SitesBLAST
Comparing WP_015886895.1 NCBI__GCF_000018545.1:WP_015886895.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
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)
45% identity, 96% coverage: 29:869/880 of query aligns to 42:909/909 of P09339
- C450 (= C414) 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 (≠ T701) 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)
45% identity, 96% coverage: 21:865/880 of query aligns to 120:987/990 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)
44% identity, 95% coverage: 31:862/880 of query aligns to 34:884/889 of P21399
- C300 (≠ T299) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ K317) to M: in dbSNP:rs150373174
- C437 (= C414) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C480) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C483) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R513) mutation to Q: Strongly reduced RNA binding.
- R541 (= R518) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H672) mutation to K: No effect on RNA binding.
- S778 (= S751) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R753) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
44% identity, 95% coverage: 31:862/880 of query aligns to 33:883/888 of 2b3xA
- active site: D124 (= D120), H125 (= H121), D204 (= D204), R535 (= R513), S777 (= S751), R779 (= R753)
- binding iron/sulfur cluster: I175 (= I171), H206 (= H206), C436 (= C414), C502 (= C480), C505 (= C483), I506 (= I484), N534 (= N512)
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)
44% identity, 95% coverage: 31:869/880 of query aligns to 40:942/943 of A0QX20
- K394 (≠ Q383) 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)
44% identity, 95% coverage: 27:866/880 of query aligns to 28:929/931 of D9X0I3
- SVIAD 125:129 (≠ SVGVD 122:126) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C480) 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 (≠ T701) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ M705) 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)
42% identity, 95% coverage: 31:862/880 of query aligns to 33:845/850 of 3snpA
- active site: D124 (= D120), H125 (= H121), D186 (= D204), R505 (= R513), S739 (= S751), R741 (= R753)
- binding : H125 (= H121), S126 (= S122), H188 (= H206), L243 (= L261), R250 (= R268), N279 (= N297), E283 (= E301), S352 (≠ A367), P357 (= P372), K360 (≠ R375), T419 (= T415), N420 (= N416), T421 (= T417), N504 (= N512), R505 (= R513), L520 (= L528), S642 (= S654), P643 (= P655), A644 (= A656), G645 (= G657), N646 (≠ A658), R649 (≠ A661), R665 (≠ T677), S669 (≠ V681), G671 (≠ A683), R674 (= R686), R741 (= R753)
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, 88% coverage: 62:833/880 of query aligns to 78:745/778 of P19414
- R604 (≠ A665) 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)
28% identity, 94% coverage: 34:858/880 of query aligns to 14:744/753 of 8acnA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R513), S641 (= S751), R643 (= R753)
- binding nitroisocitric acid: Q71 (≠ H81), T74 (= T84), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R513), R451 (= R518), R579 (= R694), S641 (= S751), S642 (= S752), R643 (= R753)
- binding iron/sulfur cluster: H100 (= H121), D164 (= D204), H166 (= H206), S356 (= S413), C357 (= C414), C420 (= C480), C423 (= C483), I424 (= I484)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 94% coverage: 34:858/880 of query aligns to 14:744/753 of 1fghA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R513), S641 (= S751), R643 (= R753)
- binding 4-hydroxy-aconitate ion: Q71 (≠ H81), T74 (= T84), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R513), R451 (= R518), R579 (= R694), S641 (= S751), S642 (= S752), R643 (= R753)
- binding iron/sulfur cluster: H100 (= H121), D164 (= D204), H166 (= H206), S356 (= S413), C357 (= C414), C420 (= C480), C423 (= C483), I424 (= I484), R451 (= R518)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 94% coverage: 34:858/880 of query aligns to 14:744/753 of 1amjA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R513), S641 (= S751), R643 (= R753)
- binding iron/sulfur cluster: I144 (= I171), H166 (= H206), C357 (= C414), C420 (= C480), C423 (= C483)
- binding sulfate ion: Q71 (≠ H81), R579 (= R694), R643 (= R753)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 94% coverage: 34:858/880 of query aligns to 14:744/753 of 1amiA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R513), S641 (= S751), R643 (= R753)
- binding alpha-methylisocitric acid: Q71 (≠ H81), T74 (= T84), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R513), R451 (= R518), R579 (= R694), S641 (= S751), S642 (= S752), R643 (= R753)
- binding iron/sulfur cluster: H100 (= H121), I144 (= I171), D164 (= D204), H166 (= H206), S356 (= S413), C357 (= C414), C420 (= C480), C423 (= C483), N445 (= N512)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 94% coverage: 34:858/880 of query aligns to 14:744/753 of 1acoA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R513), S641 (= S751), R643 (= R753)
- binding iron/sulfur cluster: H100 (= H121), I144 (= I171), D164 (= D204), H166 (= H206), S356 (= S413), C357 (= C414), C420 (= C480), C423 (= C483), N445 (= N512)
- binding aconitate ion: Q71 (≠ H81), D164 (= D204), S165 (= S205), R446 (= R513), R451 (= R518), R579 (= R694), S641 (= S751), S642 (= S752), R643 (= R753)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 94% coverage: 34:858/880 of query aligns to 14:744/753 of 1nisA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R513), S641 (= S751), R643 (= R753)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (≠ H81), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R513), R451 (= R518), R579 (= R694), S641 (= S751), S642 (= S752)
- binding iron/sulfur cluster: H100 (= H121), I144 (= I171), H166 (= H206), S356 (= S413), C357 (= C414), C420 (= C480), C423 (= C483)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 94% coverage: 34:858/880 of query aligns to 15:745/754 of 5acnA
- active site: D100 (= D120), H101 (= H121), D165 (= D204), R447 (= R513), S642 (= S751), R644 (= R753)
- binding fe3-s4 cluster: I145 (= I171), H147 (= H173), H167 (= H206), C358 (= C414), C421 (= C480), C424 (= C483), N446 (= N512)
- binding tricarballylic acid: K198 (≠ R237), G235 (≠ D274), R666 (= R775)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
27% identity, 90% coverage: 75:863/880 of query aligns to 90:784/789 of P39533
- K610 (≠ R686) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 94% coverage: 34:858/880 of query aligns to 42:772/780 of P20004
- Q99 (≠ H81) binding substrate
- DSH 192:194 (= DSH 204:206) binding substrate
- C385 (= C414) binding [4Fe-4S] cluster
- C448 (= C480) binding [4Fe-4S] cluster
- C451 (= C483) binding [4Fe-4S] cluster
- R474 (= R513) binding substrate
- R479 (= R518) binding substrate
- R607 (= R694) binding substrate
- SR 670:671 (= SR 752:753) binding substrate
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 94% coverage: 34:858/880 of query aligns to 14:744/753 of 1b0kA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R513), A641 (≠ S751), R643 (= R753)
- binding citrate anion: Q71 (≠ H81), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R513), R451 (= R518), R579 (= R694), A641 (≠ S751), S642 (= S752), R643 (= R753)
- binding oxygen atom: D164 (= D204), H166 (= H206)
- binding iron/sulfur cluster: H100 (= H121), D164 (= D204), H166 (= H206), S356 (= S413), C357 (= C414), C420 (= C480), C423 (= C483)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 94% coverage: 34:858/880 of query aligns to 42:772/781 of P16276
- Q99 (≠ H81) binding substrate
- DSH 192:194 (= DSH 204:206) binding substrate
- C385 (= C414) binding [4Fe-4S] cluster
- C448 (= C480) binding [4Fe-4S] cluster
- C451 (= C483) binding [4Fe-4S] cluster
- R474 (= R513) binding substrate
- R479 (= R518) binding substrate
- R607 (= R694) binding substrate
- SR 670:671 (= SR 752:753) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
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)
25% identity, 36% coverage: 199:518/880 of query aligns to 135:448/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_015886895.1 NCBI__GCF_000018545.1:WP_015886895.1
MPATKLAHLGVNGVDHTIIDLPAEAGEALARLPYIHRVLLENALRTAGDDAALAKEAILG
WLDRGTSEQEIPFLPNRVLMHDTTCGPALVDIAGMRSALAEAGGDPALLNPVVPVDVSTD
HSVGVDFFGQTGSLEKNMEREFERNAERYRFMKWATNTMSGFTAHPPGTGIMHTLNLERL
ATVATSKLIDGVLWAMPDTLIGTDSHTPMINGIGVLAWGVGGLEAESVFFGMPVTLRVPD
VVGVKLTGALKSGVLATDLALTLTEQLRKIDLQDRYVEFFGPGVSTLTAGDRGVVANMTP
EFGGNSGYFPIDAQTLKYLEATGRSLTQVAFVEAYARRAGLWFDPQTDPRYTLVVELDLS
SVEVSLAGPTRPQDRIAAGATLQAIKPMIEARDQDERTGRPEGGAVAIAAITSCTNTSDP
RLVVAAGLMARKARALGLKPPHWVKTSLAPGSPTAERYLRRAGLLEDLEAVGFGIVGYGC
TTCIGNSGPLTAPIAAAMEERGIVPVAVLSGNRNFPGRVHPQLEAGFLASPPLVVAFALA
GTVKLDILTDPIGTTADGRSITLSMLWPTSAEIDEVLALASSADDFKPAYDAAEASRVWG
ALDAPTTTLFPWDPRSTYIRRPAFAGFGDGTLLGCYEAHPLLVLGDDITTDHISPAGAIP
ASGAAGRYLIEHGENPTDLNVFASRRGNWEVMVRGLFTNKTVTNMLGDVPPGSTIHAPSG
DILPLLDAARRYRAAGQSVVVVAGERYGMGSSRDWAAKGVSLLGTRAVLALSFERIHRSN
LIGMGVLPLRLPAQFGPERLHLEPGDLIAISASPEAILPRSPVAVTIRRKDGSSFSFEAS
AAIETNVEMRTLRAGGILPYILNDVLNSSGKAKRADGDFQ
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