Aconitate hydratase 2 - Helicobacter pylori (strain ATCC 700392 / 26695)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Aconitate hydratase 2
Short name=Aconitase 2
EC=4.2.1.3

Alternative name(s):
2-methylisocitrate dehydratase
EC=4.2.1.99
Citrate hydro-lyase 2

Gene names

Name:	acnB
Ordered Locus Names:	HP_0779

Organism

Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP]

Taxonomic identifier

85962 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length	852 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate as well as the dehydration of 2-methylisocitrate to cis-2-methylaconitate By similarity.
Catalytic activity	Citrate = isocitrate. (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H₂O.
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.
Sequence caution	The sequence AAD07828.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytosol Inferred from electronic annotation. Source: InterPro
Molecular_function	2-methylisocitrate dehydratase activity Inferred from electronic annotation. Source: EC 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW citrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC isocitrate hydro-lyase (cis-aconitate-forming) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 852

852

Aconitate hydratase 2

PRO_0000076676

Regions

Region

237 – 239

3

Substrate binding By similarity

Region

405 – 407

3

Substrate binding By similarity

Sites

Metal binding

708

1

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

Metal binding

766

1

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

Metal binding

769

1

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

Binding site

194

1

Substrate By similarity

Binding site

489

1

Substrate By similarity

Binding site

788

1

Substrate By similarity

Binding site

793

1

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P56418 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 7051382D8A0D0AB3
Show »

FASTA

852

92,663

        10         20         30         40         50         60 
MKDFLEDYKK SVSERGSEGI PPLPLNAKQV QAVVEILTKD PTNAAFAKEL LIHRVSPGVD 

        70         80         90        100        110        120 
EGAKVKAEFL AKLSQKKLEC VHISALEATT LLGTMLGGYN VEPLIMGLES QDKNIAKESA 

       130        140        150        160        170        180 
KALKTTLLVY GSFDKIAAMS KTNALAKEVL ESWANAEWFL NKEPLNECIE ACVFKIDGET 

       190        200        210        220        230        240 
NTDDLSPASD AFTRSDIPLH AKAMLKNRIE NYEQRIKAIK TKGVPVAYVG DVVGTGSSRK 

       250        260        270        280        290        300 
SATNSIMWHF GKDIPFVPNK RSGGIVIGGV IAPIFFATCE DSGALPIVAD VKDLKEGDLI 

       310        320        330        340        350        360 
KIYPYKGEIT LNDKVVSTFK LEPETLLDEV RASGRIPLII GRGLTNKARK FLGLGESEAF 

       370        380        390        400        410        420 
KKPSAPKSDA KGYTLAQKIV GHACGVKGIL PGTYCEPKVT TVGSQDTTGA MTRDEVKELA 

       430        440        450        460        470        480 
SLKFDAPFVL QSFCHTAAYP KPSDVSLHAT LPGFITQRGG VALHPGDGVI HTWLNRMGLP 

       490        500        510        520        530        540 
DTLGTGGDSH TRFPLGISFP AGSGLVAFAA VTGTMPLNMP ESVLVRFKGE MNPGITLRDL 

       550        560        570        580        590        600 
VNAIPYYAIK KGLLTVEKKG KINVFNGRIL EIEGLPDIKM EQAFELSDAS AERSAAACVV 

       610        620        630        640        650        660 
RLNKEPMIEY LKSNIKLIDE MIASGYEDKE TLKKRRDAMQ AWVDNPVLLE PDSNAQYAAV 

       670        680        690        700        710        720 
IEIDVAEITE PILACPNDPD DVATLSEVLA DTTGKRPHAI DEVFIGSCMT NIGHFRAFGE 

       730        740        750        760        770        780 
IVKNAPPSQA RLWVVPPSKM DEQELINEGY YAIFGAAGAR TEVPGCSLCM GNQARVRDNA 

       790        800        810        820        830        840 
VVFSTSTRNF DNRMGRGAKV YLGSAELGAA CALLGRIPTK EEYMNLVSEK LESQKDKIYR 

       850 
YMNFNLMENF RL

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References

[1]

"The complete genome sequence of the gastric pathogen Helicobacter pylori."
Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J.

Venter J.C.
Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700392 / 26695.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000511 Genomic DNA. Translation: AAD07828.1. Different initiation.
PIR	C64617.
RefSeq	NP_207572.1. NC_000915.1. YP_006934694.1. NC_018939.1.
3D structure databases
ProteinModelPortal	P56418.
SMR	P56418. Positions 5-850.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-3210N.
MINT	MINT-175591.
STRING	85962.HP0779.
Proteomic databases
PRIDE	P56418.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAD07828; AAD07828; HP_0779.
GeneID	13869963. 900338.
KEGG	heo:C694_04000. hpy:HP0779.
PATRIC	20592847. VBIHelPyl33062_0812.
Phylogenomic databases
eggNOG	COG1049.
KO	K01682.
OMA	NVFNGRI.
ProtClustDB	PRK09238.
Enzyme and pathway databases
UniPathway	UPA00223; UER00718.
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. 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]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF3. PTHR11670:SF3. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF06434. Aconitase_2_N. 1 hit. PF11791. Aconitase_B_N. 1 hit. [Graphical view]
PIRSF	PIRSF036687. AcnB. 1 hit.
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit. SSF74778. Aconitase_B_HEAT-like_bac. 1 hit. SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR00117. acnB. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACON2_HELPY

Accession

Primary (citable) accession number: P56418

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Helicobacter pylori

Helicobacter pylori (strain 26695): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents