SitesBLAST
Comparing AZOBR_RS02985 FitnessBrowser__azobra:AZOBR_RS02985 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)
57% identity, 100% coverage: 5:896/896 of query aligns to 6:940/943 of A0QX20
- K394 (≠ T401) 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)
56% identity, 99% coverage: 7:896/896 of query aligns to 10:907/909 of P09339
- C450 (= C438) 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 (= R729) 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)
57% identity, 99% coverage: 8:896/896 of query aligns to 4:930/931 of D9X0I3
- SVIAD 125:129 (≠ SVMVD 134:138) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C504) 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 (= R729) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ E733) 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)
55% identity, 98% coverage: 19:896/896 of query aligns to 111:989/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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)
52% identity, 97% coverage: 25:896/896 of query aligns to 21:889/889 of P21399
- C300 (≠ A312) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ R330) to M: in dbSNP:rs150373174
- C437 (= C438) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C504) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C507) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R537) mutation to Q: Strongly reduced RNA binding.
- R541 (= R542) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H700) mutation to K: No effect on RNA binding.
- S778 (= S780) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R782) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
52% identity, 97% coverage: 25:896/896 of query aligns to 20:888/888 of 2b3xA
- active site: D124 (= D132), H125 (= H133), D204 (= D217), R535 (= R537), S777 (= S780), R779 (= R782)
- binding iron/sulfur cluster: I175 (= I183), H206 (= H219), C436 (= C438), C502 (= C504), C505 (= C507), I506 (= I508), N534 (= N536)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
51% identity, 96% coverage: 41:896/896 of query aligns to 33:850/850 of 3snpA
- active site: D124 (= D132), H125 (= H133), D186 (= D217), R505 (= R537), S739 (= S780), R741 (= R782)
- binding : H125 (= H133), S126 (= S134), H188 (= H219), L243 (= L274), R250 (= R281), N279 (= N310), E283 (= E314), S352 (≠ A381), P357 (= P386), K360 (≠ R389), T419 (= T439), N420 (= N440), T421 (= T441), N504 (= N536), R505 (= R537), L520 (= L552), S642 (= S682), P643 (= P683), A644 (= A684), G645 (= G685), N646 (≠ S686), R649 (≠ K689), R665 (≠ Q705), S669 (= S709), G671 (= G711), R674 (= R714), R741 (= R782)
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)
28% identity, 91% coverage: 75:890/896 of query aligns to 74:772/778 of P19414
- R604 (= R722) 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
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 55:745/753 of 8acnA
- active site: D99 (= D132), H100 (= H133), D164 (= D217), R446 (= R537), S641 (= S780), R643 (= R782)
- binding nitroisocitric acid: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D217), S165 (= S218), R446 (= R537), R451 (= R542), R579 (= R722), S641 (= S780), S642 (= S781), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D217), H166 (= H219), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), I424 (= I508)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 55:745/753 of 1fghA
- active site: D99 (= D132), H100 (= H133), D164 (= D217), R446 (= R537), S641 (= S780), R643 (= R782)
- binding 4-hydroxy-aconitate ion: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D217), S165 (= S218), R446 (= R537), R451 (= R542), R579 (= R722), S641 (= S780), S642 (= S781), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D217), H166 (= H219), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), I424 (= I508), R451 (= R542)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 55:745/753 of 1amjA
- active site: D99 (= D132), H100 (= H133), D164 (= D217), R446 (= R537), S641 (= S780), R643 (= R782)
- binding iron/sulfur cluster: I144 (= I183), H166 (= H219), C357 (= C438), C420 (= C504), C423 (= C507)
- binding sulfate ion: Q71 (= Q93), R579 (= R722), R643 (= R782)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 55:745/753 of 1amiA
- active site: D99 (= D132), H100 (= H133), D164 (= D217), R446 (= R537), S641 (= S780), R643 (= R782)
- binding alpha-methylisocitric acid: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D217), S165 (= S218), R446 (= R537), R451 (= R542), R579 (= R722), S641 (= S780), S642 (= S781), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), D164 (= D217), H166 (= H219), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), N445 (= N536)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 55:745/753 of 1acoA
- active site: D99 (= D132), H100 (= H133), D164 (= D217), R446 (= R537), S641 (= S780), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), D164 (= D217), H166 (= H219), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507), N445 (= N536)
- binding aconitate ion: Q71 (= Q93), D164 (= D217), S165 (= S218), R446 (= R537), R451 (= R542), R579 (= R722), S641 (= S780), S642 (= S781), R643 (= R782)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 56:746/754 of 5acnA
- active site: D100 (= D132), H101 (= H133), D165 (= D217), R447 (= R537), S642 (= S780), R644 (= R782)
- binding fe3-s4 cluster: I145 (= I183), H147 (= H185), H167 (= H219), C358 (= C438), C421 (= C504), C424 (= C507), N446 (= N536)
- binding tricarballylic acid: K198 (≠ L250), G235 (= G287), R666 (= R804)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 55:745/753 of 1nisA
- active site: D99 (= D132), H100 (= H133), D164 (= D217), R446 (= R537), S641 (= S780), R643 (= R782)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q93), H100 (= H133), D164 (= D217), S165 (= S218), R446 (= R537), R451 (= R542), R579 (= R722), S641 (= S780), S642 (= S781)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), H166 (= H219), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
29% identity, 91% coverage: 77:888/896 of query aligns to 83:773/781 of P16276
- Q99 (= Q93) binding substrate
- DSH 192:194 (= DSH 217:219) binding substrate
- C385 (= C438) binding [4Fe-4S] cluster
- C448 (= C504) binding [4Fe-4S] cluster
- C451 (= C507) binding [4Fe-4S] cluster
- R474 (= R537) binding substrate
- R479 (= R542) binding substrate
- R607 (= R722) binding substrate
- SR 670:671 (= SR 781:782) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
29% identity, 91% coverage: 77:888/896 of query aligns to 55:745/753 of 1b0kA
- active site: D99 (= D132), H100 (= H133), D164 (= D217), R446 (= R537), A641 (≠ S780), R643 (= R782)
- binding citrate anion: Q71 (= Q93), H100 (= H133), D164 (= D217), S165 (= S218), R446 (= R537), R451 (= R542), R579 (= R722), A641 (≠ S780), S642 (= S781), R643 (= R782)
- binding oxygen atom: D164 (= D217), H166 (= H219)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D217), H166 (= H219), S356 (= S437), C357 (= C438), C420 (= C504), C423 (= C507)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
29% identity, 91% coverage: 77:888/896 of query aligns to 83:773/780 of P20004
- Q99 (= Q93) binding substrate
- DSH 192:194 (= DSH 217:219) binding substrate
- C385 (= C438) binding [4Fe-4S] cluster
- C448 (= C504) binding [4Fe-4S] cluster
- C451 (= C507) binding [4Fe-4S] cluster
- R474 (= R537) binding substrate
- R479 (= R542) binding substrate
- R607 (= R722) binding substrate
- SR 670:671 (= SR 781:782) binding substrate
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 60% coverage: 42:576/896 of query aligns to 54:516/789 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)
27% identity, 40% coverage: 212:567/896 of query aligns to 135:472/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>AZOBR_RS02985 FitnessBrowser__azobra:AZOBR_RS02985
VTTFTGQDSLKTRRSLSVGGKSYDYFSIKAAEDAGLGDLSRLPYSMKVLLENLLRFEDGR
TVSTDDVKAVAQWLHDKRSDREIAYRPARVLMQDFTGVPAVCDLAAMREAMAALGGDPKK
INPLVPVDLVIDHSVMVDYFGNPSAFEKNVELEFERNLERYAFLRWGQKAFDNFRVVPPG
TGICHQVNVEYLAQGVWTDTDPAGKLVAYPDTLVGTDSHTTMVNGLGVLGWGVGGIEAEA
AMLGQPISMLIPEVVGFKLTGRLKEGTTATDLVLTVTQMLRKKGVVGKFVEFYGPGLDHL
TLADRATIGNMAPEYGATCGIFPIDAETIRYLTFTGRDADRVAMVEAYARAQGMWRDAGT
PDPVFTDALELDMTTVEPSLAGPKRPQDRVPLSQAAQSFGTDLVGAFKAEDADRSVPVKG
CGYNLDQGAVVIAAITSCTNTSNPAVLVAAGLLARKAVEKGLKSKPWVKTSLAPGSQVVT
DYLAKAGLQPYLDQLGFNIVGYGCTTCIGNSGPLPDPIAAAVEEGNLVVAAVLSGNRNFE
GRVNPHTRANYLASPPLCVAYALAGNMKIDLAKDPIGTGHDGQPVYLKDVWPTNQEVQDA
IDASLSAEMFRSRYGNVFEGPEQWRGIQTAEGQTYEWQAGSTYVKLPPFFADMPKTPDAV
SDVRGARALAVLGDSITTDHISPAGSIKKTSPAGEYLLSHQVRPQDFNSYGARRGNHEVM
MRGTFANIRIRNEMLAGVEGGETRHYPSGEQLPIYTAAMRYAQEGVPLVVIAGKEYGTGS
SRDWAAKGTKLLGIRAVIAESFERIHRSNLVGMGILPLQFKDGLTRNDLALDGTETFDID
GIEQDLRPRKDVTMTITRADGQTRQVPLLLRIDTVDEVEYYRNGGVLNFVLRNLAK
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