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Q59938 (ACON_STRMU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. 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
Short name=Aconitase
EC=4.2.1.3
Alternative name(s):
Citrate hydro-lyase
Gene names
Name:acn
Synonyms:citB
Ordered Locus Names:SMU_670
OrganismStreptococcus mutans [Complete proteome] [HAMAP]
Taxonomic identifier1309 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Lactobacillales › Streptococcaceae › Streptococcus

Protein attributes

Sequence length888 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.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 888888Aconitate hydratase
PRO_0000076674

Sites

Metal binding4331Iron-sulfur (4Fe-4S) By similarity
Metal binding4991Iron-sulfur (4Fe-4S) By similarity
Metal binding5021Iron-sulfur (4Fe-4S) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q59938 [UniParc].

Last modified November 28, 2002. Version 2.
Checksum: 87D3F8D315DC5BBE

FASTA88898,054
        10         20         30         40         50         60 
MINYTSTFTL NRQKYHYIDL VKASKDYDIE LDSLPYTIKI LLESLLRKHD DICVTKNNIE 

        70         80         90        100        110        120 
TLFHYNSKAP QGEVPFKPSR VILQDFTGVP VVVDLASMRD AVVENGGSPD LINPEIPVDL 

       130        140        150        160        170        180 
VIDHSVQVDF FGNQDAFDAN IDLEFERNNE RYEFLKWAEK TFENYRAVPP ATGIIHQVNL 

       190        200        210        220        230        240 
EFLSDVIINK DGFLYPDSMF GTDSHTTMIN GIGVLGWGVG GIEAEAAMLG EASYFPIPEV 

       250        260        270        280        290        300 
IGVRLYGELP KVATATDLAL KVTQKLRLEN VVGKFVEFFG PGLAGLSLAD RATVANMAPE 

       310        320        330        340        350        360 
YGATCGYFPI DDETLNYMKL TNRSAEHIAL TKEYAKRNHL YHDMTNLPSY TKIVEIDLSA 

       370        380        390        400        410        420 
IKPSISGPKR PQDLIELGQA KEEFQASLVR QFGVRGFGLG ADELAKKATV HFDDGQELEV 

       430        440        450        460        470        480 
KTGHVAIAAI TSCTNTSNPY VLLSAGLLAK KAVERGLSVA KTVKTSLAPG SKVVTAYLRK 

       490        500        510        520        530        540 
SGLQPYLDKL GFNLVGYGCT TCIGNSGDLV PEVAKAVQEK DLLVSAVLSG NRNFEGRVNP 

       550        560        570        580        590        600 
LVKANFLASP PLVVAYALAG TTNIDLTSKP LGYDKNGQAV YLEDIMPAKE EVLSYIEQFV 

       610        620        630        640        650        660 
TAELFEEEYG HVFSDSQKWN QIETENSKNY QWNQVSTYIQ NPPYFENLTN TENKIDLSAL 

       670        680        690        700        710        720 
KVLAKFGDSV TTDHISPAGN IARNSPAARY LEENGVTYAE FNSYGSRRGN HEVMMRGTFA 

       730        740        750        760        770        780 
NIRIKNELAD GKIGGYTKYE GEILPIYEAA MNYKKNGVST IVIAGKDYGM GSSRDWAAKG 

       790        800        810        820        830        840 
ANLLGVKVVL AESFERIHRS NLVMMGILPL QFLDGQTAES LQLTGYETYT VELPEQPQVH 

       850        860        870        880 
DIVKVKATSK EGTKEFQVLL RFDADADIRY YQNGGILPMV VRKKLNGG

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Streptococcus mutans UA159, a cariogenic dental pathogen."
Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B., Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S., Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.
Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002) [PubMed: 12397186] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700610 / UA159 / Serotype c.
[2]"Role of the citrate pathway in glutamate biosynthesis by Streptococcus mutans."
Cvitkovitch D.G., Gutierrez J.A., Bleiweis A.S.
J. Bacteriol. 179:650-655(1997) [PubMed: 9006016] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 626-888.
Strain: JH1005.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE014133 Genomic DNA. Translation: AAN58404.1.
U62799 Genomic DNA. Translation: AAC44824.1.
RefSeqNP_721098.1. NC_004350.2.

3D structure databases

ProteinModelPortalQ59938.
SMRQ59938. Positions 4-885.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTRT00000013762; EBSTRP00000013244; EBSTRG00000013762.
GeneID1028091.
GenomeReviewsGene locus SMU_670 in contig AE014133_GR.
KEGGsmu:SMU_670.
NMPDRfig|210007.1.peg.611.
PATRIC19663525. VBIStrMut61772_0595.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000029366.
HOGENOMHBG289738.
OMAKEVYANI.
ProtClustDBPRK09277.

Enzyme and pathway databases

BioCycSMUT210007:SMU_670-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. 1 hit.
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_STRMU
AccessionPrimary (citable) accession number: Q59938
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 28, 2002
Last modified: January 25, 2012
This is version 82 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

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