SitesBLAST
Comparing WP_022948414.1 NCBI__GCF_000421465.1:WP_022948414.1 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)
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: 5:894/901 of query aligns to 11:906/909 of P09339
- C450 (= C439) 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
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)
57% identity, 97% coverage: 18:893/901 of query aligns to 112:987/990 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)
56% identity, 99% coverage: 5:893/901 of query aligns to 2:886/888 of 2b3xA
- active site: D124 (= D129), H125 (= H130), D204 (= D209), R535 (= R538), S777 (= S780), R779 (= R782)
- binding iron/sulfur cluster: I175 (= I180), H206 (= H211), C436 (= C439), C502 (= C505), C505 (= C508), I506 (= I509), N534 (= N537)
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)
56% identity, 99% coverage: 5:893/901 of query aligns to 3:887/889 of P21399
- C300 (≠ A304) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ E322) to M: in dbSNP:rs150373174
- C437 (= C439) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C505) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C508) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R538) mutation to Q: Strongly reduced RNA binding.
- R541 (= R543) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ K700) 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.
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)
53% identity, 99% coverage: 4:894/901 of query aligns to 11:939/943 of A0QX20
- K394 (≠ Q393) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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)
53% identity, 99% coverage: 5:894/901 of query aligns to 4:929/931 of D9X0I3
- SVIAD 125:129 (≠ SIQVD 131:135) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C505) 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 (≠ L733) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
49% identity, 99% coverage: 5:893/901 of query aligns to 2:848/850 of 3snpA
- active site: D124 (= D129), H125 (= H130), D186 (= D209), R505 (vs. gap), S739 (= S780), R741 (= R782)
- binding : H125 (= H130), S126 (= S131), H188 (= H211), L243 (= L266), R250 (= R273), N279 (= N302), E283 (= E306), S352 (≠ A373), P357 (= P378), K360 (≠ R381), T419 (= T440), N420 (= N441), T421 (= T442), N504 (vs. gap), R505 (vs. gap), L520 (vs. gap), S642 (= S683), P643 (= P684), A644 (= A685), G645 (= G686), N646 (≠ V687), R649 (≠ E690), R665 (≠ K705), S669 (≠ T709), 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)
29% identity, 89% coverage: 84:889/901 of query aligns to 89:772/778 of P19414
- R604 (≠ K700) 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
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 88% coverage: 84:872/901 of query aligns to 90:788/789 of P39533
- K610 (= K700) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 66:746/754 of 5acnA
- active site: D100 (= D129), H101 (= H130), D165 (= D209), R447 (= R538), S642 (= S780), R644 (= R782)
- binding fe3-s4 cluster: I145 (= I180), H147 (= H182), H167 (= H211), C358 (= C439), C421 (= C505), C424 (= C508), N446 (= N537)
- binding tricarballylic acid: K198 (≠ L242), G235 (= G279), R666 (= R804)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 65:745/753 of 1b0kA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R538), A641 (≠ S780), R643 (= R782)
- binding citrate anion: Q71 (= Q90), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R538), R451 (= R543), R579 (≠ K700), A641 (≠ S780), S642 (= S781), R643 (= R782)
- binding oxygen atom: D164 (= D209), H166 (= H211)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D209), H166 (= H211), S356 (= S438), C357 (= C439), C420 (= C505), C423 (= C508)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 89% coverage: 84:887/901 of query aligns to 93:773/781 of P16276
- Q99 (= Q90) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C439) binding [4Fe-4S] cluster
- C448 (= C505) binding [4Fe-4S] cluster
- C451 (= C508) binding [4Fe-4S] cluster
- R474 (= R538) binding substrate
- R479 (= R543) binding substrate
- R607 (≠ K700) binding substrate
- SR 670:671 (= SR 781:782) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 65:745/753 of 8acnA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R538), S641 (= S780), R643 (= R782)
- binding nitroisocitric acid: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R538), R451 (= R543), R579 (≠ K700), S641 (= S780), S642 (= S781), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D209), H166 (= H211), S356 (= S438), C357 (= C439), C420 (= C505), C423 (= C508), I424 (= I509)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 65:745/753 of 1fghA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R538), S641 (= S780), R643 (= R782)
- binding 4-hydroxy-aconitate ion: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R538), R451 (= R543), R579 (≠ K700), S641 (= S780), S642 (= S781), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H130), D164 (= D209), H166 (= H211), S356 (= S438), C357 (= C439), C420 (= C505), C423 (= C508), I424 (= I509), R451 (= R543)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 65:745/753 of 1amjA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R538), S641 (= S780), R643 (= R782)
- binding iron/sulfur cluster: I144 (= I180), H166 (= H211), C357 (= C439), C420 (= C505), C423 (= C508)
- binding sulfate ion: Q71 (= Q90), R579 (≠ K700), R643 (= R782)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 65:745/753 of 1amiA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R538), S641 (= S780), R643 (= R782)
- binding alpha-methylisocitric acid: Q71 (= Q90), T74 (= T93), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R538), R451 (= R543), R579 (≠ K700), S641 (= S780), S642 (= S781), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), D164 (= D209), H166 (= H211), S356 (= S438), C357 (= C439), C420 (= C505), C423 (= C508), N445 (= N537)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 65:745/753 of 1acoA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R538), S641 (= S780), R643 (= R782)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), D164 (= D209), H166 (= H211), S356 (= S438), C357 (= C439), C420 (= C505), C423 (= C508), N445 (= N537)
- binding aconitate ion: Q71 (= Q90), D164 (= D209), S165 (= S210), R446 (= R538), R451 (= R543), R579 (≠ K700), S641 (= S780), S642 (= S781), R643 (= R782)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 89% coverage: 84:887/901 of query aligns to 65:745/753 of 1nisA
- active site: D99 (= D129), H100 (= H130), D164 (= D209), R446 (= R538), S641 (= S780), R643 (= R782)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q90), H100 (= H130), D164 (= D209), S165 (= S210), R446 (= R538), R451 (= R543), R579 (≠ K700), S641 (= S780), S642 (= S781)
- binding iron/sulfur cluster: H100 (= H130), I144 (= I180), H166 (= H211), S356 (= S438), C357 (= C439), C420 (= C505), C423 (= C508)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 89% coverage: 84:887/901 of query aligns to 93:773/780 of P20004
- Q99 (= Q90) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C439) binding [4Fe-4S] cluster
- C448 (= C505) binding [4Fe-4S] cluster
- C451 (= C508) binding [4Fe-4S] cluster
- R474 (= R538) binding substrate
- R479 (= R543) binding substrate
- R607 (≠ K700) binding substrate
- SR 670:671 (= SR 781:782) binding substrate
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, 55% coverage: 86:585/901 of query aligns to 35:487/758 of O14289
- S486 (≠ R584) modified: Phosphoserine
Sites not aligning to the query:
- 488 modified: Phosphoserine
Query Sequence
>WP_022948414.1 NCBI__GCF_000421465.1:WP_022948414.1
MHDFDPFGSRAELNTAAGKLGYFNLARLEAENLGEVTALPFTIKVLLESILRHCDGKLIR
EQDVAALAGWNPTGDNRAEVPFMPARVLLQDFTGVPALVDLAAMRQAVQRLGKQPAQVEP
LIPADLVVDHSIQVDAFGSPEALKQNMALEFERNLERYQFLKWGQQAFESFKVVPPGVGI
VHQVNLEYLARGVFCQDGIVYPDSLVGTDSHTTMINGLGILGWGVGGIEAEAGMLGQPLY
MLPPEVIGFELTGALPEGATATDLVLRITEMLRAHGVVGKFVEFFGPGLSTISVPDRATV
ANMAPEYGATVGFFPVDAAVLEYMRATGRPQDRVELIETYYKAQGLFRTDDTPAPRFSEV
LRLDLSTVEPSLAGPRRPQDRVAVGALRDAFRQALTRPASEAGFGVPPAEKDAAVSVSVD
GRKAELKHGSVVIAAITSCTNTSNPSVMLSAGLVAKKAAEKGLKPSVSVKTSLAPGSRVV
TDYLQESGLLPYLEAIGFYTVGYGCTTCIGNSGPLPEAVAKGIQSGRLVAAAVLSGNRNF
EGRVHPLTRANYLASPPLVVAYALAGTVDIDLTREPLGTDKEGRPVYLRDIWPTREELEA
VLKTASDPEKFNRVYTHLDDFNPEWNAIQVPASVLYDWPPESTYIQEPPFFQKMQPQPEP
IQPIEGARVLAMMGDSVTTDHISPAGVIPEGPAAEYLRSKGVGEKDFNTFGARRGNHEVM
MRGTFANIRLKNLLVPGKEGGVTIHFPGGEETWIFDAAMRYQAEEVPLIVLAGKDYGMGS
SRDWAAKGPRLLGVKAVIAESFERIHRSNLVGMGILPLTFKPGDSARSLGLTGRERYRIP
ADETLAVGAELTVTAEADDGTKISFPADVRLNSAAELEYYRNGGILQTVLRNMLTGEAAS
A
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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