SitesBLAST
Comparing WP_011912997.1 NCBI__GCF_000013785.1:WP_011912997.1 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)
57% identity, 99% coverage: 5:887/891 of query aligns to 11:904/909 of P09339
- C450 (= C433) 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 (= R723) 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)
58% identity, 100% coverage: 3:889/891 of query aligns to 2:929/931 of D9X0I3
- SVIAD 125:129 (≠ SVMVD 130:134) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C499) 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 (= R723) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ E727) 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)
56% identity, 100% coverage: 3:891/891 of query aligns to 10:941/943 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)
56% identity, 98% coverage: 17:888/891 of query aligns to 112:987/990 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: 37:888/891 of query aligns to 34:887/889 of P21399
- C300 (≠ A307) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ D325) to M: in dbSNP:rs150373174
- C437 (= C433) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C499) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C502) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R532) mutation to Q: Strongly reduced RNA binding.
- R541 (= R537) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ L694) mutation to K: No effect on RNA binding.
- S778 (= S774) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R776) 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: 37:888/891 of query aligns to 33:886/888 of 2b3xA
- active site: D124 (= D128), H125 (= H129), D204 (= D212), R535 (= R532), S777 (= S774), R779 (= R776)
- binding iron/sulfur cluster: I175 (= I179), H206 (= H214), C436 (= C433), C502 (= C499), C505 (= C502), I506 (= I503), N534 (= N531)
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
52% identity, 96% coverage: 37:888/891 of query aligns to 33:848/850 of 3snpA
- active site: D124 (= D128), H125 (= H129), D186 (= D212), R505 (= R532), S739 (= S774), R741 (= R776)
- binding : H125 (= H129), S126 (= S130), H188 (= H214), L243 (= L269), R250 (= R276), N279 (= N305), E283 (= E309), S352 (≠ A376), P357 (= P381), K360 (≠ R384), T419 (= T434), N420 (= N435), T421 (= T436), N504 (= N531), R505 (= R532), L520 (= L547), S642 (= S676), P643 (= P677), A644 (= A678), G645 (= G679), N646 (= N680), R649 (≠ A683), R665 (≠ E699), S669 (= S703), G671 (= G705), R674 (= R708), R741 (= R776)
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)
28% identity, 90% coverage: 79:884/891 of query aligns to 85:772/778 of P19414
- R604 (≠ L694) 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)
27% identity, 90% coverage: 79:882/891 of query aligns to 61:745/753 of 8acnA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R532), S641 (= S774), R643 (= R776)
- binding nitroisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R532), R451 (= R537), R579 (= R716), S641 (= S774), S642 (= S775), R643 (= R776)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S432), C357 (= C433), C420 (= C499), C423 (= C502), I424 (= I503)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
27% identity, 90% coverage: 79:882/891 of query aligns to 61:745/753 of 1fghA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R532), S641 (= S774), R643 (= R776)
- binding 4-hydroxy-aconitate ion: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R532), R451 (= R537), R579 (= R716), S641 (= S774), S642 (= S775), R643 (= R776)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S432), C357 (= C433), C420 (= C499), C423 (= C502), I424 (= I503), R451 (= R537)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 90% coverage: 79:882/891 of query aligns to 61:745/753 of 1amjA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R532), S641 (= S774), R643 (= R776)
- binding iron/sulfur cluster: I144 (= I179), H166 (= H214), C357 (= C433), C420 (= C499), C423 (= C502)
- binding sulfate ion: Q71 (= Q89), R579 (= R716), R643 (= R776)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 90% coverage: 79:882/891 of query aligns to 61:745/753 of 1amiA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R532), S641 (= S774), R643 (= R776)
- binding alpha-methylisocitric acid: Q71 (= Q89), T74 (= T92), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R532), R451 (= R537), R579 (= R716), S641 (= S774), S642 (= S775), R643 (= R776)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D212), H166 (= H214), S356 (= S432), C357 (= C433), C420 (= C499), C423 (= C502), N445 (= N531)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
27% identity, 90% coverage: 79:882/891 of query aligns to 61:745/753 of 1acoA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R532), S641 (= S774), R643 (= R776)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), D164 (= D212), H166 (= H214), S356 (= S432), C357 (= C433), C420 (= C499), C423 (= C502), N445 (= N531)
- binding aconitate ion: Q71 (= Q89), D164 (= D212), S165 (= S213), R446 (= R532), R451 (= R537), R579 (= R716), S641 (= S774), S642 (= S775), R643 (= R776)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
27% identity, 90% coverage: 79:882/891 of query aligns to 62:746/754 of 5acnA
- active site: D100 (= D128), H101 (= H129), D165 (= D212), R447 (= R532), S642 (= S774), R644 (= R776)
- binding fe3-s4 cluster: I145 (= I179), H147 (= H181), H167 (= H214), C358 (= C433), C421 (= C499), C424 (= C502), N446 (= N531)
- binding tricarballylic acid: K198 (≠ L245), G235 (= G282), R666 (= R798)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
27% identity, 90% coverage: 79:882/891 of query aligns to 61:745/753 of 1nisA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R532), S641 (= S774), R643 (= R776)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q89), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R532), R451 (= R537), R579 (= R716), S641 (= S774), S642 (= S775)
- binding iron/sulfur cluster: H100 (= H129), I144 (= I179), H166 (= H214), S356 (= S432), C357 (= C433), C420 (= C499), C423 (= C502)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
27% identity, 90% coverage: 79:882/891 of query aligns to 89:773/780 of P20004
- Q99 (= Q89) binding substrate
- DSH 192:194 (= DSH 212:214) binding substrate
- C385 (= C433) binding [4Fe-4S] cluster
- C448 (= C499) binding [4Fe-4S] cluster
- C451 (= C502) binding [4Fe-4S] cluster
- R474 (= R532) binding substrate
- R479 (= R537) binding substrate
- R607 (= R716) binding substrate
- SR 670:671 (= SR 775:776) binding substrate
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
27% identity, 90% coverage: 79:882/891 of query aligns to 61:745/753 of 1b0kA
- active site: D99 (= D128), H100 (= H129), D164 (= D212), R446 (= R532), A641 (≠ S774), R643 (= R776)
- binding citrate anion: Q71 (= Q89), H100 (= H129), D164 (= D212), S165 (= S213), R446 (= R532), R451 (= R537), R579 (≠ N702), A641 (≠ S774), S642 (= S775), R643 (= R776)
- binding oxygen atom: D164 (= D212), H166 (= H214)
- binding iron/sulfur cluster: H100 (= H129), D164 (= D212), H166 (= H214), S356 (= S432), C357 (= C433), C420 (= C499), C423 (= C502)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
27% identity, 90% coverage: 79:882/891 of query aligns to 89:773/781 of P16276
- Q99 (= Q89) binding substrate
- DSH 192:194 (= DSH 212:214) binding substrate
- C385 (= C433) binding [4Fe-4S] cluster
- C448 (= C499) binding [4Fe-4S] cluster
- C451 (= C502) binding [4Fe-4S] cluster
- R474 (= R532) binding substrate
- R479 (= R537) binding substrate
- R607 (= R716) binding substrate
- SR 670:671 (= SR 775:776) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 96% coverage: 27:884/891 of query aligns to 43:782/789 of P39533
- K610 (≠ R716) 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)
26% identity, 37% coverage: 207:537/891 of query aligns to 135:448/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_011912997.1 NCBI__GCF_000013785.1:WP_011912997.1
MPSLDSLKCRRSLEVAGKTYHYYSLPDAAAQLGDISRLPTSLKVLLENLLRWEDDVTVRS
DDLRSLVSWLQTRSSDQEIQYRPARVLMQDFTGVPAVVDLAAMRDAVARAGGDPQKINPL
SPVDLVIDHSVMVDRFGSDQAFEQNVEIEMQRNGERYEFLRWGQQAFDNFSVVPPGTGIC
HQVNLEYLGQVVWTREENGETVAYPDTLVGTDSHTTMINGLGVLGWGVGGIEAEAAMLGQ
PVSMLIPEVIGFRLSGKLNEGVTATDLVLTVTQMLRKHGVVGKFVEFYGPGLDHLPLADR
ATIGNMAPEYGATCGFFPVDQITIDYLRLTGRNEERIALVEAYSKAQGMWRDSNSPDPVF
TATLELDLAQVQPSVAGPKRPQDRVTLGDIGANFDLLLETGGRKQQADTSVEVKGENFHL
KHGAVVIAAITSCTNTSNPNVLMAAGLVAKKAVERGLKRQPWVKSSLAPGSKVVTDYLER
AGLTRYLDQLGFNLVGYGCTTCIGNSGPLPDAIGQAITDNDLIVSSVLSGNRNFEGRVHP
LVKANWLASPPLVVAFALAGTTRINMDREPLGYDDQNQPVYLKDIWPSSAEIAEAVARID
GEMFRSRYADVFSGDEHWQKIPVSAGDTYQWNASSSYVQNPPYFEDIGQPPAPPADVENA
RVLAVFGDSITTDHISPAGNIKASSPAGLYLQSLGVAPEDFNSYGSRRGNHEVMMRGTFA
NIRIKNEMLGGEEGGNTLYQPSGEKLSIYDAAMRYQAEDVPLVVIAGKEYGTGSSRDWAA
KGTNLLGVKAVIAESFERIHRSNLIGMGVLALQFVGEQTRQSLGLNGTEKLSIRGLGADI
KPRQLLTVDVERQDGSRDSFQVLSRIDTLNEVQYFKAGGILHYVLRQLIGS
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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