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Comparing WP_013840425.1 NCBI__GCF_000215085.1:WP_013840425.1 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)
60% identity, 99% coverage: 3:397/401 of query aligns to 2:396/400 of P59846
- 6:14 (vs. 7:15, 100% identical) binding
- A33 (= A34) binding
- G114 (= G115) binding
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
57% identity, 97% coverage: 1:390/401 of query aligns to 3:379/390 of 7k5zA
- active site: D15 (= D13), R95 (= R93), D124 (= D122), S176 (= S174)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (= A7), Y10 (= Y8), S11 (= S9), C37 (≠ A34), G117 (= G115), F128 (= F126)
- binding arginine: Y88 (= Y85), T92 (= T89), D124 (= D122), R127 (= R125), S185 (= S183), E187 (= E185), E261 (= E259), Y273 (= Y271)
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
59% identity, 98% coverage: 3:396/401 of query aligns to 2:386/386 of 1j20A
- active site: D12 (= D13), R92 (= R93), D121 (= D122), S168 (= S174)
- binding adenosine monophosphate: A6 (= A7), T13 (= T14), A33 (= A34), R92 (= R93), H113 (= H114), G114 (= G115), F125 (= F126)
- binding argininosuccinate: Y84 (= Y85), T88 (= T89), A115 (= A116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122), R124 (= R125), S177 (= S183), E179 (= E185), E253 (= E259), Y265 (= Y271)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
59% identity, 98% coverage: 3:396/401 of query aligns to 2:386/386 of 1j1zA
- active site: D12 (= D13), R92 (= R93), D121 (= D122), S168 (= S174)
- binding aspartic acid: A115 (= A116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122)
- binding adenosine-5'-triphosphate: A6 (= A7), T13 (= T14), A33 (= A34), R92 (= R93), I95 (= I96), H113 (= H114), G114 (= G115), F125 (= F126)
- binding citrulline: Y84 (= Y85), T88 (= T89), R124 (= R125), S168 (= S174), M169 (≠ R175), S177 (= S183), E179 (= E185), E253 (= E259), Y265 (= Y271)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
59% identity, 98% coverage: 3:396/401 of query aligns to 2:380/380 of 1kh3A
- active site: D12 (= D13), R92 (= R93), D121 (= D122), S168 (= S174)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (= A7), T13 (= T14), T32 (= T33), A33 (= A34), H113 (= H114), G114 (= G115), F125 (= F126), S168 (= S174), M169 (≠ R175)
- binding arginine: Y84 (= Y85), T88 (= T89), R124 (= R125), S168 (= S174), M169 (≠ R175), D170 (= D176), S177 (= S183), E179 (= E185), E253 (= E259), Y265 (= Y271)
- binding aspartic acid: A115 (= A116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
48% identity, 98% coverage: 4:397/401 of query aligns to 7:408/412 of P00966
- V64 (≠ L62) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y85) binding
- T91 (= T89) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S90) binding
- 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 (= A116) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T117) binding ; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N121) binding ; binding
- D124 (= D122) binding ; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R125) binding ; 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 (≠ E159) 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 (= K170) 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 ; 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 (= S183) binding
- E191 (= E185) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G186) to V: in CTLN1; decreased protein abundance
- V263 (≠ I252) 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 (≠ I254) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E259) binding ; 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 (= G269) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y271) binding
- T284 (= T273) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L291) 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 (≠ I348) 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
2nz2A Crystal structure of human argininosuccinate synthase in complex with aspartate and citrulline (see paper)
49% identity, 96% coverage: 4:389/401 of query aligns to 4:395/402 of 2nz2A
- active site: D13 (= D13), R92 (= R93), D121 (= D122), S176 (= S174)
- binding aspartic acid: A115 (= A116), T116 (= T117), G119 (= G120), N120 (= N121), D121 (= D122)
- binding citrulline: Y84 (= Y85), T88 (= T89), N120 (= N121), R124 (= R125), D178 (= D176), S185 (= S183), E187 (= E185), E266 (= E259), Y278 (= Y271)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
44% identity, 97% coverage: 3:392/401 of query aligns to 3:392/397 of 4xfjB
- active site: D13 (= D13), R94 (= R93), D123 (= D122), S174 (= S174)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (= A7), Y8 (= Y8), S9 (= S9), T14 (= T14), I34 (≠ A34), G116 (= G115), C117 (≠ A116), F127 (= F126)
- binding arginine: Y86 (= Y85), S90 (≠ T89), R126 (= R125), A183 (≠ S183), E185 (= E185), E259 (= E259), E269 (≠ G269), Y271 (= Y271)
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
32% identity, 91% coverage: 3:367/401 of query aligns to 12:380/438 of 6e5yA
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
32% identity, 91% coverage: 3:367/401 of query aligns to 16:384/445 of 5us8A
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
30% identity, 93% coverage: 3:374/401 of query aligns to 12:396/439 of 1kp3A
- active site: D22 (= D13), R106 (= R93), D135 (= D122), S191 (= S174)
- binding adenosine-5'-triphosphate: A16 (= A7), S18 (= S9), G20 (= G11), D22 (= D13), T23 (= T14), T41 (= T33), A42 (= A34), D127 (≠ H114), G128 (= G115), S129 (≠ A116), F139 (= F126), D193 (= D176)
- binding citrulline: Y98 (= Y85), T102 (= T89), P103 (≠ S90), T130 (= T117), G133 (= G120), N134 (= N121), D135 (= D122), R138 (= R125), D193 (= D176), T200 (≠ S183), E202 (= E185), E202 (= E185), E279 (= E259), S287 (= S267), Y291 (= Y271)
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
29% identity, 96% coverage: 3:388/401 of query aligns to 13:412/447 of P0A6E4
- 17:25 (vs. 7:15, 89% identical) binding
- A43 (= A34) binding
- Y99 (= Y85) binding
- G129 (= G115) binding
- T131 (= T117) binding ; binding
- N135 (= N121) binding ; binding
- D136 (= D122) binding ; binding
- R139 (= R125) binding
- S192 (= S174) binding
- D194 (= D176) binding
- T201 (≠ S183) binding
- E203 (= E185) binding
- E280 (= E259) binding
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)
30% identity, 93% coverage: 3:374/401 of query aligns to 12:395/432 of 1k97A
- active site: D22 (= D13), R106 (= R93), D135 (= D122), S191 (= S174)
- binding aspartic acid: S129 (≠ A116), T130 (= T117), G133 (= G120), N134 (= N121), D135 (= D122)
- binding citrulline: Y98 (= Y85), T102 (= T89), P103 (≠ S90), R138 (= R125), S191 (= S174), T192 (≠ R175), D193 (= D176), T200 (≠ S183), E202 (= E185), E279 (= E259), Y291 (= Y271), Y331 (= Y311)
Query Sequence
>WP_013840425.1 NCBI__GCF_000215085.1:WP_013840425.1
MPKVVLAYSGGLDTSVIIAWLKENYGYEVIAMTADLGQGEELAPLEEKAIQSGASKIYIE
DLRKEFVEEYVFPTLKAGAVYEGKYLLGTSFARPLIAKKLVEIAEKEGAVAVAHGATGKG
NDQVRFELGVKALAPHLKVIAPWREWDIRSREDAIDYAEARGIPVPVTKKSIYSRDRNIW
HISHEGGELESPANPASYDMLMLTVPPEKAPEQPTYVEIGFEQGIPVALNGEKTDSVSLL
EKLNEIGGANGIGIVDMVENRLVGMKSRGVYETPGGAILVYAHREMELLTLDRATLHYKE
QMALRYAELVYDGVWFSPLREALDAFVDSTQRTVTGTVKLKLYKGNIIPAGVTSPYSLYD
EELSTFSRDEVYNQADAEGFINLFGLPLKVRALMEKKAGLR
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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