SitesBLAST
Comparing WP_020174411.1 NCBI__GCF_000385335.1:WP_020174411.1 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)
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: 2:907/910 of query aligns to 9:938/943 of A0QX20
- K394 (≠ A407) 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)
54% identity, 99% coverage: 2:906/910 of query aligns to 8:904/909 of P09339
- C450 (= C445) 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 (= R736) 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)
54% identity, 99% coverage: 3:907/910 of query aligns to 2:928/931 of D9X0I3
- SVIAD 125:129 (≠ SVIVD 132:136) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C511) 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 (= R736) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ F740) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
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: 22:908/910 of query aligns to 117:988/990 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)
51% identity, 96% coverage: 39:908/910 of query aligns to 34:887/888 of 2b3xA
- active site: D124 (= D130), H125 (= H131), D204 (= D223), R535 (= R544), S777 (= S793), R779 (= R795)
- binding iron/sulfur cluster: I175 (= I181), H206 (= H225), C436 (= C445), C502 (= C511), C505 (= C514), I506 (= I515), N534 (= N543)
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)
51% identity, 96% coverage: 39:908/910 of query aligns to 35:888/889 of P21399
- C300 (≠ A318) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ S336) to M: in dbSNP:rs150373174
- C437 (= C445) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C511) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C514) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R544) mutation to Q: Strongly reduced RNA binding.
- R541 (= R549) mutation to Q: Strongly reduced RNA binding.
- R699 (= R707) mutation to K: No effect on RNA binding.
- S778 (= S793) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R795) 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)
50% identity, 96% coverage: 39:908/910 of query aligns to 34:849/850 of 3snpA
- active site: D124 (= D130), H125 (= H131), D186 (= D223), R505 (= R544), S739 (= S793), R741 (= R795)
- binding : H125 (= H131), S126 (= S132), H188 (= H225), L243 (= L280), R250 (= R287), N279 (= N316), E283 (= E320), S352 (≠ A387), P357 (= P392), K360 (≠ R395), T419 (= T446), N420 (= N447), T421 (= T448), N504 (= N543), R505 (= R544), L520 (= L559), S642 (= S689), P643 (= P690), A644 (= A691), G645 (= G692), N646 (≠ S693), R649 (≠ A696), R665 (≠ K712), S669 (≠ Q716), G671 (= G718), R674 (= R721), R741 (= R795)
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 62:745/754 of 5acnA
- active site: D100 (= D130), H101 (= H131), D165 (= D223), R447 (= R544), S642 (= S793), R644 (= R795)
- binding fe3-s4 cluster: I145 (= I181), H147 (= H183), H167 (= H225), C358 (= C445), C421 (= C511), C424 (= C514), N446 (= N543)
- binding tricarballylic acid: K198 (≠ L256), G235 (= G293), R666 (= R817)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 90% coverage: 81:900/910 of query aligns to 89:772/781 of P16276
- Q99 (= Q91) binding substrate
- DSH 192:194 (= DSH 223:225) binding substrate
- C385 (= C445) binding [4Fe-4S] cluster
- C448 (= C511) binding [4Fe-4S] cluster
- C451 (= C514) binding [4Fe-4S] cluster
- R474 (= R544) binding substrate
- R479 (= R549) binding substrate
- R607 (= R721) binding substrate
- SR 670:671 (= SR 794:795) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 61:744/753 of 1b0kA
- active site: D99 (= D130), H100 (= H131), D164 (= D223), R446 (= R544), A641 (≠ S793), R643 (= R795)
- binding citrate anion: Q71 (= Q91), H100 (= H131), D164 (= D223), S165 (= S224), R446 (= R544), R451 (= R549), R579 (= R721), A641 (≠ S793), S642 (= S794), R643 (= R795)
- binding oxygen atom: D164 (= D223), H166 (= H225)
- binding iron/sulfur cluster: H100 (= H131), D164 (= D223), H166 (= H225), S356 (= S444), C357 (= C445), C420 (= C511), C423 (= C514)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 61:744/753 of 8acnA
- active site: D99 (= D130), H100 (= H131), D164 (= D223), R446 (= R544), S641 (= S793), R643 (= R795)
- binding nitroisocitric acid: Q71 (= Q91), T74 (= T94), H100 (= H131), D164 (= D223), S165 (= S224), R446 (= R544), R451 (= R549), R579 (= R721), S641 (= S793), S642 (= S794), R643 (= R795)
- binding iron/sulfur cluster: H100 (= H131), D164 (= D223), H166 (= H225), S356 (= S444), C357 (= C445), C420 (= C511), C423 (= C514), I424 (= I515)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 61:744/753 of 1fghA
- active site: D99 (= D130), H100 (= H131), D164 (= D223), R446 (= R544), S641 (= S793), R643 (= R795)
- binding 4-hydroxy-aconitate ion: Q71 (= Q91), T74 (= T94), H100 (= H131), D164 (= D223), S165 (= S224), R446 (= R544), R451 (= R549), R579 (= R721), S641 (= S793), S642 (= S794), R643 (= R795)
- binding iron/sulfur cluster: H100 (= H131), D164 (= D223), H166 (= H225), S356 (= S444), C357 (= C445), C420 (= C511), C423 (= C514), I424 (= I515), R451 (= R549)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 61:744/753 of 1amjA
- active site: D99 (= D130), H100 (= H131), D164 (= D223), R446 (= R544), S641 (= S793), R643 (= R795)
- binding iron/sulfur cluster: I144 (= I181), H166 (= H225), C357 (= C445), C420 (= C511), C423 (= C514)
- binding sulfate ion: Q71 (= Q91), R579 (= R721), R643 (= R795)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 61:744/753 of 1amiA
- active site: D99 (= D130), H100 (= H131), D164 (= D223), R446 (= R544), S641 (= S793), R643 (= R795)
- binding alpha-methylisocitric acid: Q71 (= Q91), T74 (= T94), H100 (= H131), D164 (= D223), S165 (= S224), R446 (= R544), R451 (= R549), R579 (= R721), S641 (= S793), S642 (= S794), R643 (= R795)
- binding iron/sulfur cluster: H100 (= H131), I144 (= I181), D164 (= D223), H166 (= H225), S356 (= S444), C357 (= C445), C420 (= C511), C423 (= C514), N445 (= N543)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 61:744/753 of 1acoA
- active site: D99 (= D130), H100 (= H131), D164 (= D223), R446 (= R544), S641 (= S793), R643 (= R795)
- binding iron/sulfur cluster: H100 (= H131), I144 (= I181), D164 (= D223), H166 (= H225), S356 (= S444), C357 (= C445), C420 (= C511), C423 (= C514), N445 (= N543)
- binding aconitate ion: Q71 (= Q91), D164 (= D223), S165 (= S224), R446 (= R544), R451 (= R549), R579 (= R721), S641 (= S793), S642 (= S794), R643 (= R795)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
28% identity, 90% coverage: 81:900/910 of query aligns to 61:744/753 of 1nisA
- active site: D99 (= D130), H100 (= H131), D164 (= D223), R446 (= R544), S641 (= S793), R643 (= R795)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q91), H100 (= H131), D164 (= D223), S165 (= S224), R446 (= R544), R451 (= R549), R579 (= R721), S641 (= S793), S642 (= S794)
- binding iron/sulfur cluster: H100 (= H131), I144 (= I181), H166 (= H225), S356 (= S444), C357 (= C445), C420 (= C511), C423 (= C514)
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)
27% identity, 90% coverage: 81:900/910 of query aligns to 85:769/778 of P19414
- R604 (= R729) 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)
28% identity, 90% coverage: 81:900/910 of query aligns to 89:772/780 of P20004
- Q99 (= Q91) binding substrate
- DSH 192:194 (= DSH 223:225) binding substrate
- C385 (= C445) binding [4Fe-4S] cluster
- C448 (= C511) binding [4Fe-4S] cluster
- C451 (= C514) binding [4Fe-4S] cluster
- R474 (= R544) binding substrate
- R479 (= R549) binding substrate
- R607 (= R721) binding substrate
- SR 670:671 (= SR 794:795) binding substrate
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
26% identity, 95% coverage: 37:903/910 of query aligns to 52:782/789 of P39533
- K610 (≠ R729) 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, 36% coverage: 218:549/910 of query aligns to 135:448/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_020174411.1 NCBI__GCF_000385335.1:WP_020174411.1
MASLDSFKCLKKLNVGDKTYHYYSLKTAEKNGLPGIANLPFSMKILLENLLRFEDGRSVT
KEDILSVAQWLQNKGKDEREIAFRPTRVLMQDFTGVPAVVDLAAMRDAMTKLGGDPQKIN
PLVPVDLVIDHSVIVDAFGTNKAFKTNVDLEYQRNGERYRFLKWGQDSFNNFRVVPPGTG
ICHQVNLEYLAQTVWTKKEKVTGKGGKKETIEVAYPDSLVGTDSHTTMVNGLSVLGWGVG
GIEAEACMLGQPLSMLLPEVIGFKLTGALNPGVTATDLVLTVTQMLRKKGVVGKFVEFYG
PGLNALSLADRATIANMAPEYGATCGFFPVDGETISYLTMTARSNPRIALVEAYAKAQGL
YRTKISPDPVFTETLDLDLAEVMPSMAGPKRPEGRVALGGVAEGFKAALESDYKKSADAE
TRYPVDDKNFDLGHGDVVIAAITSCTNTSNPNVLIGAGLLARNALAKGLTTKPWVKTSLA
PGSQVVAEYLTASGLQKDLDKLGFNLVGFGCTTCIGNSGPLPPEISKTINENGIVAAAVL
SGNRNFEGRVSPDVQANYLASPPLVVAHAIAGTVTRNLDEEPIGHNKKGEPIYLKEIWPS
GEEIDAFIEDFVTRKVFKSRYADVFEGDAHWRKVKAPSGETYKWDMGSTYVQNPPYFDGM
TMTPDPVKEIEGARILALFGDKITTDHISPAGSIKAGSPAGTFLEERQVSAKDFNQYGTR
RGNHEIMMRGTFANIRIKNFIREKKPDGTVPEGGMTKHWPDGTEMPIYDAAMKYKEEGVP
LVIFAGAEYGNGSSRDWAAKGTKLLGVRAVIAESFERIHRSNLVGMGVLPLTFEAGTTWA
SLGLKGDEIVTIHGLGEGLKPRQMMEAEIKYADGGVKTVPLLCRIATEDELEYFKNGGIL
PYVLRQLAVA
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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