Comparing WP_018233113.1 NCBI__GCF_000378965.1:WP_018233113.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
1iomA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
43% identity, 98% coverage: 7:377/377 of query aligns to 1:374/374 of 1iomA
1ixeA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
43% identity, 98% coverage: 7:377/377 of query aligns to 1:371/371 of 1ixeA
8bp7E Citrate-bound hexamer of synechococcus elongatus citrate synthase (see paper)
43% identity, 98% coverage: 10:377/377 of query aligns to 8:377/379 of 8bp7E
P39120 Citrate synthase 2; Citrate synthase II; EC 2.3.3.16 from Bacillus subtilis (strain 168) (see paper)
42% identity, 98% coverage: 8:377/377 of query aligns to 4:371/372 of P39120
6abyA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with oxaloacetate (see paper)
39% identity, 99% coverage: 5:377/377 of query aligns to 1:370/372 of 6abyA
6abxA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with citrate (see paper)
39% identity, 99% coverage: 5:377/377 of query aligns to 1:370/370 of 6abxA
1aj8A Citrate synthase from pyrococcus furiosus (see paper)
38% identity, 98% coverage: 7:377/377 of query aligns to 1:370/371 of 1aj8A
I6Y9Q3 2-methylcitrate synthase; 2-MCS; MCS; Citrate synthase; EC 2.3.3.5; EC 2.3.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
39% identity, 96% coverage: 7:369/377 of query aligns to 28:387/393 of I6Y9Q3
P39119 Citrate synthase 1; Citrate synthase I; EC 2.3.3.16 from Bacillus subtilis (strain 168) (see paper)
38% identity, 95% coverage: 7:365/377 of query aligns to 2:358/366 of P39119
2c6xA Structure of bacillus subtilis citrate synthase
38% identity, 95% coverage: 7:365/377 of query aligns to 1:357/363 of 2c6xA
1a59A Cold-active citrate synthase (see paper)
37% identity, 96% coverage: 7:369/377 of query aligns to 4:374/377 of 1a59A
O34002 2-methylcitrate synthase; 2-MCS; MCS; Citrate synthase; EC 2.3.3.5; EC 2.3.3.16 from Antarctic bacterium DS2-3R (see 2 papers)
37% identity, 96% coverage: 7:369/377 of query aligns to 6:376/379 of O34002
Sites not aligning to the query:
6s87D Crystal structure of 2-methylcitrate synthase (prpc) from pseudomonas aeruginosa in complex with oxaloacetate.
36% identity, 98% coverage: 10:377/377 of query aligns to 1:365/365 of 6s87D
6abwA Crystal structure of citrate synthase (msed_0281) from metallosphaera sedula in complex with acetyl-coa (see paper)
34% identity, 97% coverage: 12:377/377 of query aligns to 1:369/369 of 6abwA
3msuA Crystal structure of citrate synthase from francisella tularensis
35% identity, 94% coverage: 18:371/377 of query aligns to 61:415/415 of 3msuA
2h12B Structure of acetobacter aceti citrate synthase complexed with oxaloacetate and carboxymethyldethia coenzyme a (cmx) (see paper)
35% identity, 95% coverage: 19:377/377 of query aligns to 52:426/426 of 2h12B
3msuB Crystal structure of citrate synthase from francisella tularensis
34% identity, 94% coverage: 19:371/377 of query aligns to 62:426/426 of 3msuB
4jagA Structural determination of the a50t:s279g:s280k:v281k:k282e:h283n variant of citrate synthase from e. Coli complexed with oxaloacetate (see paper)
34% identity, 95% coverage: 19:377/377 of query aligns to 54:426/426 of 4jagA
4jaeA Structural determination of the a50t:s279g:s280k:v281k:k282e:h283n variant of citrate synthase from e. Coli complexed with s- carboxymethyl-coa (see paper)
34% identity, 95% coverage: 19:377/377 of query aligns to 54:426/426 of 4jaeA
P0ABH7 Citrate synthase; EC 2.3.3.16 from Escherichia coli (strain K12) (see 2 papers)
34% identity, 95% coverage: 19:377/377 of query aligns to 55:427/427 of P0ABH7
>WP_018233113.1 NCBI__GCF_000378965.1:WP_018233113.1
MSDDVKINRGLKGIYFERSGVSHIDGTRGELLYRGYSIHDLATQSTFEEVAYLLIHGELP
TDKALSDFDARLKAARELPPQVHDIIAATKDGHPMDVLRTAVSALAALEPASREVSEEAF
IANGIRLTSQVPMIVAAHEAIRNGREPVAPDPEMGHAANWLWMLKGKKPSEDAARLADVD
FILHAEHGSNASSFAARVTIGTQANLHGAIVTALSTLAGPAHGGAAEDVMKMVQEIGSPE
KAADYVKAKRAAREPVMGFGHRVYRAEDPRARHLREGVRRLSEEMGSPEWYEILQAVVEA
MQPYSRHGLNVNVDFYSGVIYKLHGIPMDLYVPIFGIGRVPGWVVQCIEQLQSNILIRPL
TLYNGPEKRDYVPISKR
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory