Aconitate hydratase 1 - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P25516 (ACON1_ECOLI)

Last modified February 9, 2010. Version 93. History...

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

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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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.

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General annotation (Comments)

Function	May have an iron-responsive regulatory function.
Catalytic activity	Citrate = isocitrate.
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.

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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
Gene Ontology (GO)
Biological process	anaerobic respiration Inferred from direct assay. Source: UniProtKB regulation of translation in response to oxidative stress Inferred from direct assay. Source: UniProtKB tricarboxylic acid cycle Inferred from direct assay. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	4 iron, 4 sulfur cluster binding Inferred from direct assay. Source: UniProtKB aconitate hydratase activity Ref.5 Inferred from direct assay. Source: UniProtKB iron ion binding Inferred from mutant phenotype. Source: UniProtKB mRNA 3'-UTR binding Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
nadE	P18843	1	EBI-549739,EBI-548960

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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

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Sequences

Sequence

Length

Mass (Da)

Tools

P25516-1 [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

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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: 1541275] [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: 9097039] [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: 9278503] [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: 16738553] [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: 1838390] [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: 10585860] [Abstract] Cited for: CHARACTERIZATION, MAGNETIC CIRCULAR DICHROISM, EPR SPECTROSCOPY.

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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	AP_001902.1. NP_415792.1.
3D structure databases
SMR	P25516. Positions 9-891.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-9043N.
IntAct	P25516. 4 interactions.
STRING	P25516.
Proteomic databases
PRIDE	P25516.
Genome annotation databases
GeneID	946724.
GenomeReviews	Gene locus JW1268 in contig AP009048_GR. Gene locus b1276 in contig U00096_GR.
KEGG	ecj:JW1268. eco:b1276.
Organism-specific databases
EchoBASE	EB1301.
EcoGene	EG11325. acnA.
CMR	Search...
Phylogenomic databases
eggNOG	COG1048.
HOGENOM	HBG289738.
OMA	YSKAQGM.
Enzyme and pathway databases
BioCyc	EcoCyc:ACONITASE-MONOMER. ECOL168927:B1276-MONOMER. MetaCyc:ACONITASE-MONOMER.
Gene expression databases
Genevestigator	P25516.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. 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]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
TIGRFAMs	TIGR01341. aconitase_1. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

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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:	February 9, 2010
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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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 and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents