SitesBLAST
Comparing WP_043529276.1 NCBI__GCF_000759345.1:WP_043529276.1 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)
59% identity, 100% coverage: 1:911/914 of query aligns to 1:929/931 of D9X0I3
- SVIAD 125:129 (≠ SVMVD 130:134) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C523) 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 (= R747) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ E751) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
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)
57% identity, 98% coverage: 12:909/914 of query aligns to 18:904/909 of P09339
- C450 (= C457) 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 (= R747) 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
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)
57% identity, 99% coverage: 12:914/914 of query aligns to 19:942/943 of A0QX20
- K394 (≠ N395) 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)
55% identity, 97% coverage: 22:910/914 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)
53% identity, 96% coverage: 37:910/914 of query aligns to 34:887/889 of P21399
- C300 (≠ A307) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ N325) to M: in dbSNP:rs150373174
- C437 (= C457) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C523) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C526) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R556) mutation to Q: Strongly reduced RNA binding.
- R541 (= R561) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ H718) mutation to K: No effect on RNA binding.
- S778 (= S798) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R800) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
53% identity, 96% coverage: 37:910/914 of query aligns to 33:886/888 of 2b3xA
- active site: D124 (= D128), H125 (= H129), D204 (= D212), R535 (= R556), S777 (= S798), R779 (= R800)
- binding iron/sulfur cluster: I175 (= I179), H206 (= H214), C436 (= C457), C502 (= C523), C505 (= C526), I506 (= I527), N534 (= N555)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
52% identity, 96% coverage: 37:910/914 of query aligns to 33:848/850 of 3snpA
- active site: D124 (= D128), H125 (= H129), D186 (= D212), R505 (= R556), S739 (= S798), R741 (= R800)
- binding : H125 (= H129), S126 (= S130), H188 (= H214), L243 (= L269), R250 (= R276), N279 (= N305), E283 (= E309), S352 (≠ A375), P357 (= P380), K360 (≠ R383), T419 (= T458), N420 (= N459), T421 (= T460), N504 (= N555), R505 (= R556), L520 (= L571), S642 (= S700), P643 (= P701), A644 (= A702), G645 (= G703), N646 (≠ A704), R649 (≠ P707), R665 (≠ M723), S669 (= S727), G671 (= G729), R674 (= R732), R741 (= R800)
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)
26% identity, 92% coverage: 70:906/914 of query aligns to 76:772/778 of P19414
- R604 (≠ H718) 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
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
27% identity, 91% coverage: 70:904/914 of query aligns to 80:773/780 of P20004
- Q99 (= Q89) binding substrate
- DSH 192:194 (= DSH 212:214) binding substrate
- C385 (= C457) binding [4Fe-4S] cluster
- C448 (= C523) binding [4Fe-4S] cluster
- C451 (= C526) binding [4Fe-4S] cluster
- R474 (= R556) binding substrate
- R479 (= R561) binding substrate
- R607 (= R740) binding substrate
- SR 670:671 (= SR 799:800) binding substrate
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 53:746/754 of 5acnA
- active site: D100 (= D128), H101 (= H129), D165 (= D212), R447 (= R556), S642 (= S798), R644 (= R800)
- binding fe3-s4 cluster: I145 (= I179), H147 (= H181), H167 (= H214), C358 (= C457), C421 (= C523), C424 (= C526), N446 (= N555)
- binding tricarballylic acid: K198 (≠ L245), G235 (= G282), R666 (= R822)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 52:745/753 of 1b0kA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R556), A641 (≠ S798), R643 (= R800)
- binding citrate anion: Q71 (= Q89), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R556), R451 (= R561), R579 (≠ N726), A641 (≠ S798), S642 (= S799), R643 (= R800)
- binding oxygen atom: D164 (= D212), H166 (= H214)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S456), C357 (= C457), C420 (= C523), C423 (= C526)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 52:745/753 of 8acnA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R556), S641 (= S798), R643 (= R800)
- binding nitroisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R556), R451 (= R561), R579 (= R740), S641 (= S798), S642 (= S799), R643 (= R800)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S456), C357 (= C457), C420 (= C523), C423 (= C526), I424 (= I527)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 52:745/753 of 1fghA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R556), S641 (= S798), R643 (= R800)
- binding 4-hydroxy-aconitate ion: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R556), R451 (= R561), R579 (= R740), S641 (= S798), S642 (= S799), R643 (= R800)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S456), C357 (= C457), C420 (= C523), C423 (= C526), I424 (= I527), R451 (= R561)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 52:745/753 of 1amjA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R556), S641 (= S798), R643 (= R800)
- binding iron/sulfur cluster: I144 (= I179), H166 (= H214), C357 (= C457), C420 (= C523), C423 (= C526)
- binding sulfate ion: Q71 (= Q89), R579 (= R740), R643 (= R800)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 52:745/753 of 1amiA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R556), S641 (= S798), R643 (= R800)
- binding alpha-methylisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R556), R451 (= R561), R579 (= R740), S641 (= S798), S642 (= S799), R643 (= R800)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D212), H166 (= H214), S356 (= S456), C357 (= C457), C420 (= C523), C423 (= C526), N445 (= N555)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 52:745/753 of 1acoA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R556), S641 (= S798), R643 (= R800)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D212), H166 (= H214), S356 (= S456), C357 (= C457), C420 (= C523), C423 (= C526), N445 (= N555)
- binding aconitate ion: Q71 (= Q89), D164 (= D212), S165 (= S213), R446 (= R556), R451 (= R561), R579 (= R740), S641 (= S798), S642 (= S799), R643 (= R800)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
27% identity, 91% coverage: 70:904/914 of query aligns to 80:773/781 of P16276
- Q99 (= Q89) binding substrate
- DSH 192:194 (= DSH 212:214) binding substrate
- C385 (= C457) binding [4Fe-4S] cluster
- C448 (= C523) binding [4Fe-4S] cluster
- C451 (= C526) binding [4Fe-4S] cluster
- R474 (= R556) binding substrate
- R479 (= R561) binding substrate
- R607 (≠ N726) binding substrate
- SR 670:671 (= SR 799:800) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
27% identity, 91% coverage: 70:904/914 of query aligns to 52:745/753 of 1nisA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R556), S641 (= S798), R643 (= R800)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q89), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R556), R451 (= R561), R579 (= R740), S641 (= S798), S642 (= S799)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), H166 (= H214), S356 (= S456), C357 (= C457), C420 (= C523), C423 (= C526)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 93% coverage: 55:906/914 of query aligns to 69:782/789 of P39533
- K610 (≠ H718) 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)
25% identity, 45% coverage: 200:608/914 of query aligns to 127:492/758 of O14289
- S486 (≠ K602) modified: Phosphoserine
- S488 (≠ V604) modified: Phosphoserine
Query Sequence
>WP_043529276.1 NCBI__GCF_000759345.1:WP_043529276.1
MSADSAPNTLASLTVGEREYHYYSLPKAAEALGDIQRLPVTLKILLENQLRFADDESVSR
EDMQALVDWQQEARSTREIGYRPARVLMQDFTGVPGVVDLASMRAAVEKLGEDPSRINPL
SPVDLVIDHSVMVDKYGDPSAFRDNVAIEMDRNRERYEFLRWGQDAFDNFRVVPPGTGIC
HQVNLEYLGKTVWVKEEDGKSFAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ
PVSMLIPEVVGFKLTGKLREGITATDLVLTVTQMLRQKGVVGKFVEFYGDGLDDLPLADR
ATIANMAPEYGATCGFFPVDDETLNYLRLTGRSDEEVALVEAYCKEQDLWRKPGAEPVFS
DTLQLDMGDVEASLAGPKRPQDRVALSDMKSTFENLMGDDAAEASATARGKFDSEGGQMP
VGTHEHFEHHDSQDVDVEGSTFKLNPGAVVIAAITSCTNTSNPSVMMAAGLLARKAVEKG
LDTKPWVKTSLAPGSKVVTDYLAAGGFQDDLNALGFNLVGYGCTTCIGNSGPLLPPIEKA
IEDGDLTVASVLSGNRNFEGRVHPLVKTNWLASPPLVVAYALAGNVRLDISKEPLGEGKD
GKPVYLQDIWPSQAEIAEAVEKVRTEMYRKEYAEVFEGDEVWKAIDVPQSQVYQWSEDST
YIQHPPFFEGMGREPEPLQDVENARVLAMLGDSVTTDHISPAGAIKPDSPAGRYLQEHGV
KPMDFNSYGSRRGNHEVMMRGTFANVRIRNEMLDGVEGGYTRHVPSDEQMAIYDAAMKYA
EEGRPLVVIAGKEYGTGSSRDWAAKGTRLLGVRAVLAESYERIHRSNLIGMGVVPLQFPE
GEDRKSLGLTGDEEVSIDGIADLTPGGQVNVTIKSDKGEKKIEALCRIDTANELEYYRHG
GILHYVLRKMIGSA
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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