Reviewed, UniProtKB/Swiss-Prot P25516 (ACON1_ECOLI)

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

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	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.
Subunit structure	Monomer.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

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	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aconitate hydratase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 891	890	Aconitate hydratase 1		PRO_0000076661
Sites
	Metal binding	435	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	501	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	504	1	Iron-sulfur (4Fe-4S) By similarity
Experimental info
	Sequence conflict	522	1	S → G in CAA42834. Ref.1
	Sequence conflict	522	1	S → G in BAA14828. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P25516-1 [UniParc]. Last modified January 15, 2008. Version 3. Checksum: EB47E5B3C3F9C56C	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

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. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9043N.
IntAct	P25516. 4 interactions.
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
HOGENOM	P25516.
OMA	P25516. RIKNEML.
Enzyme and pathway databases
BioCyc	EcoCyc:ACONITASE-MON. MetaCyc:ACONITASE-MON.
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.
ProDom	PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	June 16, 2009
This is version 86 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)