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A0QX20 (ACON_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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:acnA
Synonyms:acn
Ordered Locus Names:MSMEG_3143, MSMEI_3062
OrganismMycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]
Taxonomic identifier246196 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length943 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Sequence similarities

Belongs to the aconitase/IPM isomerase family.

Ontologies

Keywords
   Biological processTricarboxylic acid cycle
   LigandIron
Iron-sulfur
Metal-binding
   Molecular functionLyase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processtricarboxylic acid cycle

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionaconitate hydratase activity

Inferred from electronic annotation. Source: UniProtKB-EC

iron-sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 943943Aconitate hydratase
PRO_0000396818

Sites

Metal binding4781Iron-sulfur (4Fe-4S) By similarity
Metal binding5441Iron-sulfur (4Fe-4S) By similarity
Metal binding5471Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Cross-link394Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Sequences

Sequence LengthMass (Da)Tools
A0QX20 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: BD10F939FA09F201

FASTA943102,171
        10         20         30         40         50         60 
MSSENTGKSS LNSFGARDTL TVGDQSYEIY RLNAVPGTEK LPYSLKVLAE NLLRTEDGAN 

        70         80         90        100        110        120 
ITKDHIEAIA NWDPNAEPSI EIQFTPARVI MQDFTGVPCI VDLATMREAV AALGGDPNKV 

       130        140        150        160        170        180 
NPLAPAELVI DHSVILDVFG NASAFERNVE LEYERNAERY QFLRWGQGAF DDFKVVPPGT 

       190        200        210        220        230        240 
GIVHQVNIEY LARTVMVRDG VAYPDTCVGT DSHTTMVNGL GVLGWGVGGI EAEAAMLGQP 

       250        260        270        280        290        300 
VSMLIPRVVG FKLSGEIKPG VTATDVVLTV TDMLRRHGVV GKFVEFYGKG VAEVPLANRA 

       310        320        330        340        350        360 
TLGNMSPEFG STAAIFPIDE ETINYLRLTG RTDEQLALVE AYAKAQGMWH DPEREPVFSE 

       370        380        390        400        410        420 
YLELDLSTVV PSISGPKRPQ DRIELTDAKN AFRKDIHNYV EQNHPTPETK LDEAVEESFP 

       430        440        450        460        470        480 
ASDPVSLSFA DDGAPDMRPS AANGATGRPT NPVLVHSEER GDFVLDHGAV VVAGITSCTN 

       490        500        510        520        530        540 
TSNPSVMLGA ALLAKKAVEK GLTTKPWVKT NMAPGSQVVT DYYNKAGLWP YLEKLGYYLG 

       550        560        570        580        590        600 
GYGCTTCIGN TGPLPEEISK AINDNDLAVT AVLSGNRNFE GRISPDVKMN YLASPPLVIA 

       610        620        630        640        650        660 
YGIAGTMDFD FESDPLGQDS EGNDVFLRDI WPSAAEIEET IASSINREMF TESYADVFKG 

       670        680        690        700        710        720 
DDRWRSLPTP EGDTFEWDPA STYVRKAPYF DGMPAEPEPV SDIKGARVLA LLGDSVTTDH 

       730        740        750        760        770        780 
ISPAGAIKPG TPAAQYLDAN GVERKDYNSL GSRRGNHEVM IRGTFANIRL RNQLLDDVSG 

       790        800        810        820        830        840 
GYTRDFTQPG GPQAFIYDAS ENYKKAGIPL VVLGGKEYGS GSSRDWAAKG TVLLGVKAVI 

       850        860        870        880        890        900 
TESFERIHRS NLIGMGVIPL QFPAGESAAS LKLDGTETYD IEGIEELNSG KTPKTVHVTA 

       910        920        930        940 
TKEDGSKVEF DAVVRIDTPG EADYYRNGGI LQYVLRNMLK SSK 

« Hide

References

« Hide 'large scale' references
[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[2]"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[3]"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700084 / mc(2)155.
[4]"Expansion of the mycobacterial 'PUPylome'."
Watrous J., Burns K., Liu W.T., Patel A., Hook V., Bafna V., Barry C.E. III, Bark S., Dorrestein P.C.
Mol. Biosyst. 6:376-385(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PUPYLATION AT LYS-394, IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ866855 Genomic DNA. Translation: ABJ96316.1.
CP000480 Genomic DNA. Translation: ABK73859.1.
CP001663 Genomic DNA. Translation: AFP39526.1.
RefSeqYP_006567821.1. NC_018289.1.
YP_887458.1. NC_008596.1.

3D structure databases

ProteinModelPortalA0QX20.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING246196.MSMEG_3143.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK73859; ABK73859; MSMEG_3143.
AFP39526; AFP39526; MSMEI_3062.
GeneID13425429.
4536477.
KEGGmsg:MSMEI_3062.
msm:MSMEG_3143.
PATRIC18078710. VBIMycSme59918_3103.

Phylogenomic databases

eggNOGCOG1048.
HOGENOMHOG000025704.
KOK01681.
OMASVMMAAG.
OrthoDBEOG67DPHM.
ProtClustDBCLSK781226.

Enzyme and pathway databases

BioCycMSME246196:GJ4Y-3143-MONOMER.
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. SSF52016. 1 hit.
SSF53732. SSF53732. 2 hits.
PROSITEPS00450. ACONITASE_1. 1 hit.
PS01244. ACONITASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACON_MYCS2
AccessionPrimary (citable) accession number: A0QX20
Secondary accession number(s): A4ZHS6, I7G8K0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 2007
Last modified: November 13, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways