SitesBLAST
Comparing WP_013011295.1 NCBI__GCF_000025725.1:WP_013011295.1 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)
54% identity, 99% coverage: 2:877/881 of query aligns to 11:903/909 of P09339
- C450 (= C424) 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 (= R715) 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)
52% identity, 99% coverage: 7:881/881 of query aligns to 9:930/931 of D9X0I3
- SVIAD 125:129 (≠ SVQVD 128:132) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C490) 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 (= R715) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ K719) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
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)
50% identity, 99% coverage: 7:881/881 of query aligns to 17:940/943 of A0QX20
- K394 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 99% coverage: 13:881/881 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)
49% identity, 98% coverage: 19:881/881 of query aligns to 21:889/889 of P21399
- C300 (≠ S305) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ R323) to M: in dbSNP:rs150373174
- C437 (= C424) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C490) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C493) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R523) mutation to Q: Strongly reduced RNA binding.
- R541 (= R528) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ N686) mutation to K: No effect on RNA binding.
- S778 (= S766) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R768) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
49% identity, 98% coverage: 19:881/881 of query aligns to 20:888/888 of 2b3xA
- active site: D124 (= D126), H125 (= H127), D204 (= D210), R535 (= R523), S777 (= S766), R779 (= R768)
- binding iron/sulfur cluster: I175 (= I177), H206 (= H212), C436 (= C424), C502 (= C490), C505 (= C493), I506 (= I494), N534 (= N522)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
49% identity, 96% coverage: 35:881/881 of query aligns to 33:850/850 of 3snpA
- active site: D124 (= D126), H125 (= H127), D186 (= D210), R505 (= R523), S739 (= S766), R741 (= R768)
- binding : H125 (= H127), S126 (= S128), H188 (= H212), L243 (= L267), R250 (= R274), N279 (= N303), E283 (= E307), S352 (≠ A372), P357 (= P377), K360 (≠ H380), T419 (= T425), N420 (= N426), T421 (= T427), N504 (= N522), R505 (= R523), L520 (= L538), S642 (= S668), P643 (= P669), A644 (= A670), G645 (= G671), N646 (≠ A672), R649 (≠ A675), R665 (≠ V691), S669 (= S695), G671 (= G697), R674 (= R700), R741 (= R768)
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, 90% coverage: 80:872/881 of query aligns to 88:769/778 of P19414
- R604 (≠ N686) 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
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 67:745/754 of 5acnA
- active site: D100 (= D126), H101 (= H127), D165 (= D210), R447 (= R523), S642 (= S766), R644 (= R768)
- binding fe3-s4 cluster: I145 (= I177), H147 (= H179), H167 (= H212), C358 (= C424), C421 (= C490), C424 (= C493), N446 (= N522)
- binding tricarballylic acid: K198 (≠ P243), G235 (≠ E280), R666 (= R790)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 88% coverage: 97:872/881 of query aligns to 94:772/781 of P16276
- Q99 (≠ R102) binding substrate
- DSH 192:194 (= DSH 210:212) binding substrate
- C385 (= C424) binding [4Fe-4S] cluster
- C448 (= C490) binding [4Fe-4S] cluster
- C451 (= C493) binding [4Fe-4S] cluster
- R474 (= R523) binding substrate
- R479 (= R528) binding substrate
- R607 (≠ N694) binding substrate
- SR 670:671 (= SR 767:768) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 66:744/753 of 1b0kA
- active site: D99 (= D126), H100 (= H127), D164 (= D210), R446 (= R523), A641 (≠ S766), R643 (= R768)
- binding citrate anion: Q71 (≠ R102), H100 (= H127), D164 (= D210), S165 (= S211), R446 (= R523), R451 (= R528), R579 (≠ N694), A641 (≠ S766), S642 (= S767), R643 (= R768)
- binding oxygen atom: D164 (= D210), H166 (= H212)
- binding iron/sulfur cluster: H100 (= H127), D164 (= D210), H166 (= H212), S356 (= S423), C357 (= C424), C420 (= C490), C423 (= C493)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 88% coverage: 97:872/881 of query aligns to 94:772/780 of P20004
- Q99 (≠ R102) binding substrate
- DSH 192:194 (= DSH 210:212) binding substrate
- C385 (= C424) binding [4Fe-4S] cluster
- C448 (= C490) binding [4Fe-4S] cluster
- C451 (= C493) binding [4Fe-4S] cluster
- R474 (= R523) binding substrate
- R479 (= R528) binding substrate
- R607 (≠ N694) binding substrate
- SR 670:671 (= SR 767:768) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 66:744/753 of 8acnA
- active site: D99 (= D126), H100 (= H127), D164 (= D210), R446 (= R523), S641 (= S766), R643 (= R768)
- binding nitroisocitric acid: Q71 (≠ R102), T74 (≠ L105), H100 (= H127), D164 (= D210), S165 (= S211), R446 (= R523), R451 (= R528), R579 (≠ N694), S641 (= S766), S642 (= S767), R643 (= R768)
- binding iron/sulfur cluster: H100 (= H127), D164 (= D210), H166 (= H212), S356 (= S423), C357 (= C424), C420 (= C490), C423 (= C493), I424 (= I494)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 66:744/753 of 1fghA
- active site: D99 (= D126), H100 (= H127), D164 (= D210), R446 (= R523), S641 (= S766), R643 (= R768)
- binding 4-hydroxy-aconitate ion: Q71 (≠ R102), T74 (≠ L105), H100 (= H127), D164 (= D210), S165 (= S211), R446 (= R523), R451 (= R528), R579 (≠ N694), S641 (= S766), S642 (= S767), R643 (= R768)
- binding iron/sulfur cluster: H100 (= H127), D164 (= D210), H166 (= H212), S356 (= S423), C357 (= C424), C420 (= C490), C423 (= C493), I424 (= I494), R451 (= R528)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 66:744/753 of 1amjA
- active site: D99 (= D126), H100 (= H127), D164 (= D210), R446 (= R523), S641 (= S766), R643 (= R768)
- binding iron/sulfur cluster: I144 (= I177), H166 (= H212), C357 (= C424), C420 (= C490), C423 (= C493)
- binding sulfate ion: Q71 (≠ R102), R579 (≠ N694), R643 (= R768)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 66:744/753 of 1amiA
- active site: D99 (= D126), H100 (= H127), D164 (= D210), R446 (= R523), S641 (= S766), R643 (= R768)
- binding alpha-methylisocitric acid: Q71 (≠ R102), T74 (≠ L105), H100 (= H127), D164 (= D210), S165 (= S211), R446 (= R523), R451 (= R528), R579 (≠ N694), S641 (= S766), S642 (= S767), R643 (= R768)
- binding iron/sulfur cluster: H100 (= H127), I144 (= I177), D164 (= D210), H166 (= H212), S356 (= S423), C357 (= C424), C420 (= C490), C423 (= C493), N445 (= N522)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 66:744/753 of 1acoA
- active site: D99 (= D126), H100 (= H127), D164 (= D210), R446 (= R523), S641 (= S766), R643 (= R768)
- binding iron/sulfur cluster: H100 (= H127), I144 (= I177), D164 (= D210), H166 (= H212), S356 (= S423), C357 (= C424), C420 (= C490), C423 (= C493), N445 (= N522)
- binding aconitate ion: Q71 (≠ R102), D164 (= D210), S165 (= S211), R446 (= R523), R451 (= R528), R579 (≠ N694), S641 (= S766), S642 (= S767), R643 (= R768)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 88% coverage: 97:872/881 of query aligns to 66:744/753 of 1nisA
- active site: D99 (= D126), H100 (= H127), D164 (= D210), R446 (= R523), S641 (= S766), R643 (= R768)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (≠ R102), H100 (= H127), D164 (= D210), S165 (= S211), R446 (= R523), R451 (= R528), R579 (≠ N694), S641 (= S766), S642 (= S767)
- binding iron/sulfur cluster: H100 (= H127), I144 (= I177), H166 (= H212), S356 (= S423), C357 (= C424), C420 (= C490), C423 (= C493)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 88% coverage: 97:875/881 of query aligns to 91:782/789 of P39533
- K610 (≠ N686) mutation to 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)
28% identity, 43% coverage: 205:581/881 of query aligns to 135:500/758 of O14289
- S486 (≠ K569) modified: Phosphoserine
- S488 (vs. gap) modified: Phosphoserine
Query Sequence
>WP_013011295.1 NCBI__GCF_000025725.1:WP_013011295.1
MDRTHFRSHFEFGGKTYAYYDLKKVQAAGMADIQKLPYSIRVLLENIVRNFDGKVVTEGD
VKEVGGWKKSYDAPFEIAHHPARVVMQDFTGVPGVVDLAAMRDALAEKGKKASLINPVVP
VDLIIDHSVQVDYYGTPDCLDKNVAKEYERNSERYSLLKWAQASFDNMRIVPPRSGICHQ
VNLEYLGQIVLKGEVNGEETAFCDTLVGTDSHTTMINAIGVMGWGVGGIEAEAVMLGQPY
YMPIPEVIGLRLTGEIAEGITGTDVVLTITELLRRHKVVEKFVEVYGPGLKALSLPDRAT
ISNMSPEYGSTMGFFPVDDETIRYMRETNRAEQSQFVENYTKMNMLFYDYNNEPEYTKVV
ELDLSTVKPCVAGPKKPQQHIPLEKLPAVAGEETPEKKSVEIELEGKKIKLSENDVVVAA
ITSCTNTSNPFVMIGAGMVAKKAVEKGLKVKPYVKTSLAPGSKVVTDYLEASGVDKYLNQ
LGFNLAAYGCTTCIGNSGPLKAPINDAVKDNKMSVAAVLSGNRNFEARIHPLIRQNYLAS
PMLVVVYALAGTVDIDLHLDPVGTDKNGKPVYMRDLWPSNDEVWALVKRYVTTDQYEKRY
SEILEGDENWKTLPIVKSDIYEWIPDSTYIRRPPFFEDFSLELTPAQDIIGAKPLAMLGD
TVTTDHISPAGAIPAEYPAGQYLEANGVKPVDFNSYGSRRGNHEVMMRGTFGNVRIKNKL
ADPKEGGFTKHMPDGKDSYIYDAAMKYIKEGTPTVVFGGKEYGTGSSRDWAAKGTLLLGV
KAVIAESFERIHRSNLAGMGILPLQFTGGNSWAGLGLDGTETFDIKGIAEVSPRCSLKVT
AVKPDGSQTEFVVLCRLDTEVEIEYFKHGGILAYVLRGMAK
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