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Q8FTA8 (ACON_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aconitate hydratase

EC=4.2.1.3
Gene names
Name:acn
Ordered Locus Names:CE1661
OrganismCorynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) [Complete proteome] [HAMAP]
Taxonomic identifier196164 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length937 AA.
Sequence statusComplete.
Protein existenceInferred 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.

Sequence caution

The sequence BAC18471.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 937937Aconitate hydratase
PRO_0000076659

Sites

Metal binding4751Iron-sulfur (4Fe-4S) By similarity
Metal binding5411Iron-sulfur (4Fe-4S) By similarity
Metal binding5441Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8FTA8 [UniParc].

Last modified February 7, 2006. Version 2.
Checksum: D23E4FD27C675273

FASTA937102,106
        10         20         30         40         50         60 
MTESKNSFNA KSTLQVGEKS YDYYALSAVP GMEKLPYSLK VLGENLLRTE DGANITEEHI 

        70         80         90        100        110        120 
EAIANWDASA DPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVKTLGGD PDKVNPLNPA 

       130        140        150        160        170        180 
EMVIDHSVIV EAFGRPDALE KNVEIEYERN EERYQFLRWG SEAFSNFRVV PPGTGIVHQV 

       190        200        210        220        230        240 
NIEYLARVVF DNDGLAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP 

       250        260        270        280        290        300 
RVVGFKLTGE IPVGVTATDV VLTITEMLRD HGVVQKFVEF YGNGVKSVPL ANRATIGNMS 

       310        320        330        340        350        360 
PEFGSTCAMF PIDEETIKYL RLTGRPEEQI ALVEAYAKAQ GMWLEQDAPE AEYSEYLELD 

       370        380        390        400        410        420 
LSTVVPSIAG PKRPQDRILL SEAKEQFRED LKAYTNDPVQ VDQSIPAKRM ANEGGFQPGS 

       430        440        450        460        470        480 
TSDLDNYNAS WPGEGESAAA NAEGRPSNPV TVVSPQGGEY TIDHGMVAIA SITSCTNTSN 

       490        500        510        520        530        540 
PSVMIGAGLI ARKAAEKGLK SKPWVKTICA PGSQVVDGYY QRADLWKDLE ALGFYLSGFG 

       550        560        570        580        590        600 
CTTCIGNSGP LPEEISEAIN EHDLAATAVL SGNRNFEGRI SPDVKMNYLA SPIMVIAYAI 

       610        620        630        640        650        660 
AGTMDFDFEN EALGQDQDGN DVFLKDIWPS TEEIEETIQA AISRELYEAD YADVFKGDKQ 

       670        680        690        700        710        720 
WQELDIPSGK TFEWDENSTY IRKAPYFDGM TAEPQPVTDI ENARVLAKLG DSVTTDHISP 

       730        740        750        760        770        780 
ASSIKPGTPA AQYLDAHGVE RQDYNSLGSR RGNHEVMMRG TFANIRLQNQ LVDIAGGYTR 

       790        800        810        820        830        840 
DFTQEGGPQA FIYDACVNYK EAGIPLVVLA GKEYGTGSSR DWAAKGTNLL GVRAVITESF 

       850        860        870        880        890        900 
ERIHRSNLIG MGVVPLQFPE GESHESLGLD GTETFDITGL TALNEGTTPK TVKVTATKEN 

       910        920        930 
GEKVEFDAVV RIDTPGEADY FRHGGILQYV LRQMAAS 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC18471.1. Different initiation.
RefSeqNP_738271.1. NC_004369.1.

3D structure databases

ProteinModelPortalQ8FTA8.
ModBaseSearch...

Protein-protein interaction databases

STRING196164.CE1661.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC18471; BAC18471; BAC18471.
GeneID1032014.
KEGGcef:CE1661.
PATRIC21489469. VBICorEff9312_1655.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000025704.
KOK01681.
ProtClustDBPRK09277.

Enzyme and pathway databases

UniPathwayUPA00223; UER00718.

Family and domain databases

Gene3D3.20.19.10. 1 hit.
3.30.499.10. 3 hits.
3.40.1060.10. 1 hit.
InterProIPR015931. Acnase/IPM_dHydase_lsu_aba_1/3.
IPR015937. Acoase/IPM_deHydtase.
IPR001030. Acoase/IPM_deHydtase_lsu_aba.
IPR015928. Aconitase/3IPM_dehydase_swvl.
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]
PANTHERPTHR11670. PTHR11670. 1 hit.
PTHR11670:SF1. PTHR11670:SF1. 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.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACON_COREF
AccessionPrimary (citable) accession number: Q8FTA8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: May 1, 2013
This is version 71 of the entry and version 2 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