SitesBLAST
Comparing WP_077243786.1 NCBI__GCF_001995255.1:WP_077243786.1 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)
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)
62% identity, 96% coverage: 33:913/917 of query aligns to 33:928/931 of D9X0I3
- SVIAD 125:129 (≠ SVQVD 125:129) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C525) 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 (= R750) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ L754) 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)
60% identity, 96% coverage: 31:913/917 of query aligns to 39:938/943 of A0QX20
- K394 (≠ R392) 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, 96% coverage: 29:912/917 of query aligns to 41:904/909 of P09339
- C450 (= C459) 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 (= R750) 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)
54% identity, 98% coverage: 22:916/917 of query aligns to 120:990/990 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)
54% identity, 97% coverage: 26:914/917 of query aligns to 27:887/888 of 2b3xA
- active site: D124 (= D123), H125 (= H124), D204 (= D208), R535 (= R558), S777 (= S801), R779 (= R803)
- binding iron/sulfur cluster: I175 (= I174), H206 (= H210), C436 (= C459), C502 (= C525), C505 (= C528), I506 (= I529), N534 (= N557)
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)
54% identity, 97% coverage: 26:914/917 of query aligns to 28:888/889 of P21399
- C300 (≠ A303) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ E321) to M: in dbSNP:rs150373174
- C437 (= C459) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C525) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C528) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R558) mutation to Q: Strongly reduced RNA binding.
- R541 (= R563) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ Q721) mutation to K: No effect on RNA binding.
- S778 (= S801) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R803) 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)
52% identity, 97% coverage: 26:914/917 of query aligns to 27:849/850 of 3snpA
- active site: D124 (= D123), H125 (= H124), D186 (= D208), R505 (= R558), S739 (= S801), R741 (= R803)
- binding : H125 (= H124), S126 (= S125), H188 (= H210), L243 (= L265), R250 (= R272), N279 (= N301), E283 (= E305), S352 (≠ A372), P357 (= P377), K360 (≠ R380), T419 (= T460), N420 (= N461), T421 (= T462), N504 (= N557), R505 (= R558), L520 (= L573), S642 (= S703), P643 (= P704), A644 (= A705), G645 (= G706), N646 (≠ S707), R649 (≠ S710), R665 (≠ A726), S669 (= S730), G671 (= G732), R674 (= R735), R741 (= R803)
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, 84% coverage: 74:843/917 of query aligns to 85:708/778 of P19414
- R604 (= R735) 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)
25% identity, 96% coverage: 33:909/917 of query aligns to 54:782/789 of P39533
- K610 (≠ R743) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 36:744/753 of 8acnA
- active site: D99 (= D123), H100 (= H124), D164 (= D208), R446 (= R558), S641 (= S801), R643 (= R803)
- binding nitroisocitric acid: Q71 (= Q84), T74 (= T87), H100 (= H124), D164 (= D208), S165 (= S209), R446 (= R558), R451 (= R563), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H124), D164 (= D208), H166 (= H210), S356 (= S458), C357 (= C459), C420 (= C525), C423 (= C528), I424 (= I529)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 36:744/753 of 1fghA
- active site: D99 (= D123), H100 (= H124), D164 (= D208), R446 (= R558), S641 (= S801), R643 (= R803)
- binding 4-hydroxy-aconitate ion: Q71 (= Q84), T74 (= T87), H100 (= H124), D164 (= D208), S165 (= S209), R446 (= R558), R451 (= R563), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H124), D164 (= D208), H166 (= H210), S356 (= S458), C357 (= C459), C420 (= C525), C423 (= C528), I424 (= I529), R451 (= R563)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 36:744/753 of 1amjA
- active site: D99 (= D123), H100 (= H124), D164 (= D208), R446 (= R558), S641 (= S801), R643 (= R803)
- binding iron/sulfur cluster: I144 (= I174), H166 (= H210), C357 (= C459), C420 (= C525), C423 (= C528)
- binding sulfate ion: Q71 (= Q84), R579 (= R743), R643 (= R803)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 36:744/753 of 1amiA
- active site: D99 (= D123), H100 (= H124), D164 (= D208), R446 (= R558), S641 (= S801), R643 (= R803)
- binding alpha-methylisocitric acid: Q71 (= Q84), T74 (= T87), H100 (= H124), D164 (= D208), S165 (= S209), R446 (= R558), R451 (= R563), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H124), I144 (= I174), D164 (= D208), H166 (= H210), S356 (= S458), C357 (= C459), C420 (= C525), C423 (= C528), N445 (= N557)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 36:744/753 of 1acoA
- active site: D99 (= D123), H100 (= H124), D164 (= D208), R446 (= R558), S641 (= S801), R643 (= R803)
- binding iron/sulfur cluster: H100 (= H124), I144 (= I174), D164 (= D208), H166 (= H210), S356 (= S458), C357 (= C459), C420 (= C525), C423 (= C528), N445 (= N557)
- binding aconitate ion: Q71 (= Q84), D164 (= D208), S165 (= S209), R446 (= R558), R451 (= R563), R579 (= R743), S641 (= S801), S642 (= S802), R643 (= R803)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 36:744/753 of 1nisA
- active site: D99 (= D123), H100 (= H124), D164 (= D208), R446 (= R558), S641 (= S801), R643 (= R803)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q84), H100 (= H124), D164 (= D208), S165 (= S209), R446 (= R558), R451 (= R563), R579 (= R743), S641 (= S801), S642 (= S802)
- binding iron/sulfur cluster: H100 (= H124), I144 (= I174), H166 (= H210), S356 (= S458), C357 (= C459), C420 (= C525), C423 (= C528)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
26% identity, 94% coverage: 43:906/917 of query aligns to 53:772/780 of P20004
- Q99 (= Q84) binding substrate
- DSH 192:194 (= DSH 208:210) binding substrate
- C385 (= C459) binding [4Fe-4S] cluster
- C448 (= C525) binding [4Fe-4S] cluster
- C451 (= C528) binding [4Fe-4S] cluster
- R474 (= R558) binding substrate
- R479 (= R563) binding substrate
- R607 (= R735) binding substrate
- SR 670:671 (= SR 802:803) binding substrate
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 37:745/754 of 5acnA
- active site: D100 (= D123), H101 (= H124), D165 (= D208), R447 (= R558), S642 (= S801), R644 (= R803)
- binding fe3-s4 cluster: I145 (= I174), H147 (= H176), H167 (= H210), C358 (= C459), C421 (= C525), C424 (= C528), N446 (= N557)
- binding tricarballylic acid: K198 (≠ L241), G235 (= G278), R666 (= R825)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
26% identity, 93% coverage: 52:906/917 of query aligns to 64:772/781 of P16276
- Q99 (= Q84) binding substrate
- DSH 192:194 (= DSH 208:210) binding substrate
- C385 (= C459) binding [4Fe-4S] cluster
- C448 (= C525) binding [4Fe-4S] cluster
- C451 (= C528) binding [4Fe-4S] cluster
- R474 (= R558) binding substrate
- R479 (= R563) binding substrate
- R607 (= R735) binding substrate
- SR 670:671 (= SR 802:803) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
26% identity, 93% coverage: 52:906/917 of query aligns to 36:744/753 of 1b0kA
- active site: D99 (= D123), H100 (= H124), D164 (= D208), R446 (= R558), A641 (≠ S801), R643 (= R803)
- binding citrate anion: Q71 (= Q84), H100 (= H124), D164 (= D208), S165 (= S209), R446 (= R558), R451 (= R563), R579 (= R735), A641 (≠ S801), S642 (= S802), R643 (= R803)
- binding oxygen atom: D164 (= D208), H166 (= H210)
- binding iron/sulfur cluster: H100 (= H124), D164 (= D208), H166 (= H210), S356 (= S458), C357 (= C459), C420 (= C525), C423 (= C528)
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, 44% coverage: 203:610/917 of query aligns to 135:492/758 of O14289
- S486 (≠ N604) modified: Phosphoserine
- S488 (≠ V606) modified: Phosphoserine
Query Sequence
>WP_077243786.1 NCBI__GCF_001995255.1:WP_077243786.1
MSDAMPRNTRTLSAGGHECQYVPIADDRRAQTLPFALKVLLENLMRHEDGRTVTRDDIEG
LLDWDPAAEPSREIAFRPARVLLQDFTGVPAVVDLAAMRDAMEDLGGDPAKIAPLQPAEL
VIDHSVQVDSYGEANSMNLNAELEYSRNRERYSFLKWGQQAFETFKVVPPDTGIVHQVNL
EYLARTVFLEDRADGSCMAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQPISM
LIPQVVGFRLTGKLAEGATATDLVLVIVEQLRKHGVVGKFVEFFGDGLADLPLADRATIA
NMAPEYGATCGIFPIDDETLEYLRLTGREESHIQFIEAYARGQGLWRDDSAPVARYSDLL
ELDLSTVEPSLAGPKRPQDRIPLSQAGAEISRHLDTVLKERVSGKDEPSEAERFATEGGH
TAVGVEHQAEEPHHTAIEMGGETFTLDHGDVVIAAITSCTNTSNPSVMLGAGLVARKARE
RGLKVKPWVKTSLAPGSRVVTDYLQNAGLLEDLEDLGFYVVGYGCTTCIGNSGPLPEAIS
EAIVKDDLVVSSVLSGNRNFEGRIHSEVQMNFLASPPLVVAYALAGRSNLDLYNDPLGDD
ADGNPVYLKDIWPTSQEVRDEVARHVGAGSFTTAYGDLYTGENRWRNLEAPSGDRFDWQE
DSTYVRKPPYFDGMGMTPAETPDIEGARVLALLGDSVTTDHISPAGSIASDSPAARYLEE
QGVKPADFNSYGSRRGNHEVMMRGTFANVRLRNLLAPGTQGGVTRHLPDGEQMSIYDASM
RYQAEGTPLVVIAGKEYGTGSSRDWAAKGTLLLGVKAVIVESYERIHRSNLVGMGVLPLQ
FHDGENAESLGLTGEETYTITGIRSGEAKEATVTATADDGSRKEFRVRVRLDTPQEIDYY
RHGGILPYVLRQLAGEG
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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