SitesBLAST
Comparing WP_073036524.1 NCBI__GCF_900129305.1:WP_073036524.1 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)
53% identity, 99% coverage: 1:873/881 of query aligns to 13:904/909 of P09339
- C450 (= C421) 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 (= R712) 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
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
52% identity, 98% coverage: 15:875/881 of query aligns to 19:887/888 of 2b3xA
- active site: D124 (= D120), H125 (= H121), D204 (= D204), R535 (= R520), S777 (= S762), R779 (= R764)
- binding iron/sulfur cluster: I175 (= I171), H206 (= H206), C436 (= C421), C502 (= C487), C505 (= C490), I506 (= I491), N534 (= N519)
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)
52% identity, 98% coverage: 15:875/881 of query aligns to 20:888/889 of P21399
- C300 (≠ S299) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (≠ E317) to M: in dbSNP:rs150373174
- C437 (= C421) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C487) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C490) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R520) mutation to Q: Strongly reduced RNA binding.
- R541 (= R525) mutation to Q: Strongly reduced RNA binding.
- R699 (≠ L683) mutation to K: No effect on RNA binding.
- S778 (= S762) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R764) mutation to Q: Nearly abolishes RNA binding.
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)
53% identity, 98% coverage: 11:875/881 of query aligns to 112:988/990 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)
51% identity, 100% coverage: 3:879/881 of query aligns to 16:943/943 of A0QX20
- K394 (≠ Q386) 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)
51% identity, 99% coverage: 3:874/881 of query aligns to 8:928/931 of D9X0I3
- SVIAD 125:129 (≠ SVQVD 122:126) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
- C538 (= C487) 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 (= R712) mutation to E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- Q767 (≠ K716) 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, 98% coverage: 15:875/881 of query aligns to 19:849/850 of 3snpA
- active site: D124 (= D120), H125 (= H121), D186 (= D204), R505 (= R520), S739 (= S762), R741 (= R764)
- binding : H125 (= H121), S126 (= S122), H188 (= H206), L243 (= L261), R250 (= R268), N279 (= N297), E283 (= E301), S352 (≠ A366), P357 (= P371), K360 (≠ R374), T419 (= T422), N420 (= N423), T421 (= T424), N504 (= N519), R505 (= R520), L520 (= L535), S642 (= S665), P643 (= P666), A644 (= A667), G645 (= G668), N646 (≠ A669), R649 (≠ E672), R665 (≠ Q688), S669 (= S692), G671 (= G694), R674 (= R697), R741 (= R764)
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: 75:870/881 of query aligns to 89:772/778 of P19414
- R604 (≠ L683) 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, 94% coverage: 40:868/881 of query aligns to 53:773/780 of P20004
- Q99 (= Q81) binding substrate
- DSH 192:194 (= DSH 204:206) binding substrate
- C385 (= C421) binding [4Fe-4S] cluster
- C448 (= C487) binding [4Fe-4S] cluster
- C451 (= C490) binding [4Fe-4S] cluster
- R474 (= R520) binding substrate
- R479 (= R525) binding substrate
- R607 (≠ L683) binding substrate
- SR 670:671 (= SR 763:764) binding substrate
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
27% identity, 90% coverage: 75:868/881 of query aligns to 65:745/753 of 8acnA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R520), S641 (= S762), R643 (= R764)
- binding nitroisocitric acid: Q71 (= Q81), T74 (≠ V89), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R520), R451 (= R525), R579 (≠ L683), S641 (= S762), S642 (= S763), R643 (= R764)
- binding iron/sulfur cluster: H100 (= H121), D164 (= D204), H166 (= H206), S356 (= S420), C357 (= C421), C420 (= C487), C423 (= C490), I424 (= I491)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
27% identity, 90% coverage: 75:868/881 of query aligns to 65:745/753 of 1fghA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R520), S641 (= S762), R643 (= R764)
- binding 4-hydroxy-aconitate ion: Q71 (= Q81), T74 (≠ V89), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R520), R451 (= R525), R579 (≠ L683), S641 (= S762), S642 (= S763), R643 (= R764)
- binding iron/sulfur cluster: H100 (= H121), D164 (= D204), H166 (= H206), S356 (= S420), C357 (= C421), C420 (= C487), C423 (= C490), I424 (= I491), R451 (= R525)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 90% coverage: 75:868/881 of query aligns to 65:745/753 of 1amjA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R520), S641 (= S762), R643 (= R764)
- binding iron/sulfur cluster: I144 (= I171), H166 (= H206), C357 (= C421), C420 (= C487), C423 (= C490)
- binding sulfate ion: Q71 (= Q81), R579 (≠ L683), R643 (= R764)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
27% identity, 90% coverage: 75:868/881 of query aligns to 65:745/753 of 1amiA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R520), S641 (= S762), R643 (= R764)
- binding alpha-methylisocitric acid: Q71 (= Q81), T74 (≠ V89), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R520), R451 (= R525), R579 (≠ L683), S641 (= S762), S642 (= S763), R643 (= R764)
- binding iron/sulfur cluster: H100 (= H121), I144 (= I171), D164 (= D204), H166 (= H206), S356 (= S420), C357 (= C421), C420 (= C487), C423 (= C490), N445 (= N519)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
27% identity, 90% coverage: 75:868/881 of query aligns to 65:745/753 of 1acoA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R520), S641 (= S762), R643 (= R764)
- binding iron/sulfur cluster: H100 (= H121), I144 (= I171), D164 (= D204), H166 (= H206), S356 (= S420), C357 (= C421), C420 (= C487), C423 (= C490), N445 (= N519)
- binding aconitate ion: Q71 (= Q81), D164 (= D204), S165 (= S205), R446 (= R520), R451 (= R525), R579 (≠ L683), S641 (= S762), S642 (= S763), R643 (= R764)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
27% identity, 90% coverage: 75:868/881 of query aligns to 65:745/753 of 1nisA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R520), S641 (= S762), R643 (= R764)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q81), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R520), R451 (= R525), R579 (≠ L683), S641 (= S762), S642 (= S763)
- binding iron/sulfur cluster: H100 (= H121), I144 (= I171), H166 (= H206), S356 (= S420), C357 (= C421), C420 (= C487), C423 (= C490)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
28% identity, 83% coverage: 75:802/881 of query aligns to 90:711/789 of P39533
- K610 (≠ R697) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
28% identity, 90% coverage: 75:868/881 of query aligns to 66:746/754 of 5acnA
- active site: D100 (= D120), H101 (= H121), D165 (= D204), R447 (= R520), S642 (= S762), R644 (= R764)
- binding fe3-s4 cluster: I145 (= I171), H147 (= H173), H167 (= H206), C358 (= C421), C421 (= C487), C424 (= C490), N446 (= N519)
- binding tricarballylic acid: K198 (≠ A237), G235 (≠ E274), R666 (= R786)
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
27% identity, 90% coverage: 75:868/881 of query aligns to 65:745/753 of 1b0kA
- active site: D99 (= D120), H100 (= H121), D164 (= D204), R446 (= R520), A641 (≠ S762), R643 (= R764)
- binding citrate anion: Q71 (= Q81), H100 (= H121), D164 (= D204), S165 (= S205), R446 (= R520), R451 (= R525), R579 (≠ L683), A641 (≠ S762), S642 (= S763), R643 (= R764)
- binding oxygen atom: D164 (= D204), H166 (= H206)
- binding iron/sulfur cluster: H100 (= H121), D164 (= D204), H166 (= H206), S356 (= S420), C357 (= C421), C420 (= C487), C423 (= C490)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
28% identity, 90% coverage: 75:868/881 of query aligns to 93:773/781 of P16276
- Q99 (= Q81) binding substrate
- DSH 192:194 (= DSH 204:206) binding substrate
- C385 (= C421) binding [4Fe-4S] cluster
- C448 (= C487) binding [4Fe-4S] cluster
- C451 (= C490) binding [4Fe-4S] cluster
- R474 (= R520) binding substrate
- R479 (= R525) binding substrate
- R607 (≠ L683) binding substrate
- SR 670:671 (= SR 763:764) 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)
27% identity, 41% coverage: 186:550/881 of query aligns to 114:472/758 of O14289
Sites not aligning to the query:
- 486 modified: Phosphoserine
- 488 modified: Phosphoserine
Query Sequence
>WP_073036524.1 NCBI__GCF_900129305.1:WP_073036524.1
MSARARLEKDGETFEFVDLKGLFGNRLGRLPYSIRVLLENVVRRRDDRLVTERDVENLAG
WRGRYAEPVEIPFFPARVLMQDFTGVPAVADLAAMRDALVALGKDPAAVNPLVPVDLVVD
HSVQVDFFGTSDALTANVRREYERNGERYTFLKWAQKSFENFRVVPPNSGICHQVNLEHL
SRVFWDRKEDGVRICFPDTVVGLDSHTTMVNGIGVLGWGVGGIEAEAVLMGQPYSMAIPE
VIGVRLVGRLPRRANATDLVLRVTEALRDYGVVEKFVEFFGPAVTALSVPARATIANMSP
EYGATVGFFPVDEKVVEYLRLTHRERQARVTEAAARAMGLYYDGSEEPDYTDVLEIDLSA
IRPAVAGPSKPKDRIELSELKTRFRQLRGEDAPKAAVPVRIRGENVELSDGSVVIAAITS
CTNTSNPHALLGAALLARNAVKRGLAVPAHVKTSLAPGSKVVVQYLDRSGLLPYLEALGF
HPVAFGCTTCIGNSGPLHPEVERAIEEHNLNVAAVLSGNRNFEARIHQKVKSNFLASPLL
VVAFALAGRVDVDLEKEPVGLDPNGGPVFLADILPDDEEIEELVNRYVQEDLFRETYEKI
LEGDQFWNELQVQESVTYPWDPRSTYIKCPPYFEGFTPQMPETTDIRGARVLLWLGDAVT
TDHISPAGAIHEDYPAGRYLKSLGLSRQEFNSYGARRGNHEVMMRGTFANIRIRNKLVSE
PGSFTVKFPEGERMYVFEAAEAYRREGVPLIVLGGKEYGTGSSRDWAAKGPKLLGVKAVI
AESFERIHRSNLIGMGILPLQFLEGESAESLGLDGTEEYHIAGIAGIEPRRKLTVTAVKD
GKEKTFQVLARLDTEIEADYYRNGGILDYVLRKMAGSDQAP
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