Aconitate hydratase - Staphylococcus aureus (strain MRSA252)

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Q6GH55 (ACON_STAAR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 63. 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
Short name=Aconitase
EC=4.2.1.3

Alternative name(s):
Citrate hydro-lyase

Gene names

Name:	acnA
Synonyms:	citB
Ordered Locus Names:	SAR1362

Organism

Staphylococcus aureus (strain MRSA252) [Complete proteome] [HAMAP]

Taxonomic identifier

282458 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus ›

Protein attributes

Sequence length	901 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.
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 – 901

901

Aconitate hydratase

PRO_0000076669

Sites

Metal binding

443

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

Metal binding

509

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

Metal binding

512

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

Sequences

Sequence

Length

Mass (Da)

Tools

Q6GH55 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: A7F24AF5E08F9116
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FASTA

901

98,912

        10         20         30         40         50         60 
MAANFKEQSK KHFDLNGQSY TYYDLKAVEE QGITKVSKLP YSIRVLLESL LRQEDDFVIT 

        70         80         90        100        110        120 
DDHIKALSQF GKDGNEGEVP FKPSRVILQD FTGVPAVVDL ASLRKAMDDV GGDITKINPE 

       130        140        150        160        170        180 
VPVDLVIDHS VQVDSYANPE ALERNMKLEF ERNYERYQFL NWATKAFDNY NAVPPATGIV 

       190        200        210        220        230        240 
HQVNLEYLAS VVHVRDVDGE KTAFPDTLVG TDSHTTMING IGVLGWGVGG IEAEAGMLGQ 

       250        260        270        280        290        300 
PSYFPIPEVI GVRLVNSLPQ GATATDLALR VTQELRKKGV VGKFVEFFGP GVQHLPLADR 

       310        320        330        340        350        360 
ATIANMAPEY GATCGFFPVD DESLKYMKLT GRSDEHIALV KEYLKQNHMF FDVEKEDPNY 

       370        380        390        400        410        420 
TDVIELDLST VEASLSGPKR PQDLIFLSDM KSSFENSVTA PAGNQGHGLD KSEFDKKAEI 

       430        440        450        460        470        480 
NFKDGSKATM KTGDIAIAAI TSCTNTSNPY VMLGAGLVAK KAVEKGLKVP EYVKTSLAPG 

       490        500        510        520        530        540 
SKVVTGYLRG AGLQPYLDDL GFNLVGYGCT TCIGNSGPLL PEIEKAIADE DLLVTSVLSG 

       550        560        570        580        590        600 
NRNFEGRIHP LVKANYLASP QLVVAYALAG SVDIDLQNEP IGKGNDGEDV YLKDIWPSIK 

       610        620        630        640        650        660 
EVSDTVDSVV TPELFIEEYN NVYNNNELWN EIDVTDQPLY DFDPNSTYIQ NPSFFQGLSK 

       670        680        690        700        710        720 
EPGTIVPLNG LRVMGKFGDS VTTDHISPAG AIGKDTPAGK YLQDHQVPIR EFNSYGSRRG 

       730        740        750        760        770        780 
NHEVMVRGTF ANIRIKNQLA PGTEGGFTTY WPTNEVMPIF DAAMKYKEDG TGLVVLAGND 

       790        800        810        820        830        840 
YGMGSSRDWA AKGTNLLGVK TVIAQSYERI HRSNLVMMGV LPLEFKKGES ADSLGLDGTE 

       850        860        870        880        890        900 
EISVNIDENV QPHDYVKVTA KKQDGDLVEF DAMVRFDSLV EMDYYRHGGI LQMVLRNKLA 


Q

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References

[1]

"Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance."
Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C.

Parkhill J.
Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MRSA252.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571856 Genomic DNA. Translation: CAG40360.1.
RefSeq	YP_040767.1. NC_002952.2.
3D structure databases
ProteinModelPortal	Q6GH55.
SMR	Q6GH55. Positions 7-899.
ModBase	Search...
Protein-protein interaction databases
STRING	282458.SAR1362.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAG40360; CAG40360; SAR1362.
GeneID	2861357.
KEGG	sar:SAR1362.
PATRIC	19546267. VBIStaAur71814_1363.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1048.
HOGENOM	HOG000025704.
KO	K01681.
OMA	DEALYKW.
ProtClustDB	PRK09277.
Enzyme and pathway databases
BioCyc	SAUR282458:GJA5-1361-MONOMER.
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. 1 hit. 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_STAAR

Accession

Primary (citable) accession number: Q6GH55

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 63 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