SitesBLAST
Comparing WP_013684503.1 NCBI__GCF_000194625.1:WP_013684503.1 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)
52% identity, 98% coverage: 1:384/393 of query aligns to 1:389/400 of P59846
- 6:14 (vs. 6:14, 78% identical) binding ATP
- A33 (≠ V34) binding ATP
- G114 (= G113) binding ATP
7k5zA Crystal structure of argininosuccinate synthase from legionella pneumophila philadelphia 1 in complex with anppnp and a substrate analogue arginine
45% identity, 98% coverage: 2:388/393 of query aligns to 5:383/390 of 7k5zA
- active site: D15 (= D12), R95 (= R91), D124 (= D120), S176 (= S169)
- binding phosphoaminophosphonic acid-adenylate ester: A9 (≠ S6), Y10 (= Y7), S11 (= S8), C37 (≠ V34), G117 (= G113), F128 (= F124)
- binding arginine: Y88 (= Y83), T92 (= T87), D124 (= D120), R127 (= R123), S185 (= S178), E187 (= E180), E261 (= E254), Y273 (= Y266)
1j20A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with product (see paper)
51% identity, 98% coverage: 1:384/393 of query aligns to 1:380/386 of 1j20A
- active site: D12 (= D12), R92 (= R91), D121 (= D120), S168 (= S169)
- binding adenosine monophosphate: A6 (≠ S6), T13 (= T13), A33 (≠ V34), R92 (= R91), H113 (= H112), G114 (= G113), F125 (= F124)
- binding argininosuccinate: Y84 (vs. gap), T88 (= T87), A115 (≠ C114), T116 (= T115), G119 (= G118), N120 (= N119), D121 (= D120), R124 (= R123), S177 (= S178), E179 (= E180), E253 (= E254), Y265 (= Y266)
1j1zA Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with substrate (see paper)
51% identity, 98% coverage: 1:384/393 of query aligns to 1:380/386 of 1j1zA
- active site: D12 (= D12), R92 (= R91), D121 (= D120), S168 (= S169)
- binding aspartic acid: A115 (≠ C114), T116 (= T115), G119 (= G118), N120 (= N119), D121 (= D120)
- binding adenosine-5'-triphosphate: A6 (≠ S6), T13 (= T13), A33 (≠ V34), R92 (= R91), I95 (= I94), H113 (= H112), G114 (= G113), F125 (= F124)
- binding citrulline: Y84 (vs. gap), T88 (= T87), R124 (= R123), S168 (= S169), M169 (≠ I170), S177 (= S178), E179 (= E180), E253 (= E254), Y265 (= Y266)
1kh3A Crystal structure of thermus thermophilus hb8 argininosuccinate synthetase in complex with inhibitor (see paper)
49% identity, 98% coverage: 1:384/393 of query aligns to 1:374/380 of 1kh3A
- active site: D12 (= D12), R92 (= R91), D121 (= D120), S168 (= S169)
- binding phosphoaminophosphonic acid-adenylate ester: A6 (≠ S6), T13 (= T13), T32 (= T33), A33 (≠ V34), H113 (= H112), G114 (= G113), F125 (= F124), S168 (= S169), M169 (≠ I170)
- binding arginine: Y84 (vs. gap), T88 (= T87), R124 (= R123), S168 (= S169), M169 (≠ I170), D170 (= D171), S177 (= S178), E179 (= E180), E253 (= E254), Y265 (= Y266)
- binding aspartic acid: A115 (≠ C114), T116 (= T115), G119 (= G118), N120 (= N119), D121 (= D120)
4xfjB Crystal structure of argininosuccinate synthase from mycobacterium thermoresistibile in complex with amppnp and arginine
41% identity, 97% coverage: 2:384/393 of query aligns to 3:390/397 of 4xfjB
- active site: D13 (= D12), R94 (= R91), D123 (= D120), S174 (= S169)
- binding phosphoaminophosphonic acid-adenylate ester: A7 (≠ S6), Y8 (= Y7), S9 (= S8), T14 (= T13), I34 (≠ V34), G116 (= G113), C117 (= C114), F127 (= F124)
- binding arginine: Y86 (= Y83), S90 (≠ T87), R126 (= R123), A183 (≠ S178), E185 (= E180), E259 (= E254), E269 (= E264), Y271 (= Y266)
P00966 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Homo sapiens (Human) (see 16 papers)
42% identity, 99% coverage: 3:391/393 of query aligns to 7:408/412 of P00966
- V64 (≠ A62) to I: in CTLN1; uncertain significance; dbSNP:rs556297791
- Y87 (= Y83) binding L-citrulline
- T91 (= T87) to P: in CTLN1; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs769018733
- S92 (= S88) binding L-citrulline
- R95 (= R91) to S: in CTLN1; increased thermal stability; loss of argininosuccinate synthase activity
- P96 (= P92) 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 (= G113) to S: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity; dbSNP:rs770944877
- A118 (≠ C114) to T: in CTLN1; decreased thermal stability; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs775305020
- T119 (= T115) binding L-aspartate; to I: in CTLN1; decreased thermal stability; loss of argininosuccinate synthase activity
- N123 (= N119) binding L-aspartate; binding L-citrulline
- D124 (= D120) binding L-aspartate; to N: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs936192871
- R127 (= R123) 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 (= K154) 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 (≠ E165) 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 (≠ Y168) to R: in CTLN1; mild; decreased affinity for aspartate; decreased affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908646
- S180 (= S169) 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 (= S178) binding L-citrulline
- E191 (= E180) to Q: in CTLN1; loss of argininosuccinate synthase activity
- A192 (≠ G181) to V: in CTLN1; decreased protein abundance
- V263 (= V247) 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 (= R249) to C: in CTLN1; severe clinical course; loss of argininosuccinate synthase activity; dbSNP:rs148918985
- E270 (= E254) binding L-citrulline; to Q: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs775163147
- R272 (= R256) 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 (≠ E264) to R: in CTLN1; loss of argininosuccinate synthase activity
- Y282 (= Y266) binding L-citrulline
- T284 (≠ H268) to I: in CTLN1; mild clinical course; dbSNP:rs886039853
- M302 (≠ L286) to V: in CTLN1; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity
- R304 (= R288) to W: in CTLN1; decreased protein abundance; dbSNP:rs121908642
- G324 (= G308) to S: in CTLN1; loss of argininosuccinate synthase activity; dbSNP:rs121908639
- G347 (= G331) to R: in CTLN1; severe clinical course
- Y359 (≠ T343) to D: in CTLN1; mild clinical course
- G362 (≠ A346) to V: in CTLN1; mild; no effect on affinity for aspartate; no effect on affinity for citrulline; decreased argininosuccinate synthase activity; dbSNP:rs121908647
- G390 (= G373) 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)
42% identity, 98% coverage: 3:388/393 of query aligns to 4:400/402 of 2nz2A
- active site: D13 (= D12), R92 (= R91), D121 (= D120), S176 (= S169)
- binding aspartic acid: A115 (≠ C114), T116 (= T115), G119 (= G118), N120 (= N119), D121 (= D120)
- binding citrulline: Y84 (= Y83), T88 (= T87), N120 (= N119), R124 (= R123), D178 (= D171), S185 (= S178), E187 (= E180), E266 (= E254), Y278 (= Y266)
5us8A 2.15 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis
28% identity, 87% coverage: 2:341/393 of query aligns to 16:371/445 of 5us8A
6e5yA 1.50 angstrom resolution crystal structure of argininosuccinate synthase from bordetella pertussis in complex with amp.
28% identity, 87% coverage: 2:341/393 of query aligns to 12:367/438 of 6e5yA
1k97A Crystal structure of e. Coli argininosuccinate synthetase in complex with aspartate and citrulline (see paper)
28% identity, 91% coverage: 2:359/393 of query aligns to 12:386/432 of 1k97A
- active site: D22 (= D12), R106 (= R91), D135 (= D120), S191 (= S169)
- binding aspartic acid: S129 (≠ C114), T130 (= T115), G133 (= G118), N134 (= N119), D135 (= D120)
- binding citrulline: Y98 (= Y83), T102 (= T87), P103 (≠ S88), R138 (= R123), S191 (= S169), T192 (≠ I170), D193 (= D171), T200 (≠ S178), E202 (= E180), E279 (= E254), Y291 (= Y266), Y331 (= Y306)
1kp3A Crystal structure of e. Coli argininosuccinate synthetase in complex with atp and citrulline (see paper)
28% identity, 87% coverage: 2:341/393 of query aligns to 12:367/439 of 1kp3A
- active site: D22 (= D12), R106 (= R91), D135 (= D120), S191 (= S169)
- binding adenosine-5'-triphosphate: A16 (≠ S6), S18 (= S8), G20 (= G10), D22 (= D12), T23 (= T13), T41 (= T33), A42 (≠ V34), D127 (≠ H112), G128 (= G113), S129 (≠ C114), F139 (= F124), D193 (= D171)
- binding citrulline: Y98 (= Y83), T102 (= T87), P103 (≠ S88), T130 (= T115), G133 (= G118), N134 (= N119), D135 (= D120), R138 (= R123), D193 (= D171), T200 (≠ S178), E202 (= E180), E202 (= E180), E279 (= E254), S287 (≠ A262), Y291 (= Y266)
P0A6E4 Argininosuccinate synthase; Citrulline--aspartate ligase; EC 6.3.4.5 from Escherichia coli (strain K12) (see 4 papers)
28% identity, 87% coverage: 2:341/393 of query aligns to 13:368/447 of P0A6E4
- 17:25 (vs. 6:14, 67% identical) binding ATP
- A43 (≠ V34) binding ATP
- Y99 (= Y83) binding L-citrulline
- G129 (= G113) binding ATP
- T131 (= T115) binding ATP; binding L-aspartate
- N135 (= N119) binding L-aspartate; binding L-citrulline
- D136 (= D120) binding ATP; binding L-aspartate
- R139 (= R123) binding L-citrulline
- S192 (= S169) binding L-citrulline
- D194 (= D171) binding ATP
- T201 (≠ S178) binding L-citrulline
- E203 (= E180) binding L-citrulline
- E280 (= E254) binding L-citrulline
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
Query Sequence
>WP_013684503.1 NCBI__GCF_000194625.1:WP_013684503.1
MKVVLSYSGGLDTTVCIPLLKEKYGFDEVVTVTVDIGQPPEEIKEAEKRGKKYADKHYTI
DAKEEFVRLLFRLIKANGDYEGYVLGTSLARPLIAEKIVEVAKKENADAIAHGCTGKGND
QLRFENVFYQYGFRVIAPMRELNLTREWEIEYAKQHGIEVPVTKEKPYSIDENLWSRSIE
GGKLEDPSFEPPEDIFEWTASPAKAPDEPEKVEIYFEQGVPVAINGERLPGLELIRKLNE
IGGRHGVGRTDMMEDRVLGLKARENYEHPAATILITAHRDLEKLVLSRRELKFKKFVEEE
WAELVYYGLTNDPLFDALNAFIDETQKRVTGWVRLKLFKGSVTPVARYSEFALYREELVS
FDTTAIDQKYAEGFSRFHGLQGRIYREIIKKKE
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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