= R125), D178 (= D176), S185 (≠ A183), E187 (= E185), E266 (= E260), Y278 (= Y272)
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
30% identity, 93% coverage: 3:374/399 of query aligns to 11:394/439 of 1kp3A
- active site: D22 (= D14), R106 (= R93), D135 (= D122), S191 (= S174)
- binding adenosine-5'-triphosphate: A16 (= A8), S18 (= S10), G20 (= G12), D22 (= D14), T23 (= T15), T41 (= T33), A42 (= A34), D127 (≠ H114), G128 (= G115), S129 (= S116), F139 (= F126), D193 (= D176)
- binding citrulline: Y98 (= Y85), T102 (≠ S89), P103 (≠ A90), T130 (= T117), G133 (= G120), N134 (= N121), D135 (= D122), R138 (= R125), D193 (= D176), T200 (≠ A183), E202 (= E185), E202 (= E185), E279 (= E260), S287 (= S268), Y291 (= Y272)
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
29% identity, 93% coverage: 3:374/399 of query aligns to 11:393/432 of 1k97A
- active site: D22 (= D14), R106 (= R93), D135 (= D122), S191 (= S174)
- binding aspartic acid: S129 (= S116), T130 (= T117), G133 (= G120), N134 (= N121), D135 (= D122)
- binding citrulline: Y98 (= Y85), T102 (≠ S89), P103 (≠ A90), R138 (= R125), S191 (= S174), T192 (≠ Y175), D193 (= D176), T200 (≠ A183), E202 (= E185), E279 (= E260), Y291 (= Y272), Y331 (= Y313)
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
30% identity, 95% coverage: 3:383/399 of query aligns to 12:397/447 of P0A6E4
- 17:25 (vs. 8:16, 89% identical) binding ATP
- A43 (= A34) binding ATP
- Y99 (= Y85) binding L-citrulline
- G129 (= G115) binding ATP
- T131 (= T117) binding ATP; binding L-aspartate
- N135 (= N121) binding L-aspartate; binding L-citrulline
- D136 (= D122) binding ATP; binding L-aspartate
- R139 (= R125) binding L-citrulline
- S192 (= S174) binding L-citrulline
- D194 (= D176) binding ATP
- T201 (≠ A183) binding L-citrulline
- E203 (= E185) binding L-citrulline
- E280 (= E260) binding L-citrulline
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
30% identity, 92% coverage: 3:371/399 of query aligns to 15:388/445 of 5us8A
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
30% identity, 92% coverage: 3:371/399 of query aligns to 11:384/438 of 6e5yA
Query Sequence
>WP_012676091.1 NCBI__GCF_000021565.1:WP_012676091.1
MKKRVVLAYSGGLDTSVIVRWLTDKGFEVITYTADVGQGEELDEIEEKAKASGAVEAIID
DIKEEFAREYCMPLMRSGALYEGRYTLLSALSRPLISKKLVELAHRYDAHYVAHGSTGKG
NDQVRFESSVWALDPDIEVLAPVRDWEFKSREEEIEYALKHGIPVKATKEKPYSYDRNLW
GVAIEAGPLEDIWAEPPEDAFEITVNPENAPDSPEYLEIQFEKGVPVAINGKRYDQLWKL
IWDLNEIAGKHGVGRIDMVENRLVGIKSREVYESPAGIILIKAYDEIESLVLDRFTYHYK
LTHISQPYADLVYNGLWFSKLREALDAFTSEIAQLVNGTVRFKLYKGNAQIVGRKSPNGL
YFETLATYSPEDEFDHKAGEMFTKIWGLPLKVFAKANKR
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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