Aconitate hydratase 2 - Escherichia coli (strain K12)

Names and origin

Protein names

Recommended name:
    Aconitate hydratase 2
      Short name=Aconitase
    EC=4.2.1.3
Alternative name(s):
    Citrate hydro-lyase

Gene names

Name:	acnB
Synonyms:	yacI, yacJ
Ordered Locus Names:	b0118, JW0114

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	865 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	Citrate = isocitrate.
Cofactor	Binds 1 4Fe-4S cluster per subunit.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
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	3D-structure 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 electronic annotation. Source: InterPro
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 865

865

Aconitate hydratase 2

PRO_0000076675

Sites

Metal binding

710

1

Iron-sulfur (4Fe-4S)

Metal binding

769

1

Iron-sulfur (4Fe-4S)

Metal binding

772

1

Iron-sulfur (4Fe-4S)

Experimental info

Sequence conflict

39

1

Missing Ref.1

Sequence conflict

75 – 76

2

EA → RS Ref.1

Secondary structure

1

.

865

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P36683-1 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: FEC8AA5D2A9DD2BD
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FASTA

865

93,498

        10         20         30         40         50         60 
MLEEYRKHVA ERAAEGIAPK PLDANQMAAL VELLKNPPAG EEEFLLDLLT NRVPPGVDEA 

        70         80         90        100        110        120 
AYVKAGFLAA IAKGEAKSPL LTPEKAIELL GTMQGGYNIH PLIDALDDAK LAPIAAKALS 

       130        140        150        160        170        180 
HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW ADAEWFLNRP ALAEKLTVTV FKVTGETNTD 

       190        200        210        220        230        240 
DLSPAPDAWS RPDIPLHALA MLKNAREGIE PDQPGVVGPI KQIEALQQKG FPLAYVGDVV 

       250        260        270        280        290        300 
GTGSSRKSAT NSVLWFMGDD IPHVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN 

       310        320        330        340        350        360 
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG RGLTTKAREA 

       370        380        390        400        410        420 
LGLPHSDVFR QAKDVAESDR GFSLAQKMVG RACGVKGIRP GAYCEPKMTS VGSQDTTGPM 

       430        440        450        460        470        480 
TRDELKDLAC LGFSADLVMQ SFCHTAAYPK PVDVNTHHTL PDFIMNRGGV SLRPGDGVIH 

       490        500        510        520        530        540 
SWLNRMLLPD TVGTGGDSHT RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM 

       550        560        570        580        590        600 
QPGITLRDLV HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA 

       610        620        630        640        650        660 
ERSAAGCTIK LNKEPIIEYL NSNIVLLKWM IAEGYGDRRT LERRIQGMEK WLANPELLEA 

       670        680        690        700        710        720 
DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARPLSAVQGE KIDEVFIGSC MTNIGHFRAA 

       730        740        750        760        770        780 
GKLLDAHKGQ LPTRLWVAPP TRMDAAQLTE EGYYSVFGKS GARIEIPGCS LCMGNQARVA 

       790        800        810        820        830        840 
DGATVVSTST RNFPNRLGTG ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT 

       850        860 
YRYLNFNQLS QYTEKADGVI FQTAV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region." Fujita N., Mori H., Yura T., Ishihama A. Nucleic Acids Res. 22:1637-1639(1994) [PubMed: 8202364] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[3]	"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], SEQUENCE REVISION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The second aconitase (AcnB) of Escherichia coli." Bradbury A.J., Gruer M.J., Rudd K.E., Guest J.R. Microbiology 142:389-400(1996) [PubMed: 8932712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-131, PROTEIN SEQUENCE OF 1-11, CHARACTERIZATION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[6]	"Two genetically-distinct and differentially-regulated aconitases (AcnA and AcnB) in Escherichia coli." Gruer M.J., Guest J.R. Microbiology 140:2531-2541(1994) [PubMed: 8000525] [Abstract] Cited for: CHARACTERIZATION.
[7]	"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.
[8]	"E. coli aconitase B structure reveals a HEAT-like domain with implications for protein-protein recognition." Williams C.H. Jr., Stillman T.J., Barynin V.V., Sedelnikova S.E., Tang Y., Green J., Guest J.R., Artymiuk P.J. Nat. Struct. Biol. 9:447-452(2002) [PubMed: 11992126] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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Cross-references

Sequence databases

U00096 Genomic DNA. Translation: AAC73229.1.
AP009048 Genomic DNA. Translation: BAB96692.2.
U41560 Genomic DNA. Translation: AAC43710.1.

PIR

F64734.

RefSeq

AP_000779.1.
NP_414660.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L5J	X-ray	2.40	A/B	1-865	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9044N.

PTM databases

PhosSite

P36683.

2-D gel databases

SWISS-2DPAGE

P36683.

Genome annotation databases

GeneID

944864.

GenomeReviews

Gene locus JW0114 in contig AP009048_GR.
Gene locus b0118 in contig U00096_GR.

KEGG

ecj:JW0114.
eco:b0118.

Organism-specific databases

EchoBASE

EB2222.

EcoGene

EG12316. acnB.

CMR

Search...

Phylogenomic databases

HOGENOM

P36683.

OMA

P36683. VELLGTM.

Enzyme and pathway databases

BioCyc

EcoCyc:ACONITATEDEHYDRB-MON.
MetaCyc:ACONITATEDEHYDRB-MON.

BRENDA

4.2.1.3. 246.

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.
IPR015932. Aconitase/IPMdHydase_lsu_aba_2.
IPR018136. Aconitase_4Fe-4S_BS.
IPR004406. Aconitase_B_bac.
IPR015930. Aconitase_B_FeS-bd_bac.
IPR015933. Aconitase_B_HEAT-like_bac.
IPR015929. Aconitase_B_N_bac.
[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.
G3DSA:1.25.40.160. Aconitase_B_HEAT-like_bac. 1 hit.

PANTHER

PTHR11670. Aconitase-like_core. 1 hit.
PTHR11670:SF3. Aconitase_2. 1 hit.

Pfam

PF00330. Aconitase. 1 hit.
PF06434. Aconitase_2_N. 1 hit.
[Graphical view]

PIRSF

PIRSF036687. AcnB. 1 hit.

ProDom

PD000511. Aconitase_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR00117. acnB. 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

ACON2_ECOLI

Accession

Primary (citable) accession number: P36683
Secondary accession number(s): P36648, P75652, Q59382

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 91 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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