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Q6NH63 (ACON_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aconitate hydratase
EC=4.2.1.3
Gene names
Name:acn
Synonyms:acnA
Ordered Locus Names:DIP1283
OrganismCorynebacterium diphtheriae [Complete proteome] [HAMAP]
Taxonomic identifier1717 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium

Protein attributes

Sequence length934 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 934934Aconitate hydratase
PRO_0000076658

Sites

Metal binding4731Iron-sulfur (4Fe-4S) By similarity
Metal binding5391Iron-sulfur (4Fe-4S) By similarity
Metal binding5421Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NH63 [UniParc].

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

FASTA934101,158
        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

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BX248357 Genomic DNA. Translation: CAE49810.1.
RefSeqNP_939635.2. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NH63.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2649836.
GenomeReviewsGene locus DIP1283 in contig BX248353_GR.
KEGGcdi:DIP1283.
NMPDRfig|257309.1.peg.1226.
PATRIC21483758. VBICorDip47633_1262.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG289738.
OMAYSKAQGM.
PhylomeDBQ6NH63.
ProtClustDBPRK09277.

Enzyme and pathway databases

BioCycCDIP257309:DIP1283-MONOMER.

Family and domain databases

InterProIPR015931. 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]
Gene3DG3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 3 hits.
G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit.
G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
KOK01681.
PANTHERPTHR11670. Aconitase-like_core. 1 hit.
PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
PfamPF00330. Aconitase. 2 hits.
PF00694. Aconitase_C. 1 hit.
[Graphical view]
PRINTSPR00415. ACONITASE.
SUPFAMSSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
SSF53732. Aconitase_N. 1 hit.
TIGRFAMsTIGR01341. Aconitase_1. 1 hit.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACON_CORDI
AccessionPrimary (citable) accession number: Q6NH63
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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