SitesBLAST
Comparing WP_012852507.1 NCBI__GCF_000024385.1:WP_012852507.1 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)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
70% identity, 99% coverage: 2:395/400 of query aligns to 1:395/397 of 4xfjB
- active site: D13 (= D14), R94 (= R95), D123 (= D124), S174 (= S175)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A8), Y8 (= Y9), S9 (= S10), T14 (= T15), I34 (≠ V35), G116 (= G117), C117 (= C118), F127 (= F128)
- binding arginine: Y86 (= Y87), S90 (= S91), R126 (= R127), A183 (= A184), E185 (= E186), E259 (= E259), E269 (= E269), Y271 (= Y271)
P59846 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) (see 2 papers)
42% identity, 99% coverage: 4:400/400 of query aligns to 2:399/400 of P59846
- 6:14 (vs. 8:16, 100% identical) binding ATP
- A33 (≠ V35) binding ATP
- G114 (= G117) binding ATP
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
44% identity, 98% coverage: 1:390/400 of query aligns to 2:379/390 of 7k5zA
- active site: D15 (= D14), R95 (= R95), D124 (= D124), S176 (= S175)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A8), Y10 (= Y9), S11 (= S10), C37 (≠ V35), G117 (= G117), F128 (= F128)
- binding arginine: Y88 (= Y87), T92 (≠ A92), D124 (= D124), R127 (= R127), S185 (≠ A184), E187 (= E186), E261 (= E259), Y273 (= Y271)
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
42% identity, 98% coverage: 4:396/400 of query aligns to 2:386/386 of 1j20A
- active site: D12 (= D14), R92 (= R95), D121 (= D124), S168 (= S175)
- binding adenosine monophosphate: A6 (= A8), T13 (= T15), A33 (≠ V35), R92 (= R95), H113 (= H116), G114 (= G117), F125 (= F128)
- binding argininosuccinate: Y84 (= Y87), T88 (≠ S91), A115 (≠ C118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124), R124 (= R127), S177 (≠ A184), E179 (= E186), E253 (= E259), Y265 (= Y271)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
42% identity, 98% coverage: 4:396/400 of query aligns to 2:386/386 of 1j1zA
- active site: D12 (= D14), R92 (= R95), D121 (= D124), S168 (= S175)
- binding aspartic acid: A115 (≠ C118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124)
- binding adenosine-5'-triphosphate: A6 (= A8), T13 (= T15), A33 (≠ V35), R92 (= R95), I95 (= I98), H113 (= H116), G114 (= G117), F125 (= F128)
- binding citrulline: Y84 (= Y87), T88 (≠ S91), R124 (= R127), S168 (= S175), M169 (≠ I176), S177 (≠ A184), E179 (= E186), E253 (= E259), Y265 (= Y271)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
42% identity, 98% coverage: 4:396/400 of query aligns to 2:380/380 of 1kh3A
- active site: D12 (= D14), R92 (= R95), D121 (= D124), S168 (= S175)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A8), T13 (= T15), T32 (≠ A34), A33 (≠ V35), H113 (= H116), G114 (= G117), F125 (= F128), S168 (= S175), M169 (≠ I176)
- binding arginine: Y84 (= Y87), T88 (≠ S91), R124 (= R127), S168 (= S175), M169 (≠ I176), D170 (= D177), S177 (≠ A184), E179 (= E186), E253 (= E259), Y265 (= Y271)
- binding aspartic acid: A115 (≠ C118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124)
2nz2A Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline (see paper)
43% identity, 96% coverage: 5:386/400 of query aligns to 4:392/402 of 2nz2A
- active site: D13 (= D14), R92 (= R95), D121 (= D124), S176 (= S175)
- binding aspartic acid: A115 (≠ C118), T116 (= T119), G119 (= G122), N120 (= N123), D121 (= D124)
- binding citrulline: Y84 (= Y87), T88 (≠ S91), N120 (= N123), R124 (= R127), D178 (= D177), S185 (≠ A184), E187 (= E186), E266 (= E259), Y278 (= Y271)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
42% identity, 96% coverage: 5:386/400 of query aligns to 7:397/412 of P00966
- V64 (≠ A64) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y87) binding L-citrulline
- T91 (≠ S91) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (≠ A92) binding L-citrulline
- R95 (= R95) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P96) 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 (= G117) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (≠ C118) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T119) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N123) binding L-aspartate; binding L-citrulline
- D124 (= D124) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R127) 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 (= R152) 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 (≠ E160) 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 (= K171) 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 (≠ Y174) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S175) 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 (≠ A184) binding L-citrulline
- E191 (= E186) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ T187) to V: in CTLN1; decreased protein abundance
- V263 (= V252) 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 (= R254) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E259) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R261) 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 (≠ E269) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y271) binding L-citrulline
- T284 (≠ A273) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ V291) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R293) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G313) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G336) to R: in CTLN1; severe clinical course
- Y359 (≠ V348) to D: in CTLN1; mild clinical course
- G362 (= G351) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G379) to R: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908641
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
32% identity, 86% coverage: 3:345/400 of query aligns to 11:366/438 of 6e5yA
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
32% identity, 86% coverage: 3:345/400 of query aligns to 15:370/445 of 5us8A
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 92% coverage: 3:371/400 of query aligns to 12:394/447 of P0A6E4
- 17:25 (vs. 8:16, 89% identical) binding ATP
- A43 (≠ V35) binding ATP
- Y99 (= Y87) binding L-citrulline
- G129 (= G117) binding ATP
- T131 (= T119) binding ATP; binding L-aspartate
- N135 (= N123) binding L-aspartate; binding L-citrulline
- D136 (= D124) binding ATP; binding L-aspartate
- R139 (= R127) binding L-citrulline
- S192 (= S175) binding L-citrulline
- D194 (= D177) binding ATP
- T201 (≠ A184) binding L-citrulline
- E203 (= E186) binding L-citrulline
- E280 (= E259) 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)
29% identity, 86% coverage: 3:345/400 of query aligns to 11:366/439 of 1kp3A
- active site: D22 (= D14), R106 (= R95), D135 (= D124), S191 (= S175)
- binding adenosine-5'-triphosphate: A16 (= A8), S18 (= S10), G20 (= G12), D22 (= D14), T23 (= T15), T41 (≠ A34), A42 (≠ V35), D127 (≠ H116), G128 (= G117), S129 (≠ C118), F139 (= F128), D193 (= D177)
- binding citrulline: Y98 (= Y87), T102 (≠ S91), P103 (≠ A92), T130 (= T119), G133 (= G122), N134 (= N123), D135 (= D124), R138 (= R127), D193 (= D177), T200 (≠ A184), E202 (= E186), E202 (= E186), E279 (= E259), S287 (= S267), Y291 (= Y271)
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
29% identity, 86% coverage: 3:346/400 of query aligns to 11:367/432 of 1k97A
- active site: D22 (= D14), R106 (= R95), D135 (= D124), S191 (= S175)
- binding aspartic acid: S129 (≠ C118), T130 (= T119), G133 (= G122), N134 (= N123), D135 (= D124)
- binding citrulline: Y98 (= Y87), T102 (≠ S91), P103 (≠ A92), R138 (= R127), S191 (= S175), T192 (≠ I176), D193 (= D177), T200 (≠ A184), E202 (= E186), E279 (= E259), Y291 (= Y271), Y331 (= Y311)
Query Sequence
>WP_012852507.1 NCBI__GCF_000024385.1:WP_012852507.1
MTERVVLAYSGGLDTSVAIPYLAEQTGGEVIAVAVDVGQGGEDLEVIRKRALACGAVEAV
VVDAREEFASDFCVPALQANALYMDRYPLVSALSRPLIVKHLAAAAKEFGGTAVAHGCTG
KGNDQVRFEAGLAALNPDLKVIAPARDFAWTRDKAIEYAESKGLPIDVSAKSPYSIDQNL
WGRAVETGFLEDIWNAPIEDLYDYTSDPSAQRDPDEVVITFRAGVPVALDGRELTPLQII
EELNQRAGAQGVGRIDMVEDRLVGIKSREVYEAPAAIALITAHMELENVTVERDLARFKR
SVDQRWGELVYDGLWYSPLKRSLDAFIAESQKHVSGEIRMTLHGGRAVVTGRRSDASLYD
HDLATYDTGDTFDQSLAKGFVELWSLPSKIAAVRDRRVQG
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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