Comparing WP_017178953.1 NCBI__GCF_000295095.1:WP_017178953.1 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)
59% identity, 92% coverage: 18:450/473 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)
48% identity, 90% coverage: 23:450/473 of query aligns to 1:426/426 of 2h12B
4tvmA Structure of citrate synthase from mycobacterium tuberculosis (see paper)
53% identity, 88% coverage: 34:447/473 of query aligns to 11:380/380 of 4tvmA
P0ABH7 Citrate synthase; EC 2.3.3.16 from Escherichia coli (strain K12) (see 2 papers)
50% identity, 91% coverage: 21:450/473 of query aligns to 2:427/427 of P0ABH7
4jagA Structural determination of the a50t:s279g:s280k:v281k:k282e:h283n variant of citrate synthase from e. Coli complexed with oxaloacetate (see paper)
49% identity, 91% coverage: 21:450/473 of query aligns to 1:426/426 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)
49% identity, 91% coverage: 21:450/473 of query aligns to 1:426/426 of 4jaeA
1owbA Three dimensional structure analysis of the variant r109l nadh complex of type ii citrate synthase from e. Coli (see paper)
49% identity, 91% coverage: 21:450/473 of query aligns to 1:426/426 of 1owbA
1nxgA The f383a variant of type ii citrate synthase complexed with nadh (see paper)
49% identity, 91% coverage: 21:450/473 of query aligns to 1:426/426 of 1nxgA
3msuB Crystal structure of citrate synthase from francisella tularensis
45% identity, 87% coverage: 33:444/473 of query aligns to 22:426/426 of 3msuB
3msuA Crystal structure of citrate synthase from francisella tularensis
44% identity, 87% coverage: 33:444/473 of query aligns to 22:415/415 of 3msuA
8bp7E Citrate-bound hexamer of synechococcus elongatus citrate synthase (see paper)
38% identity, 82% coverage: 64:450/473 of query aligns to 7:377/379 of 8bp7E
6abyA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with oxaloacetate (see paper)
38% identity, 82% coverage: 62:450/473 of query aligns to 3:370/372 of 6abyA
6abxA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with citrate (see paper)
38% identity, 82% coverage: 62:450/473 of query aligns to 3:370/370 of 6abxA
1aj8A Citrate synthase from pyrococcus furiosus (see paper)
36% identity, 82% coverage: 62:451/473 of query aligns to 1:371/371 of 1aj8A
6abwA Crystal structure of citrate synthase (msed_0281) from metallosphaera sedula in complex with acetyl-coa (see paper)
36% identity, 81% coverage: 68:450/473 of query aligns to 2:369/369 of 6abwA
1iomA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
36% identity, 82% coverage: 65:450/473 of query aligns to 4:374/374 of 1iomA
P39120 Citrate synthase 2; Citrate synthase II; EC 2.3.3.16 from Bacillus subtilis (strain 168) (see paper)
34% identity, 82% coverage: 65:450/473 of query aligns to 6:371/372 of P39120
1ixeA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
36% identity, 82% coverage: 65:450/473 of query aligns to 4:371/371 of 1ixeA
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)
34% identity, 81% coverage: 61:443/473 of query aligns to 5:377/379 of O34002
Sites not aligning to the query:
1a59A Cold-active citrate synthase (see paper)
34% identity, 81% coverage: 61:443/473 of query aligns to 3:375/377 of 1a59A
>WP_017178953.1 NCBI__GCF_000295095.1:WP_017178953.1
MTDTSPTMGPAAAEPQSLNDSDAVGVLTIEDRRLELPRAYATEGSDGLGVGKLLASTGMV
TLDPGFTNTASCTSEITYIDGGAGILRYCGYPIEELAKSSSFLEVAFLLINGELPDAETF
ERFERRIARHRLLHEDFRSFFTAFPSSGHPMAILQAGISGLATYYEDTLNPHDPYERELA
TVLLLSKMPTMISYIARRAIGLPLVYPDPKCGYVEDFLRLTFGMPYQAYEIDPAIVKALD
MLLILHADHEQNCSTSTVRLVGSADANMYASVAAGVGALSGPLHGGANEAVLRMLDTIQA
SGMTTAEFVRKVKNKEDGVRLMGFGHRVYKNYDPRAAIVKATAHDVLTRLGSDSGDRMLQ
IAMELEETALSDDYFVSRRLYPNVDFYTGLIYQAMGFPTKMFTPLFALGRLPGWIAQYRE
MISDPAKRIGRPRQVYTGATERHYVAIHRRKRSDAVYPGTRVGERALDHVNKV
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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