Comparing WP_078715671.1 NCBI__GCF_900167125.1:WP_078715671.1 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)
P9WPD5 Citrate synthase 1; EC 2.3.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
52% identity, 98% coverage: 1:429/437 of query aligns to 1:431/431 of P9WPD5
2h12B Structure of acetobacter aceti citrate synthase complexed with oxaloacetate and carboxymethyldethia coenzyme a (cmx) (see paper)
49% identity, 97% coverage: 6:429/437 of query aligns to 1:426/426 of 2h12B
4jagA Structural determination of the a50t:s279g:s280k:v281k:k282e:h283n variant of citrate synthase from e. Coli complexed with oxaloacetate (see paper)
47% identity, 95% coverage: 8:421/437 of query aligns to 5:418/426 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)
47% identity, 95% coverage: 8:421/437 of query aligns to 5:418/426 of 4jaeA
P0ABH7 Citrate synthase; EC 2.3.3.16 from Escherichia coli (strain K12) (see 2 papers)
46% identity, 96% coverage: 1:421/437 of query aligns to 1:419/427 of P0ABH7
1owbA Three dimensional structure analysis of the variant r109l nadh complex of type ii citrate synthase from e. Coli (see paper)
46% identity, 95% coverage: 8:421/437 of query aligns to 5:418/426 of 1owbA
1nxgA The f383a variant of type ii citrate synthase complexed with nadh (see paper)
46% identity, 95% coverage: 8:421/437 of query aligns to 5:418/426 of 1nxgA
4tvmA Structure of citrate synthase from mycobacterium tuberculosis (see paper)
45% identity, 96% coverage: 7:426/437 of query aligns to 1:380/380 of 4tvmA
3msuB Crystal structure of citrate synthase from francisella tularensis
44% identity, 95% coverage: 8:421/437 of query aligns to 12:424/426 of 3msuB
3msuA Crystal structure of citrate synthase from francisella tularensis
43% identity, 95% coverage: 8:421/437 of query aligns to 12:413/415 of 3msuA
8bp7E Citrate-bound hexamer of synechococcus elongatus citrate synthase (see paper)
36% identity, 88% coverage: 45:429/437 of query aligns to 5:377/379 of 8bp7E
6abyA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with oxaloacetate (see paper)
35% identity, 87% coverage: 48:429/437 of query aligns to 6:370/372 of 6abyA
6abxA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with citrate (see paper)
35% identity, 87% coverage: 48:429/437 of query aligns to 6:370/370 of 6abxA
1iomA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
35% identity, 86% coverage: 55:429/437 of query aligns to 11:374/374 of 1iomA
1ixeA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
34% identity, 86% coverage: 55:429/437 of query aligns to 11:371/371 of 1ixeA
6abwA Crystal structure of citrate synthase (msed_0281) from metallosphaera sedula in complex with acetyl-coa (see paper)
33% identity, 86% coverage: 56:429/437 of query aligns to 7:369/369 of 6abwA
1aj8A Citrate synthase from pyrococcus furiosus (see paper)
32% identity, 86% coverage: 56:430/437 of query aligns to 12:371/371 of 1aj8A
P39119 Citrate synthase 1; Citrate synthase I; EC 2.3.3.16 from Bacillus subtilis (strain 168) (see paper)
33% identity, 85% coverage: 48:418/437 of query aligns to 5:359/366 of P39119
2c6xA Structure of bacillus subtilis citrate synthase
33% identity, 85% coverage: 48:418/437 of query aligns to 4:358/363 of 2c6xA
P39120 Citrate synthase 2; Citrate synthase II; EC 2.3.3.16 from Bacillus subtilis (strain 168) (see paper)
33% identity, 89% coverage: 43:429/437 of query aligns to 1:371/372 of P39120
>WP_078715671.1 NCBI__GCF_900167125.1:WP_078715671.1
MSSTKNSATLTFDGKTIELPVVRGSEDEYGIDITRLRQDTGLITYDPGFGNTGSCSSSVT
FVNGEEGALHYRGYPIEEIAEHCSFIETAYLLIFGYLPTRDQLQHFSTLLTEQELLHEGL
RHHFDGFPSQGHPMAILSAVINSLGCYHPDLLELESKDQFLLAVSKIISKVRTIAAWAYR
KSIGRPFMYPNPSLSYCRNFLHMMFSIPNKIYDAPQEAVRALSLFFILHADHEQNCSCST
VRMVGSTQANLFASVSAGICALWGKLHGGANAAVIDMLTTIREQDIPVKEYIERVKNKEF
RLMGFGHRIYKNFDPRSQILRKAAYDLLEKTGNHDPLLDTAMELGEAALSDDYFLERKLY
PNVDFYSGIILRTLGIPVNMFPVMFAIGRMPGWVAHWYEDFQNPAMRIHRPRQIYTGARR
RPVVPMNKRKKPGEPAE
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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