SitesBLAST
Comparing WP_013451188.1 NCBI__GCF_000183405.1:WP_013451188.1 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)
53% identity, 99% coverage: 9:875/877 of query aligns to 18:904/909 of P09339
- C450 (= C422) 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 (= R713) 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)
51% identity, 98% coverage: 19:876/877 of query aligns to 117:987/990 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)
50% identity, 98% coverage: 19:876/877 of query aligns to 21:887/889 of P21399
- C300 (≠ T304) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ E322) to M: in dbSNP:rs150373174
- C437 (= C422) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C488) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C491) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R521) mutation to Q: Strongly reduced RNA binding.
- R541 (= R526) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ K684) mutation to K: No effect on RNA binding.
- S778 (= S763) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R765) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
50% identity, 98% coverage: 19:876/877 of query aligns to 20:886/888 of 2b3xA
- active site: D124 (= D125), H125 (= H126), D204 (= D209), R535 (= R521), S777 (= S763), R779 (= R765)
- binding iron/sulfur cluster: I175 (= I176), H206 (= H211), C436 (= C422), C502 (= C488), C505 (= C491), I506 (= I492), N534 (= N520)
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)
49% identity, 99% coverage: 14:877/877 of query aligns to 24:939/943 of A0QX20
- K394 (vs. gap) 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)
48% identity, 99% coverage: 8:877/877 of query aligns to 10:929/931 of D9X0I3
- SVIAD 125:129 (≠ SVQVD 127:131) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C488) 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 (= R713) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ K717) 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)
48% identity, 98% coverage: 19:876/877 of query aligns to 20:848/850 of 3snpA
- active site: D124 (= D125), H125 (= H126), D186 (= D209), R505 (= R521), S739 (= S763), R741 (= R765)
- binding : H125 (= H126), S126 (= S127), H188 (= H211), L243 (= L266), R250 (= R273), N279 (= N302), E283 (= E306), S352 (≠ A371), P357 (= P376), K360 (≠ R379), T419 (= T423), N420 (= N424), T421 (= T425), N504 (= N520), R505 (= R521), L520 (= L536), S642 (= S666), P643 (= P667), A644 (= A668), G645 (= G669), N646 (≠ E670), R649 (≠ P673), R665 (≠ D689), S669 (= S693), G671 (= G695), R674 (= R698), R741 (= R765)
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)
30% identity, 90% coverage: 79:869/877 of query aligns to 88:769/778 of P19414
- R604 (≠ K684) 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, 91% coverage: 80:875/877 of query aligns to 90:787/789 of P39533
- K610 (= K684) 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, 90% coverage: 79:869/877 of query aligns to 65:745/754 of 5acnA
- active site: D100 (= D125), H101 (= H126), D165 (= D209), R447 (= R521), S642 (= S763), R644 (= R765)
- binding fe3-s4 cluster: I145 (= I176), H147 (= H178), H167 (= H211), C358 (= C422), C421 (= C488), C424 (= C491), N446 (= N520)
- binding tricarballylic acid: K198 (≠ P242), G235 (≠ D279), R666 (= R787)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 90% coverage: 79:869/877 of query aligns to 64:744/753 of 1b0kA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R521), A641 (≠ S763), R643 (= R765)
- binding citrate anion: Q71 (= Q86), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R521), R451 (= R526), R579 (≠ K684), A641 (≠ S763), S642 (= S764), R643 (= R765)
- binding oxygen atom: D164 (= D209), H166 (= H211)
- binding iron/sulfur cluster: H100 (= H126), D164 (= D209), H166 (= H211), S356 (= S421), C357 (= C422), C420 (= C488), C423 (= C491)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 98% coverage: 11:869/877 of query aligns to 36:772/781 of P16276
- Q99 (= Q86) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C422) binding [4Fe-4S] cluster
- C448 (= C488) binding [4Fe-4S] cluster
- C451 (= C491) binding [4Fe-4S] cluster
- R474 (= R521) binding substrate
- R479 (= R526) binding substrate
- R607 (≠ K684) binding substrate
- SR 670:671 (= SR 764:765) 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, 90% coverage: 79:869/877 of query aligns to 64:744/753 of 8acnA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R521), S641 (= S763), R643 (= R765)
- binding nitroisocitric acid: Q71 (= Q86), T74 (= T89), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R521), R451 (= R526), R579 (≠ K684), S641 (= S763), S642 (= S764), R643 (= R765)
- binding iron/sulfur cluster: H100 (= H126), D164 (= D209), H166 (= H211), S356 (= S421), C357 (= C422), C420 (= C488), C423 (= C491), I424 (= I492)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 90% coverage: 79:869/877 of query aligns to 64:744/753 of 1fghA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R521), S641 (= S763), R643 (= R765)
- binding 4-hydroxy-aconitate ion: Q71 (= Q86), T74 (= T89), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R521), R451 (= R526), R579 (≠ K684), S641 (= S763), S642 (= S764), R643 (= R765)
- binding iron/sulfur cluster: H100 (= H126), D164 (= D209), H166 (= H211), S356 (= S421), C357 (= C422), C420 (= C488), C423 (= C491), I424 (= I492), R451 (= R526)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 90% coverage: 79:869/877 of query aligns to 64:744/753 of 1amjA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R521), S641 (= S763), R643 (= R765)
- binding iron/sulfur cluster: I144 (= I176), H166 (= H211), C357 (= C422), C420 (= C488), C423 (= C491)
- binding sulfate ion: Q71 (= Q86), R579 (≠ K684), R643 (= R765)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 90% coverage: 79:869/877 of query aligns to 64:744/753 of 1amiA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R521), S641 (= S763), R643 (= R765)
- binding alpha-methylisocitric acid: Q71 (= Q86), T74 (= T89), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R521), R451 (= R526), R579 (≠ K684), S641 (= S763), S642 (= S764), R643 (= R765)
- binding iron/sulfur cluster: H100 (= H126), I144 (= I176), D164 (= D209), H166 (= H211), S356 (= S421), C357 (= C422), C420 (= C488), C423 (= C491), N445 (= N520)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 90% coverage: 79:869/877 of query aligns to 64:744/753 of 1acoA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R521), S641 (= S763), R643 (= R765)
- binding iron/sulfur cluster: H100 (= H126), I144 (= I176), D164 (= D209), H166 (= H211), S356 (= S421), C357 (= C422), C420 (= C488), C423 (= C491), N445 (= N520)
- binding aconitate ion: Q71 (= Q86), D164 (= D209), S165 (= S210), R446 (= R521), R451 (= R526), R579 (≠ K684), S641 (= S763), S642 (= S764), R643 (= R765)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 90% coverage: 79:869/877 of query aligns to 64:744/753 of 1nisA
- active site: D99 (= D125), H100 (= H126), D164 (= D209), R446 (= R521), S641 (= S763), R643 (= R765)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q86), H100 (= H126), D164 (= D209), S165 (= S210), R446 (= R521), R451 (= R526), R579 (≠ K684), S641 (= S763), S642 (= S764)
- binding iron/sulfur cluster: H100 (= H126), I144 (= I176), H166 (= H211), S356 (= S421), C357 (= C422), C420 (= C488), C423 (= C491)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 90% coverage: 79:869/877 of query aligns to 92:772/780 of P20004
- Q99 (= Q86) binding substrate
- DSH 192:194 (= DSH 209:211) binding substrate
- C385 (= C422) binding [4Fe-4S] cluster
- C448 (= C488) binding [4Fe-4S] cluster
- C451 (= C491) binding [4Fe-4S] cluster
- R474 (= R521) binding substrate
- R479 (= R526) binding substrate
- R607 (≠ K684) binding substrate
- SR 670:671 (= SR 764:765) binding substrate
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
27% identity, 56% coverage: 57:551/877 of query aligns to 6:417/423 of 4kp1A
- active site: D64 (= D125), H65 (= H126), D121 (= D209), R387 (= R521)
- binding 2,4-dimethylpentane-2,4-diol: F299 (≠ A418), S302 (= S421), S383 (≠ L517), F389 (= F523)
- binding magnesium ion: C303 (= C422), T304 (= T423), R387 (= R521)
Query Sequence
>WP_013451188.1 NCBI__GCF_000183405.1:WP_013451188.1
MDKEKYLSSFEFEEREYFFYDINKLSKDGFDIKKLPYSIKILVENILRNLGDGQVNEKDL
KNIAGWSRKQPIPIEIPYKPVRVLMQDFTGVPAVVDLAAMRDAMLELGKNPEKINPLVPV
DLIVDHSVQVDYYGTEDSILKNVALEYKRNEERYKLLKWAQKSFHNFRVVPPNSGICHQV
NLEYLAKVVCIDDRKDKKLLYLDTCIGTDSHTPMVNGIGVMGWGVGGIEAEAVMLGQPYY
MPIPEVIGVKLIGELNEGVTATDLILTITEKLRRYGVVDKFVEYFGPGVKTLSIPDRATI
SNMTPEFGATLGIFPIDRKTIEYLRMTNRDRYADILEIYAKKAGIFYTGQEKVEYTDVLE
IDLNSIEPSIAGPSRPQDRISLSQVKSNLQNLKTDNFVDIEIDQNPVRIKDGSVVIAAIT
SCTNTSNPFVIIGAGLMARNAVKKGLRVKPYVKTSFAPGSKVVESYLKKSGLMPYLEALG
FHITAYGCTTCIGNSGPVLPQIEEAIIKNNLNVAAVLSGNRNFEARIHQLVRSNFLASPM
LVVAYALAGKIDIDFKNEPLGYTPYGEKVMLKDLWPSSEEIHEIISDTFTKSDFKRDYGK
IFDGDLFWQKMNVKVDKTYHWHEKSTYIKKPPYFDNFMKEPGKIFDITNARILLLLGDSI
TTDHISPAGEIDPDYPAGKYLISKGVKEDDFNSYGSRRGNHEVMIRGTFGNIRIKNKMVN
REGSFTVKYPENEEMFIFDAAMKYQMENTPLVVFAGKEYGTGSSRDWAAKGTSLLGIKAV
IAESFERIHKSNLVGMGILPLQFKEGESWAKYEIKGDEVVSIFGLENLSPRKDIRIELSK
PDGEKREFFVTLRLDTEVEVEYYANGGILPYVLRRFL
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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