Aconitate hydratase 1 - Escherichia coli (strain K12)

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P25516 (ACON1_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aconitate hydratase 1
Short name=Aconitase 1
EC=4.2.1.3

Alternative name(s):
Citrate hydro-lyase 1

Gene names

Name:	acnA
Synonyms:	acn
Ordered Locus Names:	b1276, JW1268

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	891 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. May have an iron-responsive regulatory function.
Catalytic activity	Citrate = isocitrate. Ref.6
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
Subunit structure	Monomer.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.
Biophysicochemical properties	Kinetic parameters: K_M=1.16 mM for citrate Ref.6 K_M=0.058 mM for cis-aconitate K_M=0.014 mM for isocitrate (using 0.01-0.8 mM substrate) K_M=1.77 mM for isocitrate (using 0.8-40 mM substrate) V_max=6.13 µmol/min/mg enzyme with citrate as substrate V_max=14.5 µmol/min/mg enzyme with cis-aconitate as substrate V_max=3.57 µmol/min/mg enzyme using 0.01-0.8 mM isocitrate as substrate V_max=14.7 µmol/min/mg enzyme using 0.8-40 mM isocitrate as substrate pH dependence: Optimum pH is 7.4.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	anaerobic respiration Inferred from direct assay PubMed 12486059. Source: EcoliWiki glyoxylate cycle Non-traceable author statement PubMed 10589714. Source: EcoliWiki response to oxidative stress Inferred from direct assay PubMed 12486059. Source: EcoliWiki tricarboxylic acid cycle Non-traceable author statement PubMed 10589714. Source: EcoliWiki
Cellular_component	cytoplasm Inferred from direct assay PubMed 12486059. Source: EcoliWiki
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from direct assay PubMed 7588761. Source: EcoCyc aconitate hydratase activity Inferred from direct assay PubMed 7588761. Source: EcoCyc citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from mutant phenotype PubMed 12486059. Source: EcoliWiki isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC mRNA 3'-UTR binding Inferred from direct assay PubMed 10589714. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.5

Chain

2 – 891

890

Aconitate hydratase 1

PRO_0000076661

Sites

Metal binding

435

Iron-sulfur (4Fe-4S) By similarity

Metal binding

501

Iron-sulfur (4Fe-4S) By similarity

Metal binding

504

Iron-sulfur (4Fe-4S) By similarity

Experimental info

Sequence conflict

522

S → G in CAA42834. Ref.1

Sequence conflict

522

S → G in BAA14828. Ref.4

Sequences

Sequence

Length

Mass (Da)

Tools

P25516 [UniParc].

Last modified January 15, 2008. Version 3.
Checksum: EB47E5B3C3F9C56C
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FASTA

891

97,677

        10         20         30         40         50         60 
MSSTLREASK DTLQAKDKTY HYYSLPLAAK SLGDITRLPK SLKVLLENLL RWQDGNSVTE 

        70         80         90        100        110        120 
EDIHALAGWL KNAHADREIA YRPARVLMQD FTGVPAVVDL AAMREAVKRL GGDTAKVNPL 

       130        140        150        160        170        180 
SPVDLVIDHS VTVDRFGDDE AFEENVRLEM ERNHERYVFL KWGKQAFSRF SVVPPGTGIC 

       190        200        210        220        230        240 
HQVNLEYLGK AVWSELQDGE WIAYPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ 

       250        260        270        280        290        300 
PVSMLIPDVV GFKLTGKLRE GITATDLVLT VTQMLRKHGV VGKFVEFYGD GLDSLPLADR 

       310        320        330        340        350        360 
ATIANMSPEY GATCGFFPID AVTLDYMRLS GRSEDQVELV EKYAKAQGMW RNPGDEPIFT 

       370        380        390        400        410        420 
STLELDMNDV EASLAGPKRP QDRVALPDVP KAFAASNELE VNATHKDRQP VDYVMNGHQY 

       430        440        450        460        470        480 
QLPDGAVVIA AITSCTNTSN PSVLMAAGLL AKKAVTLGLK RQPWVKASLA PGSKVVSDYL 

       490        500        510        520        530        540 
AKAKLTPYLD ELGFNLVGYG CTTCIGNSGP LPDPIETAIK KSDLTVGAVL SGNRNFEGRI 

       550        560        570        580        590        600 
HPLVKTNWLA SPPLVVAYAL AGNMNINLAS EPIGHDRKGD PVYLKDIWPS AQEIARAVEQ 

       610        620        630        640        650        660 
VSTEMFRKEY AEVFEGTAEW KGINVTRSDT YGWQEDSTYI RLSPFFDEMQ ATPAPVEDIH 

       670        680        690        700        710        720 
GARILAMLGD SVTTDHISPA GSIKPDSPAG RYLQGRGVER KDFNSYGSRR GNHEVMMRGT 

       730        740        750        760        770        780 
FANIRIRNEM VPGVEGGMTR HLPDSDVVSI YDAAMRYKQE QTPLAVIAGK EYGSGSSRDW 

       790        800        810        820        830        840 
AAKGPRLLGI RVVIAESFER IHRSNLIGMG ILPLEFPQGV TRKTLGLTGE EKIDIGDLQN 

       850        860        870        880        890 
LQPGATVPVT LTRADGSQEV VPCRCRIDTA TELTYYQNDG ILHYVIRNML K

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The aconitase of Escherichia coli. Nucleotide sequence of the aconitase gene and amino acid sequence similarity with mitochondrial aconitases, the iron-responsive-element-binding protein and isopropylmalate isomerases." Prodromou C., Artymiuk P.J., Guest J.R. Eur. J. Biochem. 204:599-609(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. Horiuchi T. DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The aconitase of Escherichia coli: purification of the enzyme and molecular cloning and map location of the gene (acn)." Prodromou C., Haynes M.J., Guest J.R. J. Gen. Microbiol. 137:2505-2515(1991) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-19.
[6]	"Biochemical and spectroscopic characterization of Escherichia coli aconitases (AcnA and AcnB)." Jordan P.A., Tang Y., Bradbury A.J., Thomson A.J., Guest J.R. Biochem. J. 344:739-746(1999) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X60293 Genomic DNA. Translation: CAA42834.1. U00096 Genomic DNA. Translation: AAC74358.1. AP009048 Genomic DNA. Translation: BAA14828.1.
PIR	G64875.
RefSeq	NP_415792.1. NC_000913.2. YP_489544.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P25516.
SMR	P25516. Positions 37-891.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9043N.
IntAct	P25516. 4 interactions.
MINT	MINT-1249275.
STRING	511145.b1276.
Proteomic databases
PaxDb	P25516.
PRIDE	P25516.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC74358; AAC74358; b1276. BAA14828; BAA14828; BAA14828.
GeneID	12931140. 946724.
KEGG	ecj:Y75_p1251. eco:b1276.
PATRIC	32117814. VBIEscCol129921_1327.
Organism-specific databases
EchoBASE	EB1301.
EcoGene	EG11325. acnA.
Phylogenomic databases
eggNOG	COG1048.
HOGENOM	HOG000025704.
KO	K01681.
OMA	YSKAQGM.
ProtClustDB	PRK09277.
Enzyme and pathway databases
BioCyc	EcoCyc:ACONITASE-MONOMER. ECOL316407:JW1268-MONOMER. MetaCyc:ACONITASE-MONOMER.
UniPathway	UPA00223; UER00718.
Gene expression databases
Genevestigator	P25516.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 2 hits. 3.40.1060.10. 1 hit.
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR006249. Aconitase/Fe_reg_prot_2. IPR015934. Aconitase/Fe_reg_prot_2/AcnD. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF1. PTHR11670:SF1. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR01341. aconitase_1. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACON1_ECOLI

Accession

Primary (citable) accession number: P25516
Secondary accession number(s): P78060, P78148

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 119 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents