SitesBLAST
Comparing WP_011187373.1 NCBI__GCF_000025945.1:WP_011187373.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
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)
53% identity, 97% coverage: 16:755/760 of query aligns to 41:773/778 of P19414
- R604 (= R586) 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)
53% identity, 97% coverage: 16:755/760 of query aligns to 45:776/780 of P20004
- Q99 (= Q70) binding substrate
- DSH 192:194 (= DSH 163:165) binding substrate
- C385 (= C362) binding [4Fe-4S] cluster
- C448 (= C425) binding [4Fe-4S] cluster
- C451 (= C428) binding [4Fe-4S] cluster
- R474 (= R451) binding substrate
- R479 (= R456) binding substrate
- R607 (= R586) binding substrate
- SR 670:671 (= SR 649:650) binding substrate
5acnA Structure of activated aconitase. Formation of the (4fe-4s) cluster in the crystal (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 18:749/754 of 5acnA
- active site: D100 (= D98), H101 (= H99), D165 (= D163), R447 (= R451), S642 (= S648), R644 (= R650)
- binding fe3-s4 cluster: I145 (= I143), H147 (= H145), H167 (= H165), C358 (= C362), C421 (= C425), C424 (= C428), N446 (= N450)
- binding tricarballylic acid: K198 (≠ L196), G235 (≠ N233), R666 (= R672)
P16276 Aconitate hydratase, mitochondrial; Aconitase; Citrate hydro-lyase; EC 4.2.1.3 from Sus scrofa (Pig) (see 3 papers)
53% identity, 97% coverage: 16:755/760 of query aligns to 45:776/781 of P16276
- Q99 (= Q70) binding substrate
- DSH 192:194 (= DSH 163:165) binding substrate
- C385 (= C362) binding [4Fe-4S] cluster
- C448 (= C425) binding [4Fe-4S] cluster
- C451 (= C428) binding [4Fe-4S] cluster
- R474 (= R451) binding substrate
- R479 (= R456) binding substrate
- R607 (= R586) binding substrate
- SR 670:671 (= SR 649:650) binding substrate
Sites not aligning to the query:
- 28 modified: Pyrrolidone carboxylic acid
1b0kA S642a:fluorocitrate complex of aconitase (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 17:748/753 of 1b0kA
- active site: D99 (= D98), H100 (= H99), D164 (= D163), R446 (= R451), A641 (≠ S648), R643 (= R650)
- binding citrate anion: Q71 (= Q70), H100 (= H99), D164 (= D163), S165 (= S164), R446 (= R451), R451 (= R456), R579 (= R586), A641 (≠ S648), S642 (= S649), R643 (= R650)
- binding oxygen atom: D164 (= D163), H166 (= H165)
- binding iron/sulfur cluster: H100 (= H99), D164 (= D163), H166 (= H165), S356 (= S361), C357 (= C362), C420 (= C425), C423 (= C428)
8acnA Crystal structures of aconitase with isocitrate and nitroisocitrate bound (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 17:748/753 of 8acnA
- active site: D99 (= D98), H100 (= H99), D164 (= D163), R446 (= R451), S641 (= S648), R643 (= R650)
- binding nitroisocitric acid: Q71 (= Q70), T74 (= T73), H100 (= H99), D164 (= D163), S165 (= S164), R446 (= R451), R451 (= R456), R579 (= R586), S641 (= S648), S642 (= S649), R643 (= R650)
- binding iron/sulfur cluster: H100 (= H99), D164 (= D163), H166 (= H165), S356 (= S361), C357 (= C362), C420 (= C425), C423 (= C428), I424 (= I429)
1fghA Complex with 4-hydroxy-trans-aconitate (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 17:748/753 of 1fghA
- active site: D99 (= D98), H100 (= H99), D164 (= D163), R446 (= R451), S641 (= S648), R643 (= R650)
- binding 4-hydroxy-aconitate ion: Q71 (= Q70), T74 (= T73), H100 (= H99), D164 (= D163), S165 (= S164), R446 (= R451), R451 (= R456), R579 (= R586), S641 (= S648), S642 (= S649), R643 (= R650)
- binding iron/sulfur cluster: H100 (= H99), D164 (= D163), H166 (= H165), S356 (= S361), C357 (= C362), C420 (= C425), C423 (= C428), I424 (= I429), R451 (= R456)
1amjA Steric and conformational features of the aconitase mechanism (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 17:748/753 of 1amjA
- active site: D99 (= D98), H100 (= H99), D164 (= D163), R446 (= R451), S641 (= S648), R643 (= R650)
- binding iron/sulfur cluster: I144 (= I143), H166 (= H165), C357 (= C362), C420 (= C425), C423 (= C428)
- binding sulfate ion: Q71 (= Q70), R579 (= R586), R643 (= R650)
1amiA Steric and conformational features of the aconitase mechanism (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 17:748/753 of 1amiA
- active site: D99 (= D98), H100 (= H99), D164 (= D163), R446 (= R451), S641 (= S648), R643 (= R650)
- binding alpha-methylisocitric acid: Q71 (= Q70), T74 (= T73), H100 (= H99), D164 (= D163), S165 (= S164), R446 (= R451), R451 (= R456), R579 (= R586), S641 (= S648), S642 (= S649), R643 (= R650)
- binding iron/sulfur cluster: H100 (= H99), I144 (= I143), D164 (= D163), H166 (= H165), S356 (= S361), C357 (= C362), C420 (= C425), C423 (= C428), N445 (= N450)
1acoA Crystal structure of aconitase with transaconitate bound (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 17:748/753 of 1acoA
- active site: D99 (= D98), H100 (= H99), D164 (= D163), R446 (= R451), S641 (= S648), R643 (= R650)
- binding iron/sulfur cluster: H100 (= H99), I144 (= I143), D164 (= D163), H166 (= H165), S356 (= S361), C357 (= C362), C420 (= C425), C423 (= C428), N445 (= N450)
- binding aconitate ion: Q71 (= Q70), D164 (= D163), S165 (= S164), R446 (= R451), R451 (= R456), R579 (= R586), S641 (= S648), S642 (= S649), R643 (= R650)
1nisA Crystal structure of aconitase with trans-aconitate and nitrocitrate bound (see paper)
53% identity, 97% coverage: 16:755/760 of query aligns to 17:748/753 of 1nisA
- active site: D99 (= D98), H100 (= H99), D164 (= D163), R446 (= R451), S641 (= S648), R643 (= R650)
- binding 2-hydroxy-2-nitromethyl succinic acid: Q71 (= Q70), H100 (= H99), D164 (= D163), S165 (= S164), R446 (= R451), R451 (= R456), R579 (= R586), S641 (= S648), S642 (= S649)
- binding iron/sulfur cluster: H100 (= H99), I144 (= I143), H166 (= H165), S356 (= S361), C357 (= C362), C420 (= C425), C423 (= C428)
P39533 Homocitrate dehydratase, mitochondrial; Aconitase 2; EC 4.2.1.- from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
47% identity, 95% coverage: 31:754/760 of query aligns to 51:782/789 of P39533
- K610 (≠ R586) mutation to R: Reduces catalytic activity towards homoaconitate by 45% and increases the activity towards aconitate by a factor 116.
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)
27% identity, 92% coverage: 60:760/760 of query aligns to 172:989/990 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)
27% identity, 95% coverage: 38:758/760 of query aligns to 61:887/889 of P21399
- C300 (≠ G258) mutation to S: No effect on aconitase activity or on RNA binding.
- T318 (= T276) to M: in dbSNP:rs150373174
- C437 (= C362) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C503 (= C425) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- C506 (= C428) mutation to S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
- R536 (= R451) mutation to Q: Strongly reduced RNA binding.
- R541 (= R456) mutation to Q: Strongly reduced RNA binding.
- R699 (vs. gap) mutation to K: No effect on RNA binding.
- S778 (= S648) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
- R780 (= R650) mutation to Q: Nearly abolishes RNA binding.
2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
27% identity, 95% coverage: 38:758/760 of query aligns to 60:886/888 of 2b3xA
- active site: D124 (= D98), H125 (= H99), D204 (= D163), R535 (= R451), S777 (= S648), R779 (= R650)
- binding iron/sulfur cluster: I175 (= I143), H206 (= H165), C436 (= C362), C502 (= C425), C505 (= C428), I506 (= I429), N534 (= N450)
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)
27% identity, 91% coverage: 63:757/760 of query aligns to 89:904/909 of P09339
- C450 (= C362) 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 (vs. gap) 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
3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
26% identity, 92% coverage: 60:758/760 of query aligns to 75:848/850 of 3snpA
- active site: D124 (= D98), H125 (= H99), D186 (= D163), R505 (= R451), S739 (= S648), R741 (= R650)
- binding : H125 (= H99), S126 (≠ A107), H188 (= H165), L243 (= L220), R250 (≠ T227), N279 (= N256), E283 (= E260), S352 (≠ V327), P357 (= P332), K360 (= K334), T419 (≠ C362), N420 (≠ T363), T421 (≠ N364), N504 (= N450), R505 (= R451), L520 (= L467), S642 (= S577), P643 (= P578), A644 (= A579), G645 (= G580), N646 (vs. gap), R649 (vs. gap), R665 (vs. gap), S669 (vs. gap), G671 (vs. gap), R674 (= R586), R741 (= R650)
4kp1A Crystal structure of ipm isomerase large subunit from methanococcus jannaschii (mj0499) (see paper)
28% identity, 49% coverage: 111:486/760 of query aligns to 67:420/423 of 4kp1A
Sites not aligning to the query:
4nqyA The reduced form of mj0499 (see paper)
29% identity, 47% coverage: 130:486/760 of query aligns to 73:407/409 of 4nqyA
Sites not aligning to the query:
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)
31% identity, 38% coverage: 60:344/760 of query aligns to 74:383/931 of D9X0I3
- SVIAD 125:129 (≠ LIQAY 100:104) mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
Sites not aligning to the query:
- 538 C→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.
- 763 R→E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
- 767 Q→E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.
Query Sequence
>WP_011187373.1 NCBI__GCF_000025945.1:WP_011187373.1
MKTSVDSTATFIEKVYQRTTEQLKTVRARLNRPLTYTEKIMYGHLDDADNAELIAGKSYI
KTRPDRIALQDATAQMAVLQFMLAEKDEAAVPVTIHCDHLIQAYKGAETDLPIAKTENNE
VYNFLSSASKRYGFGYWHPGAGIIHQVVLERYAFPGLMMLGTDSHTPNAGGMGVFASGVG
GADAVDVMVDMPWEVLHPQVVGVHLKGKLQEWSSPKDIILKLLEVLTCSGGTNRVFEYFG
EGAASISATGKSTICNMGAELGATTSLFPYDQSMATYLQACGRGEVADLANQYQTILQAD
DEVLTNPESYYDKVVVIDLDKLVPYIVGPHSPDKAATVAALAEQVTINGYPEKISATLIG
SCTNSSYEDMGRIAAIADQIIEEGAQLKTPLYITPGSEQVRATIERDGILEKLLQIGAIV
LTNACGPCIGQWRRDDQVPNTPNTIVSSYNRNFPKRNDGNPETCSFLTSPETCMAYALHG
SLAVNPYTTPIEGKNGPFLLKTPGRVAEVPAQGFVCDQEGFQAPIAKEERAGISVEISPD
SKRLAKLIPFPAWDGKNFKDLRLLLKAKGKCTTDHISPAGPWLRFRGHLDNISDNMFSGA
INSFTGMAGSGINQLDGKVEGFNQIARAYQAAGDSWLVVGDNNYGEGSSREHAAMSPRHM
GAKVVICKAFARIHETNLKKQGVLPLTFTSSNDYQLVQDGDRIDVLGVKEIAPASALQAV
LKHSDGSSDRVELQHSLNQEQISWFKAGSALNYLRHELNE
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