SitesBLAST
Comparing WP_011020308.1 NCBI__GCF_000007345.1:WP_011020308.1 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)
56% identity, 99% coverage: 6:932/933 of query aligns to 11:908/909 of P09339
- C450 (= C466) 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 (= R757) 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, 96% coverage: 37:932/933 of query aligns to 128:990/990 of Q9SIB9
Sites not aligning to the query:
- 91 modified: Phosphoserine
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)
53% identity, 100% coverage: 2:933/933 of query aligns to 8:942/943 of A0QX20
- K394 (≠ E400) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)
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, 97% coverage: 23:931/933 of query aligns to 21:889/889 of P21399
- C300 (≠ A311) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ N329) to M: in dbSNP:rs150373174
- C437 (= C466) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C532) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C535) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R565) mutation to Q: Strongly reduced RNA binding.
- R541 (= R570) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ W728) mutation to K: No effect on RNA binding.
- S778 (= S816) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R818) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
53% identity, 97% coverage: 23:931/933 of query aligns to 20:888/888 of 2b3xA
- active site: D124 (= D132), H125 (= H133), D204 (= D216), R535 (= R565), S777 (= S816), R779 (= R818)
- binding iron/sulfur cluster: I175 (= I183), H206 (= H218), C436 (= C466), C502 (= C532), C505 (= C535), I506 (= I536), N534 (= N564)
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)
54% identity, 99% coverage: 6:932/933 of query aligns to 4:931/931 of D9X0I3
- SVIAD 125:129 (≠ SVQVD 134:138) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C532) 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 (= R757) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ R761) 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)
51% identity, 97% coverage: 23:931/933 of query aligns to 20:850/850 of 3snpA
- active site: D124 (= D132), H125 (= H133), D186 (= D216), R505 (= R565), S739 (= S816), R741 (= R818)
- binding : H125 (= H133), S126 (= S134), H188 (= H218), L243 (= L273), R250 (= R280), N279 (= N309), E283 (= E313), S352 (≠ A380), P357 (= P385), K360 (≠ Q388), T419 (= T467), N420 (= N468), T421 (= T469), N504 (= N564), R505 (= R565), L520 (= L580), S642 (= S710), P643 (= P711), A644 (= A712), G645 (= G713), N646 (≠ D714), R649 (≠ A717), R665 (≠ K733), S669 (= S737), G671 (= G739), R674 (= R742), R741 (= R818)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 50:748/754 of 5acnA
- active site: D100 (= D132), H101 (= H133), D165 (= D216), R447 (= R565), S642 (= S816), R644 (= R818)
- binding fe3-s4 cluster: I145 (= I183), H147 (= H185), H167 (= H218), C358 (= C466), C421 (= C532), C424 (= C535), N446 (= N564)
- binding tricarballylic acid: K198 (≠ P249), G235 (= G286), R666 (= R840)
P20004 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Bos taurus (Bovine) (see 2 papers)
28% identity, 91% coverage: 75:925/933 of query aligns to 77:775/780 of P20004
- Q99 (= Q93) binding substrate
- DSH 192:194 (= DSH 216:218) binding substrate
- C385 (= C466) binding [4Fe-4S] cluster
- C448 (= C532) binding [4Fe-4S] cluster
- C451 (= C535) binding [4Fe-4S] cluster
- R474 (= R565) binding substrate
- R479 (= R570) binding substrate
- R607 (= R750) binding substrate
- SR 670:671 (= SR 817:818) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 49:747/753 of 8acnA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R565), S641 (= S816), R643 (= R818)
- binding nitroisocitric acid: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R565), R451 (= R570), R579 (= R750), S641 (= S816), S642 (= S817), R643 (= R818)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D216), H166 (= H218), S356 (= S465), C357 (= C466), C420 (= C532), C423 (= C535), I424 (= I536)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 49:747/753 of 1fghA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R565), S641 (= S816), R643 (= R818)
- binding 4-hydroxy-aconitate ion: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R565), R451 (= R570), R579 (= R750), S641 (= S816), S642 (= S817), R643 (= R818)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D216), H166 (= H218), S356 (= S465), C357 (= C466), C420 (= C532), C423 (= C535), I424 (= I536), R451 (= R570)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 49:747/753 of 1amjA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R565), S641 (= S816), R643 (= R818)
- binding iron/sulfur cluster: I144 (= I183), H166 (= H218), C357 (= C466), C420 (= C532), C423 (= C535)
- binding sulfate ion: Q71 (= Q93), R579 (= R750), R643 (= R818)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 49:747/753 of 1amiA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R565), S641 (= S816), R643 (= R818)
- binding alpha-methylisocitric acid: Q71 (= Q93), T74 (= T96), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R565), R451 (= R570), R579 (= R750), S641 (= S816), S642 (= S817), R643 (= R818)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), D164 (= D216), H166 (= H218), S356 (= S465), C357 (= C466), C420 (= C532), C423 (= C535), N445 (= N564)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 49:747/753 of 1acoA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R565), S641 (= S816), R643 (= R818)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), D164 (= D216), H166 (= H218), S356 (= S465), C357 (= C466), C420 (= C532), C423 (= C535), N445 (= N564)
- binding aconitate ion: Q71 (= Q93), D164 (= D216), S165 (= S217), R446 (= R565), R451 (= R570), R579 (= R750), S641 (= S816), S642 (= S817), R643 (= R818)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 49:747/753 of 1b0kA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R565), A641 (≠ S816), R643 (= R818)
- binding citrate anion: Q71 (= Q93), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R565), R451 (= R570), R579 (= R750), A641 (≠ S816), S642 (= S817), R643 (= R818)
- binding oxygen atom: D164 (= D216), H166 (= H218)
- binding iron/sulfur cluster: H100 (= H133), D164 (= D216), H166 (= H218), S356 (= S465), C357 (= C466), C420 (= C532), C423 (= C535)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
27% identity, 91% coverage: 75:925/933 of query aligns to 49:747/753 of 1nisA
- active site: D99 (= D132), H100 (= H133), D164 (= D216), R446 (= R565), S641 (= S816), R643 (= R818)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q93), H100 (= H133), D164 (= D216), S165 (= S217), R446 (= R565), R451 (= R570), R579 (= R750), S641 (= S816), S642 (= S817)
- binding iron/sulfur cluster: H100 (= H133), I144 (= I183), H166 (= H218), S356 (= S465), C357 (= C466), C420 (= C532), C423 (= C535)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
27% identity, 91% coverage: 75:925/933 of query aligns to 77:775/781 of P16276
- Q99 (= Q93) binding substrate
- DSH 192:194 (= DSH 216:218) binding substrate
- C385 (= C466) binding [4Fe-4S] cluster
- C448 (= C532) binding [4Fe-4S] cluster
- C451 (= C535) binding [4Fe-4S] cluster
- R474 (= R565) binding substrate
- R479 (= R570) binding substrate
- R607 (= R750) binding substrate
- SR 670:671 (= SR 817:818) 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, 88% coverage: 87:904/933 of query aligns to 90:750/789 of P39533
- K610 (≠ R750) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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, 39% coverage: 21:385/933 of query aligns to 20:352/778 of P19414
Sites not aligning to the query:
- 1:16 modified: transit peptide, Mitochondrion
- 604 R→K: Strongly diminishes the catalytic activity towards both known substrates, aconitate and homoaconitate.
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)
27% identity, 42% coverage: 206:593/933 of query aligns to 129:470/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_011020308.1 NCBI__GCF_000007345.1:WP_011020308.1
MREGLDPFGVRDSIETTAGKATIYRLSKLEEKGFEGISLLPYSIRILLESLLRHADTEKH
LIAAEDVEALARWSPGNRIERDIPFIPSRVIMQDFTGVPAVVDLAALRSAMERLEGDPAK
INPVIPADLVIDHSVQVDSYGTAYALEENEKKEFERNRERYIVLRWAQKAFDNFRVVPPG
RGIIHQVNLEYLTPLVHLKEKEGELFAFPDTLVGTDSHTTMINGIGVLGWGVGGIEAEAV
MLGQPYYMPVPEVVGFKLYGKLEPGVTATDLVLTITKMLRKQGVVGKFVEFYGPGLNSLS
LPDRATISNMAPEYGATLGIFPPDTETLNYLKRTGRSDEQVDLVKKYLEAQDLLYSIHKP
EPLFSSNLELDMETVKPCLAGPKRPQDQLFLNEVSENFRETMRQTFIRKKEGGAELAGDP
AYQRWLGEGGAPVEETGIEEVKKVEPHEKGFRVTHGSVVIAAITSCTNTSNPSVLIGAGL
LAKKAVERGLRVKPFVKTSLSPGSRVATEYLGAAGLLPYLEALGFHQVGYGCTTCIGNSG
PLPEHIAKEIEEKDLTVAAVLSGNRNFEGRINPHVKANYLASPPLVVAYAIAGTVNINLE
TDPLAYDPNGLPVYIRDIWPGNEEIREAEKNSIKPEMFKKEYSGVLEGSKLWKELDVPEG
TLYAWSPTSTYIQEPPYFVDFPLTLPLPGDIQNARVLALFGDSITTDHISPAGDIPADGP
AGRYLISWGVDQKDFNSYGSRRGNHEVMMRGTFANIRLRNRLVSREGGWTVSHLKGEDFP
PEACGEGIPIYDAALLYAENDVPLIVLAGKEYGTGSSRDWAAKGTFLLGVKAVIAESFER
IHRSNLVGMGVLPLQFNVGENADTLGLTGKESYDILGIEQMEPHGELTVRAKDDNGGETE
FRVTLRLDSAVEIEYYRNGGILHKFLRDSVKKK
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