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Comparing WP_072905980.1 NCBI__GCF_900142125.1:WP_072905980.1 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)
6cscA Chicken citrate synthase complex with trifluoroacetonyl-coa and citrate
50% identity, 99% coverage: 2:432/437 of query aligns to 4:432/437 of 6cscA
- active site: S244 (= S241), H274 (= H271), H320 (= H318), R329 (= R327), D375 (= D375)
- binding trifluoroacetonyl coenzyme a: R46 (= R44), L273 (= L270), H274 (= H271), A277 (= A274), V314 (= V312), V315 (≠ I313), G317 (= G315), Y318 (= Y316), G319 (= G317), H320 (= H318), A321 (= A319), K366 (= K366), A367 (= A367), K368 (= K368), N373 (= N373)
1cssA Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-coa as inhibitors of of citrate synthase: effect of pka matching on binding affinity and hydrogen bond length (see paper)
50% identity, 99% coverage: 2:432/437 of query aligns to 2:430/435 of 1cssA
- active site: S242 (= S241), H272 (= H271), H318 (= H318), R327 (= R327), D373 (= D375)
- binding alpha-fluoro-carboxymethyldethia coenzyme a complex: R44 (= R44), L271 (= L270), H272 (= H271), A275 (= A274), V312 (= V312), V313 (≠ I313), G315 (= G315), Y316 (= Y316), G317 (= G317), H318 (= H318), A319 (= A319), K364 (= K366), A365 (= A367), K366 (= K368), N371 (= N373), D373 (= D375)
- binding oxaloacetate ion: H236 (= H235), N240 (= N239), H318 (= H318), R327 (= R327), R399 (= R401)
1csrA Alpha-fluoro acid and alpha-fluoro amide analogs of acetyl-coa as inhibitors of of citrate synthase: effect of pka matching on binding affinity and hydrogen bond length (see paper)
50% identity, 99% coverage: 2:432/437 of query aligns to 2:430/435 of 1csrA
- active site: S242 (= S241), H272 (= H271), H318 (= H318), R327 (= R327), D373 (= D375)
- binding alpha-fluoro-amidocarboxymethyldethia coenzyme a complex: R44 (= R44), L271 (= L270), H272 (= H271), A275 (= A274), V312 (= V312), V313 (≠ I313), G315 (= G315), Y316 (= Y316), G317 (= G317), H318 (= H318), A319 (= A319), K364 (= K366), A365 (= A367), K366 (= K368), N371 (= N373), D373 (= D375), F395 (= F397)
- binding oxaloacetate ion: H236 (= H235), N240 (= N239), H272 (= H271), H318 (= H318), R327 (= R327), R399 (= R401)
1csiA A very short hydrogen bond provides only moderate stabilization of an enzyme: inhibitor complex of citrate synthase (see paper)
50% identity, 99% coverage: 2:432/437 of query aligns to 2:430/435 of 1csiA
- active site: S242 (= S241), H272 (= H271), H318 (= H318), R327 (= R327), D373 (= D375)
- binding carboxymethyldethia coenzyme *a: R44 (= R44), L271 (= L270), H272 (= H271), A275 (= A274), V312 (= V312), V313 (≠ I313), G315 (= G315), Y316 (= Y316), G317 (= G317), H318 (= H318), A319 (= A319), K364 (= K366), A365 (= A367), K366 (= K368), N371 (= N373), D373 (= D375)
- binding oxaloacetate ion: H236 (= H235), N240 (= N239), H272 (= H271), H318 (= H318), R327 (= R327), R399 (= R401)
1cshA A very short hydrogen bond provides only moderate stabilization of an enzyme: inhibitor complex of citrate synthase (see paper)
50% identity, 99% coverage: 2:432/437 of query aligns to 2:430/435 of 1cshA
- active site: S242 (= S241), H272 (= H271), H318 (= H318), R327 (= R327), D373 (= D375)
- binding amidocarboxymethyldethia coenzyme *a: R44 (= R44), L271 (= L270), H272 (= H271), A275 (= A274), V312 (= V312), V313 (≠ I313), G315 (= G315), Y316 (= Y316), G317 (= G317), H318 (= H318), A319 (= A319), K364 (= K366), A365 (= A367), K366 (= K368), N371 (= N373), D373 (= D375)
- binding oxaloacetate ion: H236 (= H235), N240 (= N239), H272 (= H271), H318 (= H318), R327 (= R327), R399 (= R401)
1amzA Chicken citrate synthase complex with nitromethylde-coa and malate
50% identity, 99% coverage: 2:432/437 of query aligns to 2:430/435 of 1amzA
- active site: S242 (= S241), H272 (= H271), H318 (= H318), R327 (= R327), D373 (= D375)
- binding nitromethyldethia coenzyme a: R44 (= R44), L271 (= L270), H272 (= H271), A275 (= A274), V312 (= V312), V313 (≠ I313), G315 (= G315), Y316 (= Y316), G317 (= G317), H318 (= H318), A319 (= A319), K364 (= K366), A365 (= A367), K366 (= K368), N371 (= N373), D373 (= D375)
1al6A Chicken citrate synthase complex with n-hydroxyamido-coa and oxaloacetate
50% identity, 99% coverage: 2:432/437 of query aligns to 2:430/435 of 1al6A
- active site: S242 (= S241), H272 (= H271), H318 (= H318), R327 (= R327), D373 (= D375)
- binding n-hydroxyamidocarboxymethyldethia coenzyme *a: R44 (= R44), L271 (= L270), H272 (= H271), G273 (= G272), A275 (= A274), V312 (= V312), V313 (≠ I313), G315 (= G315), Y316 (= Y316), G317 (= G317), H318 (= H318), A319 (= A319), K364 (= K366), A365 (= A367), K366 (= K368), N371 (= N373), D373 (= D375), F395 (= F397)
- binding oxaloacetate ion: H236 (= H235), N240 (= N239), H272 (= H271), H318 (= H318), R327 (= R327), R399 (= R401)
Q29RK1 Citrate synthase, mitochondrial; Citrate (Si)-synthase; EC 2.3.3.1 from Bos taurus (Bovine) (see paper)
49% identity, 97% coverage: 2:427/437 of query aligns to 31:454/466 of Q29RK1
- K76 (≠ R47) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
O75390 Citrate synthase, mitochondrial; Citrate (Si)-synthase; EC 2.3.3.1 from Homo sapiens (Human) (see 3 papers)
49% identity, 97% coverage: 2:427/437 of query aligns to 31:454/466 of O75390
- K393 (= K366) mutation to R: Does not inhibit methylation.
- K395 (= K368) modified: N6,N6,N6-trimethyllysine; mutation to R: Inhibits methylation.
Sites not aligning to the query:
P00889 Citrate synthase, mitochondrial; Citrate (Si)-synthase; EC 2.3.3.1 from Sus scrofa (Pig) (see paper)
50% identity, 97% coverage: 2:427/437 of query aligns to 31:454/464 of P00889
- K395 (= K368) modified: N6,N6,N6-trimethyllysine
Sites not aligning to the query:
- 1:27 modified: transit peptide, Mitochondrion
2ctsA Crystallographic refinement and atomic models of two different forms of citrate synthase at 2.7 and 1.7 angstroms resolution (see paper)
50% identity, 97% coverage: 2:427/437 of query aligns to 4:427/437 of 2ctsA
- active site: S244 (= S241), H274 (= H271), H320 (= H318), R329 (= R327), D375 (= D375)
- binding coenzyme a: R46 (= R44), P272 (= P269), A277 (= A274), E280 (= E277), V314 (= V312), V315 (≠ I313), P316 (= P314), G317 (= G315), Y318 (= Y316), A321 (= A319), K366 (= K366)
P00890 Citrate synthase, mitochondrial; EC 2.3.3.1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
50% identity, 98% coverage: 3:432/437 of query aligns to 44:470/479 of P00890
- S462 (= S424) modified: Phosphoserine; mutation to A: Loss of phosphorylation. Greatly increases catalytic activity and promotes homodimerization.; mutation to E: Phosphomimetic mutant. Inhibits catalytic activity and homodimerization.
3enjA Structure of pig heart citrate synthase at 1.78 a resolution (see paper)
50% identity, 97% coverage: 2:427/437 of query aligns to 4:427/437 of 3enjA
P08679 Citrate synthase, peroxisomal; EC 2.3.3.16 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 3 papers)
49% identity, 98% coverage: 3:432/437 of query aligns to 25:451/460 of P08679
- H293 (= H271) mutation to G: Prevents the stabilization of the enzyme by oxaloacetate and impairs the catalytic activity.
- G294 (= G272) mutation G->A,V: Leads to a decrease of the catalytic activity and the ubiquitination efficiency.
- H339 (= H318) mutation H->Q,N: Prevents the stabilization of the enzyme by oxaloacetate and impairs the catalytic activity.
- K354 (≠ E333) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
- K385 (= K366) modified: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Sites not aligning to the query:
- 458:460 C-terminal peroxisome targeting signal (PTS1)
8gr9A Crystal structure of peroxisomal citrate synthase (cit2) from saccharomyces cerevisiae in complex with oxaloacetate and coenzyme-a (see paper)
49% identity, 98% coverage: 3:432/437 of query aligns to 3:424/432 of 8gr9A
- binding coenzyme a: R44 (= R44), L270 (= L270), A274 (= A274), V306 (= V312), I307 (= I313), G309 (= G315), Y310 (= Y316), G311 (= G317), H312 (= H318), A313 (= A319), K358 (= K366), T359 (≠ A367), K360 (= K368), N365 (= N373)
- binding oxaloacetate ion: H235 (= H235), N239 (= N239), H271 (= H271), H312 (= H318), R321 (= R327), R393 (= R401)
6ctsA Proposed mechanism for the condensation reaction of citrate synthase. 1.9-angstroms structure of the ternary complex with oxaloacetate and carboxymethyl coenzyme a (see paper)
49% identity, 97% coverage: 2:427/437 of query aligns to 4:423/429 of 6ctsA
- active site: S243 (= S241), H273 (= H271), H316 (= H318), R325 (= R327), D371 (= D375)
- binding citryl-thioether-coenzyme *a: R46 (= R44), H237 (= H235), N241 (= N239), L272 (= L270), H273 (= H271), A276 (= A274), V310 (= V312), V311 (≠ I313), G313 (= G315), Y314 (= Y316), G315 (= G317), H316 (= H318), A317 (= A319), R325 (= R327), A362 (≠ K366), A363 (= A367), A364 (≠ K368), N369 (= N373), R397 (= R401)
3cscA Structure of ternary complexes of citrate synthase with d-and l- malate: mechanistic implications (see paper)
49% identity, 97% coverage: 2:427/437 of query aligns to 4:423/429 of 3cscA
- active site: S243 (= S241), H273 (= H271), H316 (= H318), R325 (= R327), D371 (= D375)
- binding acetyl coenzyme *a: R46 (= R44), L272 (= L270), H273 (= H271), V310 (= V312), V311 (≠ I313), G313 (= G315), Y314 (= Y316), G315 (= G317), H316 (= H318), A317 (= A319), A362 (≠ K366), A363 (= A367), A364 (≠ K368), N369 (= N373), D371 (= D375)
- binding (2S)-2-hydroxybutanedioic acid: H237 (= H235), N241 (= N239), H273 (= H271), H316 (= H318), R325 (= R327), R397 (= R401)
2cscA Structure of ternary complexes of citrate synthase with d-and l- malate: mechanistic implications (see paper)
49% identity, 97% coverage: 2:427/437 of query aligns to 4:423/429 of 2cscA
- active site: S243 (= S241), H273 (= H271), H316 (= H318), R325 (= R327), D371 (= D375)
- binding carboxymethyl coenzyme *a: R46 (= R44), L272 (= L270), H273 (= H271), G274 (= G272), A276 (= A274), V310 (= V312), V311 (≠ I313), G313 (= G315), Y314 (= Y316), G315 (= G317), H316 (= H318), A317 (= A319), A362 (≠ K366), A363 (= A367), A364 (≠ K368), N369 (= N373), D371 (= D375)
- binding d-malate: H237 (= H235), N241 (= N239), H273 (= H271), H316 (= H318), R325 (= R327), R397 (= R401)
1cscA Structure of ternary complexes of citrate synthase with d-and l- malate: mechanistic implications (see paper)
49% identity, 97% coverage: 2:427/437 of query aligns to 4:423/429 of 1cscA
- active site: S243 (= S241), H273 (= H271), H316 (= H318), R325 (= R327), D371 (= D375)
- binding carboxymethyl coenzyme *a: R46 (= R44), L272 (= L270), H273 (= H271), G274 (= G272), A276 (= A274), V310 (= V312), V311 (≠ I313), G313 (= G315), Y314 (= Y316), G315 (= G317), H316 (= H318), A317 (= A319), A362 (≠ K366), A363 (= A367), A364 (≠ K368), N369 (= N373), D371 (= D375)
- binding (2S)-2-hydroxybutanedioic acid: H237 (= H235), N241 (= N239), H273 (= H271), H316 (= H318), R325 (= R327), R397 (= R401)
5uquB Crystal structure of mutant 2-methylcitrate synthase (mcsag352a) from aspergillus fumigatus (see paper)
44% identity, 98% coverage: 6:432/437 of query aligns to 7:436/436 of 5uquB
- active site: S246 (= S241), H276 (= H271), H322 (= H318), R331 (= R327), D379 (= D375)
- binding coenzyme a: R45 (= R44), L275 (= L270), A279 (= A274), V316 (= V312), V317 (≠ I313), G319 (= G315), Y320 (= Y316), G321 (= G317), H322 (= H318), A323 (= A319), K370 (= K366), T371 (≠ A367), K372 (= K368), N377 (= N373)
Query Sequence
>WP_072905980.1 NCBI__GCF_900142125.1:WP_072905980.1
MSTLKETLFKKIQEHRPRTTKLVKECADVKLGDVTVGQAIGGARGVRCLVTDISYLDPME
GIRFRGMTIPETFAALPKVPGSEYPYVEGFWYLLLTGDVPTMEQTLEVVEDWKQRSAVPE
YVIDVLRALPRDSHPMAMFSAAIVAMQRESVFASNYAAGKFNKMTCWEDMYEDANTLMAR
LGPIGAYIYRMKYKGDTHIAPDPELDMGGQFAHMIGQSDEYKDVARMYFILHSDHESGNV
SAHTTHLVASALSDAYYAYSAGINGLAGPLHGLANEEVLRWTQNFMQKLGGEVPTEEGLK
EALWATLNSGQVIPGYGHAVLRKTDPRYTSQREFCMNTPGLKDYPLFQLVKMIFEVAPGV
LTEHGKAKNPWPNVDAQSGVIQWYYGVTEYEYYTVLFGIGRALGCLANITWDRALGYGIE
RPKSLTTAMLEEAAGIA
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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