SitesBLAST
Comparing WP_068459766.1 NCBI__GCF_001541235.1:WP_068459766.1 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)
A0QX20 Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; Iron-responsive protein-like; IRP-like; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
56% identity, 99% coverage: 8:902/905 of query aligns to 10:938/943 of A0QX20
- K394 (≠ T404) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
P09339 Aconitate hydratase A; ACN; Aconitase; Aconitate/2-methylaconitate hydratase; Iron-responsive protein-like; IRP-like; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.- from Bacillus subtilis (strain 168) (see 2 papers)
55% identity, 98% coverage: 10:900/905 of query aligns to 11:903/909 of P09339
- C450 (= C442) mutation to S: Loss of aconitase activity. It is glutamate auxotroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of inactive aconitase.
- R741 (= R733) mutation to E: Same aconitase activity compared to the wild-type. It is glutamate prototroph and accumulates citrate. Exhibits overexpression of the citB promoter and accumulates high levels of active aconitase.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
D9X0I3 Aconitate hydratase A; ACN; Aconitase; EC 4.2.1.3 from Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) (see paper)
56% identity, 99% coverage: 7:902/905 of query aligns to 1:928/931 of D9X0I3
- SVIAD 125:129 (≠ SVIVD 137:141) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C508) mutation to A: Loss of aconitase activity. Cannot rescue the growth defect of a disruption mutant and results in only a slight increase in PTT production in the mutant. Shows weak IRE-binding activity.
- R763 (= R733) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ F737) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
Q9SIB9 Aconitate hydratase 3, mitochondrial; Aconitase 3; mACO1; Citrate hydro-lyase 3; EC 4.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
54% identity, 98% coverage: 21:903/905 of query aligns to 111:988/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
51% identity, 95% coverage: 43:903/905 of query aligns to 33:887/888 of 2b3xA
- active site: D124 (= D135), H125 (= H136), D204 (= D220), R535 (= R541), S777 (= S789), R779 (= R791)
- binding iron/sulfur cluster: I175 (= I186), H206 (= H222), C436 (= C442), C502 (= C508), C505 (= C511), I506 (= I512), N534 (= N540)
P21399 Cytoplasmic aconitate hydratase; Aconitase; Citrate hydro-lyase; Ferritin repressor protein; Iron regulatory protein 1; IRP1; Iron-responsive element-binding protein 1; IRE-BP 1; EC 4.2.1.3 from Homo sapiens (Human) (see 2 papers)
51% identity, 95% coverage: 43:903/905 of query aligns to 34:888/889 of P21399
- C300 (≠ A315) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ N333) to M: in dbSNP:rs150373174
- C437 (= C442) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C508) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C511) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R541) mutation to Q: Strongly reduced RNA binding.
- R541 (= R546) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H704) mutation to K: No effect on RNA binding.
- S778 (= S789) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R791) mutation to Q: Nearly abolishes RNA binding.
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
49% identity, 95% coverage: 43:903/905 of query aligns to 33:849/850 of 3snpA
- active site: D124 (= D135), H125 (= H136), D186 (= D220), R505 (= R541), S739 (= S789), R741 (= R791)
- binding : H125 (= H136), S126 (= S137), H188 (= H222), L243 (= L277), R250 (= R284), N279 (= N313), E283 (= E317), S352 (≠ A384), P357 (= P389), K360 (≠ R392), T419 (= T443), N420 (= N444), T421 (= T445), N504 (= N540), R505 (= R541), L520 (= L556), S642 (= S686), P643 (= P687), A644 (= A688), G645 (= G689), N646 (≠ S690), R649 (≠ P693), R665 (≠ A709), S669 (≠ Q713), G671 (= G715), R674 (= R718), R741 (= R791)
P19414 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see 2 papers)
27% identity, 90% coverage: 86:898/905 of query aligns to 85:772/778 of P19414
- R604 (= R726) mutation to K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.
Sites not aligning to the query:
- 1:16 modified: transit peptide, Mitochondrion
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 93% coverage: 54:896/905 of query aligns to 53:773/780 of P20004
- Q99 (= Q96) binding substrate
- DSH 192:194 (= DSH 220:222) binding substrate
- C385 (= C442) binding [4Fe-4S] cluster
- C448 (= C508) binding [4Fe-4S] cluster
- C451 (= C511) binding [4Fe-4S] cluster
- R474 (= R541) binding substrate
- R479 (= R546) binding substrate
- R607 (= R726) binding substrate
- SR 670:671 (= SR 790:791) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 89% coverage: 88:896/905 of query aligns to 63:745/753 of 8acnA
- active site: D99 (= D135), H100 (= H136), D164 (= D220), R446 (= R541), S641 (= S789), R643 (= R791)
- binding nitroisocitric acid: Q71 (= Q96), T74 (= T99), H100 (= H136), D164 (= D220), S165 (= S221), R446 (= R541), R451 (= R546), R579 (= R726), S641 (= S789), S642 (= S790), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H136), D164 (= D220), H166 (= H222), S356 (= S441), C357 (= C442), C420 (= C508), C423 (= C511), I424 (= I512)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 89% coverage: 88:896/905 of query aligns to 63:745/753 of 1fghA
- active site: D99 (= D135), H100 (= H136), D164 (= D220), R446 (= R541), S641 (= S789), R643 (= R791)
- binding 4-hydroxy-aconitate ion: Q71 (= Q96), T74 (= T99), H100 (= H136), D164 (= D220), S165 (= S221), R446 (= R541), R451 (= R546), R579 (= R726), S641 (= S789), S642 (= S790), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H136), D164 (= D220), H166 (= H222), S356 (= S441), C357 (= C442), C420 (= C508), C423 (= C511), I424 (= I512), R451 (= R546)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 89% coverage: 88:896/905 of query aligns to 63:745/753 of 1amjA
- active site: D99 (= D135), H100 (= H136), D164 (= D220), R446 (= R541), S641 (= S789), R643 (= R791)
- binding iron/sulfur cluster: I144 (= I186), H166 (= H222), C357 (= C442), C420 (= C508), C423 (= C511)
- binding sulfate ion: Q71 (= Q96), R579 (= R726), R643 (= R791)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 89% coverage: 88:896/905 of query aligns to 63:745/753 of 1amiA
- active site: D99 (= D135), H100 (= H136), D164 (= D220), R446 (= R541), S641 (= S789), R643 (= R791)
- binding alpha-methylisocitric acid: Q71 (= Q96), T74 (= T99), H100 (= H136), D164 (= D220), S165 (= S221), R446 (= R541), R451 (= R546), R579 (= R726), S641 (= S789), S642 (= S790), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H136), I144 (= I186), D164 (= D220), H166 (= H222), S356 (= S441), C357 (= C442), C420 (= C508), C423 (= C511), N445 (= N540)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 89% coverage: 88:896/905 of query aligns to 63:745/753 of 1acoA
- active site: D99 (= D135), H100 (= H136), D164 (= D220), R446 (= R541), S641 (= S789), R643 (= R791)
- binding iron/sulfur cluster: H100 (= H136), I144 (= I186), D164 (= D220), H166 (= H222), S356 (= S441), C357 (= C442), C420 (= C508), C423 (= C511), N445 (= N540)
- binding aconitate ion: Q71 (= Q96), D164 (= D220), S165 (= S221), R446 (= R541), R451 (= R546), R579 (= R726), S641 (= S789), S642 (= S790), R643 (= R791)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 89% coverage: 88:896/905 of query aligns to 63:745/753 of 1nisA
- active site: D99 (= D135), H100 (= H136), D164 (= D220), R446 (= R541), S641 (= S789), R643 (= R791)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q96), H100 (= H136), D164 (= D220), S165 (= S221), R446 (= R541), R451 (= R546), R579 (= R726), S641 (= S789), S642 (= S790)
- binding iron/sulfur cluster: H100 (= H136), I144 (= I186), H166 (= H222), S356 (= S441), C357 (= C442), C420 (= C508), C423 (= C511)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 89% coverage: 88:896/905 of query aligns to 64:746/754 of 5acnA
- active site: D100 (= D135), H101 (= H136), D165 (= D220), R447 (= R541), S642 (= S789), R644 (= R791)
- binding fe3-s4 cluster: I145 (= I186), H147 (= H188), H167 (= H222), C358 (= C442), C421 (= C508), C424 (= C511), N446 (= N540)
- binding tricarballylic acid: K198 (≠ L253), G235 (= G290), R666 (= R813)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 89% coverage: 88:896/905 of query aligns to 91:773/781 of P16276
- Q99 (= Q96) binding substrate
- DSH 192:194 (= DSH 220:222) binding substrate
- C385 (= C442) binding [4Fe-4S] cluster
- C448 (= C508) binding [4Fe-4S] cluster
- C451 (= C511) binding [4Fe-4S] cluster
- R474 (= R541) binding substrate
- R479 (= R546) binding substrate
- R607 (= R726) binding substrate
- SR 670:671 (= SR 790:791) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
27% identity, 89% coverage: 88:896/905 of query aligns to 63:745/753 of 1b0kA
- active site: D99 (= D135), H100 (= H136), D164 (= D220), R446 (= R541), A641 (≠ S789), R643 (= R791)
- binding citrate anion: Q71 (= Q96), H100 (= H136), D164 (= D220), S165 (= S221), R446 (= R541), R451 (= R546), R579 (= R726), A641 (≠ S789), S642 (= S790), R643 (= R791)
- binding oxygen atom: D164 (= D220), H166 (= H222)
- binding iron/sulfur cluster: H100 (= H136), D164 (= D220), H166 (= H222), S356 (= S441), C357 (= C442), C420 (= C508), C423 (= C511)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 58% coverage: 44:569/905 of query aligns to 54:505/789 of P39533
Sites not aligning to the query:
- 610 K→R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
O14289 3-isopropylmalate dehydratase; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
26% identity, 41% coverage: 215:588/905 of query aligns to 135:487/758 of O14289
- S486 (≠ E587) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
Query Sequence
>WP_068459766.1 NCBI__GCF_001541235.1:WP_068459766.1
MSDVQPISLDSFKCRRTISAGGKTYTYYSLPEAEKNGLAGISRLPFSMRVLLENLLRHED
GRTVTKTDIEAVAAWLNDKGKAGKEIGFRPARVLMQDFTGVPAVVDLAAMRDGMKSLGGD
AQKINPLVPVDLVIDHSVIVDEFGSPQAFAQNVELEYKRNVERYNFLKWGQGAFDNFRVV
PPGTGICHQVNLEFLAQTVWTRELPDGTILAYPDTLVGTDSHTTMVNGLAVLGWGVGGIE
AEAAMLGQAQSMLLPEVIGFKLTGKVNEGVTATDLVLTVTQMLRKKGVVGKFVEFYGPGL
DTMPLADRATIANMAPEYGATCGFFPIDGETLNYLRISGRESGRIELVEEYAKAQNMYRI
AGSEDPVFTDTLELDLSTVVPSMAGPKRPEGRIALPDVAPGFATALAGEYKKTGDTSARF
PVKGRDFDIGHGDVVITAITSCTNTSNPSVLIAAGLLAKKAVEKGLTAKPWVKTSLAPGS
QVVSAYLEKAGLQPYLDKVGFNLVGFGCTTCIGNSGPLAPEISATINENGIVAAAVLSGN
RNFEGRVSPDVQANYLASPPLVVAYALAGTVAKDLTVEPIGIGSDGEPVYLRDIWPSSQE
IHRFIAENITRELFLERYADVFNGDASWRAIDTAGGETYTWDDDSTYVRNPPYFEGISKD
PRPISDIKGARILGLFGDKITTDHISPAGSIKPSSPAGEYLSSHDVAVADFNQYGTRRGN
HEVMMRGTFANIRIKNFMLRDADGNVKEGGNTVHYPSGQQMSIYDAAMRYRDENVPLVVF
AGVEYGNGSSRDWAAKGTNLLGVRAVISQSFERIHRSNLVGMGIVPFVFEEGTSWETLGL
KGDEIVSIPGLTTIKPRQKMEAEITSADGTVRKVPIICRIDTLDEIEYFRNGGILHYVLR
NLAAA
Or try a new SitesBLAST search
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