LipidDB-10090-00865

Lipid Modification Database

Tag

Content

LipidDB ID

LipidDB-10090-00865

Entry Name

ACON_MOUSE

UniProt Accession

Q99KI0; Q3UDK9; Q3ULG9; Q3UNH7; Q505P4;

Theoretical PI

8.08

Molecular Weight

85463.51

Genbank Protein ID

BAE25602.1; BAE25770.1; BAE26479.1; BAE29252.1; BAE38169.1; AAH04645.1; AAH94462.1;

Genbank Nucleotide ID

AK143917; AK144207; AK145511; AK150027; AK165411; BC004645; BC094462;

Protein Name

Aconitate hydratase, mitochondrial

Protein Synonyms/Alias

Aconitase; 4.2.1.3; Citrate hydro-lyase;

Gene Name

Aco2

Gene Synonyms/Alias

Created Date

01-FEB-2005

Lipid Modification Sites
Position	Sequence Form	Peptide	References	Modification Type
451	Canonical	LANACGPCIGQWDRK	[1]	S-Palmitoylation

Organism

Mus musculus (Mouse)

NCBI Taxa ID

10090

Reference

[1] Predicted from GPS-Lipid

Functional Description

Catalyzes the isomerization of citrate to isocitrate via cis-aconitate.

Sequence Annotation

Region: 192 194 Substrate binding.
Region: 670 671 Substrate binding.
Metal binding site: 385 385 Iron-sulfur (4Fe-4S).
Metal binding site: 448 448 Iron-sulfur (4Fe-4S).
Metal binding site: 451 451 Iron-sulfur (4Fe-4S).
Binding site: 99 99 Substrate.
Binding site: 474 474 Substrate.
Binding site: 479 479 Substrate.
Binding site: 607 607 Substrate.
Modified residue: 28 28 Pyrrolidone carboxylic acid.
Modified residue: 31 31 N6-succinyllysine.
Modified residue: 50 50 N6-acetyllysine; alternate.
Modified residue: 50 50 N6-succinyllysine; alternate.
Modified residue: 138 138 N6-acetyllysine; alternate.
Modified residue: 138 138 N6-succinyllysine; alternate.
Modified residue: 144 144 N6-acetyllysine; alternate.
Modified residue: 144 144 N6-succinyllysine; alternate.
Modified residue: 233 233 N6-acetyllysine; alternate.
Modified residue: 233 233 N6-succinyllysine; alternate.
Modified residue: 411 411 N6-succinyllysine.
Modified residue: 517 517 N6-acetyllysine; alternate.
Modified residue: 517 517 N6-succinyllysine; alternate.
Modified residue: 523 523 N6-acetyllysine; alternate.
Modified residue: 523 523 N6-succinyllysine; alternate.
Modified residue: 549 549 N6-succinyllysine.
Modified residue: 559 559 Phosphoserine.
Modified residue: 573 573 N6-acetyllysine; alternate.
Modified residue: 573 573 N6-succinyllysine; alternate.
Modified residue: 577 577 N6-succinyllysine.
Modified residue: 591 591 N6-succinyllysine.
Modified residue: 605 605 N6-acetyllysine; alternate.
Modified residue: 605 605 N6-succinyllysine; alternate.
Modified residue: 628 628 N6-succinyllysine.
Modified residue: 689 689 N6-succinyllysine.
Modified residue: 723 723 N6-acetyllysine; alternate.
Modified residue: 723 723 N6-succinyllysine; alternate.
Modified residue: 730 730 N6-acetyllysine; alternate.
Modified residue: 730 730 N6-succinyllysine; alternate.
Modified residue: 736 736 N6-acetyllysine.
Modified residue: 739 739 N6-acetyllysine.
Modified residue: 743 743 N6-acetyllysine.

Protein Length

780 AA.

Protein Sequence
(Canonical)

MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPS EYIRYDLLEK NINIVRKRLN  60
RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD ATAQMAMLQF ISSGLPKVAV  120
PSTIHCDHLI EAQVGGEKDL RRAKDINQEV YNFLATAGAK YGVGFWRPGS GIIHQIILEN  180
YAYPGVLLIG TDSHTPNGGG LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG  240
WTSPKDVILK VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN  300
HRMKKYLSKT GRTDIANLAE EFKDHLVPDP GCQYDQVIEI NLNELKPHIN GPFTPDLAHP  360
VADVGTVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA KQALAHGLKC KSQFTITPGS  420
EQIRATIERD GYAQILRDVG GIVLANACGP CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN  480
DANPETHAFV TSPEIVTALA IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRSDFDPG  540
QDTYQHPPKD SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA  600
GPWLKFRGHL DNISNNLLIG AINIENGKAN SVRNAVTQEF GPVPDTARYY KKHGIRWVVI  660
GDENYGEGSS REHAALEPRH LGGRAIITKS FARIHETNLK KQGLLPLTFA DPSDYNKIHP  720
VDKLTIQGLK DFAPGKPLKC VIKHPNGTQE TILLNHTFNE TQIEWFRAGS ALNRMKELQQ  780

FASTA
(Canonical)

>LipidDB-10090-00865|Q99KI0
MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPSEYIRYDLLEKNINIVRKRLN
RPLTLSEKIVYGHLDDPANQEIERGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAV
PSTIHCDHLIEAQVGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILEN
YAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSG
WTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYN
HRMKKYLSKTGRTDIANLAEEFKDHLVPDPGCQYDQVIEINLNELKPHINGPFTPDLAHP
VADVGTVAEKEGWPLDIRVGLIGSCTNSSYEDMGRSAAVAKQALAHGLKCKSQFTITPGS
EQIRATIERDGYAQILRDVGGIVLANACGPCIGQWDRKDIKKGEKNTIVTSYNRNFTGRN
DANPETHAFVTSPEIVTALAIAGTLKFNPETDFLTGKDGKKFKLEAPDADELPRSDFDPG
QDTYQHPPKDSSGQRVDVSPTSQRLQLLEPFDKWDGKDLEDLQILIKVKGKCTTDHISAA
GPWLKFRGHLDNISNNLLIGAINIENGKANSVRNAVTQEFGPVPDTARYYKKHGIRWVVI
GDENYGEGSSREHAALEPRHLGGRAIITKSFARIHETNLKKQGLLPLTFADPSDYNKIHP
VDKLTIQGLKDFAPGKPLKCVIKHPNGTQETILLNHTFNETQIEWFRAGSALNRMKELQQ

Gene Ontology

GO:0005739; C:mitochondrion; IDA:MGI
GO:0005634; C:nucleus; IEA:Ensembl
GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:Ensembl
GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW
GO:0003994; F:aconitate hydratase activity; IDA:MGI
GO:0005506; F:iron ion binding; IEA:Ensembl
GO:0006101; P:citrate metabolic process; IEA:Ensembl
GO:0006102; P:isocitrate metabolic process; IEA:Ensembl
GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway

Interpro

InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3
InterPro; IPR015937; Acoase/IPM_deHydtase
InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba
InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl
InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2
InterPro; IPR018136; Aconitase_4Fe-4S_BS
InterPro; IPR006248; Aconitase_mito-like
InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl

Pfam

Pfam; PF00330; Aconitase;
Pfam; PF00694; Aconitase_C;

SMART

PROSITE

PROSITE; PS00450; ACONITASE_1;
PROSITE; PS01244; ACONITASE_2;

PRINTS

PRINTS; PR00415; ACONITASE;