Reviewed, UniProtKB/Swiss-Prot Q6GH55 (ACON_STAAR)

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 › Bacillales › Staphylococcus

Protein attributes

Sequence length	901 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	Citrate = isocitrate.
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity.
Pathway	Carbohydrate metabolism; tricarboxylic acid cycle.
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-KW
Molecular function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: InterPro aconitate hydratase activity Inferred from electronic annotation. Source: EC iron 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	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	509	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	512	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6GH55-1 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: A7F24AF5E08F9116	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

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. , Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX571856 Genomic DNA. Translation: CAG40360.1.
RefSeq	YP_040767.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q6GH55.
Genome annotation databases
GeneID	2861357.
GenomeReviews	Gene locus SAR1362 in contig BX571856_GR.
KEGG	sar:SAR1362.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q6GH55.
OMA	RIKNEML.
Enzyme and pathway databases
BioCyc	SAUR282458:SAR1362-MON.
Family and domain databases
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015937. Aconitase-like_core. 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]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.20.19.10. Aconitase/3IPM_dehydase_swvl. 1 hit. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF1. Aconitase/Fe_reg_prot_2/AcnD. 1 hit.
Pfam	PF00330. Aconitase. 1 hit. PF00694. Aconitase_C. 1 hit. [Graphical view]
PRINTS	PR00415. ACONITASE.
ProDom	PD000511. Aconitase_N. 1 hit. [Graphical view] [Entries sharing at least one domain]
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:	November 3, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)