Aconitate hydratase - Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)

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Q6NH63 (ACON_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. History...

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

Documents (2) |

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
EC=4.2.1.3

Gene names

Name:	acn
Synonyms:	acnA
Ordered Locus Names:	DIP1283

Organism

Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis) [Complete proteome] [HAMAP]

Taxonomic identifier

257309 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium ›

Protein attributes

Sequence length	934 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the isomerization of citrate to isocitrate via cis-aconitate By similarity.
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.
Induction	Repressed by AcnR By similarity.
Sequence similarities	Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro 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 – 934

934

Aconitate hydratase

PRO_0000076658

Sites

Metal binding

473

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

Metal binding

539

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

Metal binding

542

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q6NH63 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 52CD61FBBFBB90BC
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FASTA

934

101,158

        10         20         30         40         50         60 
MTESKNSFNA KQTLEVGDKS YDYFALSAVK GMEKLPYSLK VLGENLLRTE DGANITADHI 

        70         80         90        100        110        120 
NAIANWDPSA EPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVKTLGGD PDKVNPLNPA 

       130        140        150        160        170        180 
EMVIDHSVII EAFGSTLALA KNVEIEYERN EERYQFLRWG SKAFSNFRVV PPGTGIVHQV 

       190        200        210        220        230        240 
NIENLARVVF DNNGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP 

       250        260        270        280        290        300 
RVVGFKLTGE IPAGVTATDV VLTITEMLRE HGVVQKFVEF YGNGVKSIPL ANRATIGNMS 

       310        320        330        340        350        360 
PEFGSTCAIF PIDEETVKYM HLTGRSEEQV ALVEAYAKAQ GMWLEQDAPE AEYSEYLELD 

       370        380        390        400        410        420 
LSTVVPSIAG PKRPQDRILL TEAKEQFRKD LPDYCSAEPV DESLPAKRMD SEGAVQKEGE 

       430        440        450        460        470        480 
DVAGYNSSRA GHGESAAEGA AGRQSNPVVV SSPNGGEYTL DHGMVAIASI TSCTNTSNPS 

       490        500        510        520        530        540 
VMIGAGLIAR KAAAKGLKAK PWVKTICAPG SQVVDGYYKR ADLWKDLEAL GFYLSGFGCT 

       550        560        570        580        590        600 
TCIGNSGPLP EEISAAINEN DLTATAVLSG NRNFEGRISP DVKMNYLVSP IMVIAYAIAG 

       610        620        630        640        650        660 
TMDFDFETQP LGQDIDGNDV FLKDIWPSTE EIEETIAGAI SRELYEADYA DVFKGDEQWQ 

       670        680        690        700        710        720 
NLPTPEGKTF DWDEKSTYIR KAPYFDGMTM EPAPVSDIKG ARVLAKLGDS VTTDHISPAS 

       730        740        750        760        770        780 
SIKPGTPAAQ YLDENGVARN DYNSLGSRRG NHEVMMRGTF ANIRLQNQLV DIAGGYTRDF 

       790        800        810        820        830        840 
TKNGEQAFIF DACQNYKAAG IPLVVIAGKE YGTGSSRDWA AKGTNLLGVK AVITESFERI 

       850        860        870        880        890        900 
HRSNLIGMGV IPLQFPAGES HASLGLDGTE TFDIEGIEEL NNGVTPKTVH VTATKESGDQ 

       910        920        930 
VEFDAVVRID TPGEADYYRN GGILQYVLRN MINA

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References

[1]

"The complete genome sequence and analysis of Corynebacterium diphtheriae NCTC13129."
Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G., Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D., De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K., Moule S.

Parkhill J.
Nucleic Acids Res. 31:6516-6523(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700971 / NCTC 13129 / Biotype gravis.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX248357 Genomic DNA. Translation: CAE49810.1.
3D structure databases
ProteinModelPortal	Q6NH63.
ModBase	Search...
Protein-protein interaction databases
STRING	257309.DIP1283.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE49810; CAE49810; DIP1283.
PATRIC	21483758. VBICorDip47633_1262.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1048.
HOGENOM	HOG000025703.
OMA	YSKAQGM.
ProtClustDB	PRK09277.
Enzyme and pathway databases
UniPathway	UPA00223; UER00718.
Family and domain databases
Gene3D	3.20.19.10. 1 hit. 3.30.499.10. 3 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. 2 hits. 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

ACON_CORDI

Accession

Primary (citable) accession number: Q6NH63

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

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

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents