Comparing HSERO_RS06380 FitnessBrowser__HerbieS:HSERO_RS06380 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)
P39120 Citrate synthase 2; Citrate synthase II; EC 2.3.3.16 from Bacillus subtilis (strain 168) (see paper)
30% identity, 73% coverage: 78:393/431 of query aligns to 15:363/372 of P39120
6abxA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with citrate (see paper)
28% identity, 73% coverage: 75:389/431 of query aligns to 12:358/370 of 6abxA
6abyA Crystal structure of citrate synthase (msed_1522) from metallosphaera sedula in complex with oxaloacetate (see paper)
28% identity, 73% coverage: 75:389/431 of query aligns to 12:358/372 of 6abyA
6abwA Crystal structure of citrate synthase (msed_0281) from metallosphaera sedula in complex with acetyl-coa (see paper)
29% identity, 74% coverage: 78:394/431 of query aligns to 8:362/369 of 6abwA
8glbD Selenomethionine derivatized citrate synthase (cita) in mycobacterium tuberculosis with pyruvate (see paper)
29% identity, 74% coverage: 84:403/431 of query aligns to 28:368/374 of 8glbD
8gmiA Citrate synthase (cita) in mycobacterium tuberculosis modified by ebselen at c143 residue (see paper)
29% identity, 74% coverage: 84:403/431 of query aligns to 27:367/369 of 8gmiA
8gi7A C143a variant of citrate synthase (cita) in mycobacterium tuberculosis (see paper)
28% identity, 74% coverage: 84:403/431 of query aligns to 25:365/368 of 8gi7A
1ixeA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
28% identity, 74% coverage: 72:389/431 of query aligns to 7:359/371 of 1ixeA
P39119 Citrate synthase 1; Citrate synthase I; EC 2.3.3.16 from Bacillus subtilis (strain 168) (see paper)
28% identity, 75% coverage: 72:394/431 of query aligns to 8:363/366 of P39119
2c6xA Structure of bacillus subtilis citrate synthase
28% identity, 75% coverage: 72:394/431 of query aligns to 7:362/363 of 2c6xA
1iomA Crystal structure of citrate synthase from thermus thermophilus hb8 (see paper)
28% identity, 74% coverage: 72:389/431 of query aligns to 7:362/374 of 1iomA
6s87D Crystal structure of 2-methylcitrate synthase (prpc) from pseudomonas aeruginosa in complex with oxaloacetate.
30% identity, 42% coverage: 211:389/431 of query aligns to 165:353/365 of 6s87D
1aj8A Citrate synthase from pyrococcus furiosus (see paper)
23% identity, 73% coverage: 77:389/431 of query aligns to 12:358/371 of 1aj8A
2r9eA The structure of the binary complex of citryl dethia coa and citrate synthase from the thermophilic archaeonthermoplasma acidophilum
33% identity, 41% coverage: 213:390/431 of query aligns to 175:370/381 of 2r9eA
2r26A The structure of the ternary complex of carboxymethyl coenzyme a and oxalateacetate with citrate synthase from the thermophilic archaeonthermoplasma acidophilum
33% identity, 41% coverage: 213:390/431 of query aligns to 175:370/381 of 2r26A
4yboB Structure of citrate synthase from the thermoacidophilic euryarchaeon thermolasma acidophilum (see paper)
33% identity, 41% coverage: 213:390/431 of query aligns to 174:369/381 of 4yboB
P9WPD5 Citrate synthase 1; EC 2.3.3.16 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
29% identity, 74% coverage: 77:394/431 of query aligns to 56:424/431 of P9WPD5
2ifcC The structure of the binary complex of oxalateacetate with citrate synthase from the thermophilic archaeon thermolasma acidophilum
33% identity, 41% coverage: 213:390/431 of query aligns to 175:370/382 of 2ifcC
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)
29% identity, 42% coverage: 211:391/431 of query aligns to 175:374/379 of O34002
Sites not aligning to the query:
1a59A Cold-active citrate synthase (see paper)
29% identity, 42% coverage: 211:391/431 of query aligns to 173:372/377 of 1a59A
>HSERO_RS06380 FitnessBrowser__HerbieS:HSERO_RS06380
MSNYLNSTEAAARLGVSRQTLYAYVSRGLLHAEPGATARESRYFAADVERVAAQRAHGRK
PKEVAKAALNWGAPVLESSITLIDGGRLFYRGVDALSLAEHASLEEVAAGLWQCDRRTAF
GPHGAASPAVLRALFRHYGDQRAEEVLLPLFAVASDDASTAIWQKAVERQAQGCGDLVRI
LAACLLRTRPDTSPIHVQCARAWGVGRAGGELIRMALVLCADHELNASSFTSRCVASTDA
SLRAVVIAGLAGLSGGRHGATTGRVEALWDELGTRDVDRKMRERLSRGDDLPGFGHTLYP
DGDPRASYLLSQILPRHSPWAAMIDAGITLTGQKPSVDFALVALRRHLRLPVGAAFGLFA
LGRSIGWIAHGLEQREQHHLIRPRAVYIGPQPEDGQAEPGRPRSRARSAGRQTQQGSVPK
GDLPAGFFKTR
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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