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A3CUF2 (CIMA_METMJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:
Putative (R)-citramalate synthase CimA

EC=2.3.1.182
Gene names
Name:cimA
Ordered Locus Names:Memar_1069
OrganismMethanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1) [Complete proteome] [HAMAP]
Taxonomic identifier368407 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanomicrobiaceaeMethanoculleus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate By similarity. HAMAP-Rule MF_01028

Catalytic activity

Acetyl-CoA + pyruvate + H2O = CoA + (2R)-2-hydroxy-2-methylbutanedioate. HAMAP-Rule MF_01028

Pathway

Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-oxobutanoate from pyruvate: step 1/3. HAMAP-Rule MF_01028

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01028

Sequence similarities

Belongs to the alpha-IPM synthase/homocitrate synthase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Putative (R)-citramalate synthase CimA HAMAP-Rule MF_01028
PRO_0000407913

Sequences

Sequence LengthMass (Da)Tools
A3CUF2 [UniParc].

Last modified March 20, 2007. Version 1.
Checksum: EA9E955BCE0B7118

FASTA50353,275
        10         20         30         40         50         60 
MIVLFVEPIR FFDTTLRDGE QTPGVSLTPA GKLEIATHLA DVGVHVIEAG SAAASVGERE 

        70         80         90        100        110        120 
SIRAIADAGL AAECCTYVRA LPGDIDLAAD AGADSVHLVV PVSDLHIAKK LRKTREQVSE 

       130        140        150        160        170        180 
MAWSAVEYAK ERGLVVELSG EDASRADQDF LAEVFREGVE RGADRLCFCD TVGLLTPERA 

       190        200        210        220        230        240 
AAIIPPLLFA PLSIHCHDDL GFGLATTVAA LRAGATCAHV TVNGLGERAG NTSLEELVMA 

       250        260        270        280        290        300 
LEVLYGVDTG IATEELYPLS THVARLTGVP LATNKPIVGE MAFTHESGIH AHGVMRDAST 

       310        320        330        340        350        360 
YEPLQPERVG RRRRIVLGKH SGSAAVEAAL HDMGYAPSAA QLKEIVDRIK RLGDAGMRIT 

       370        380        390        400        410        420 
DADIMAIADT VMEIEFTPCI ELRQFTIVSG SNAIPTASVT MLVRGEEITG AAVGTGPVDA 

       430        440        450        460        470        480 
AIRALQRSVA DVGSVRLDEY SVDAITGGTD ALVDVSVKLS KDGKTVTSRG ARTDIIMASV 

       490        500 
EAVIAGMNRL LREEHEDRSQ DSD 

« Hide

References

[1]"Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 type strain JR1."
Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., Land M. expand/collapse author list , Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.
Stand. Genomic Sci. 1:189-196(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35101 / DSM 1498 / JR1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000562 Genomic DNA. Translation: ABN57002.1.
RefSeqYP_001046984.1. NC_009051.1.

3D structure databases

ProteinModelPortalA3CUF2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING368407.Memar_1069.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABN57002; ABN57002; Memar_1069.
GeneID4847429.
KEGGmem:Memar_1069.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0119.
HOGENOMHOG000046859.
KOK09011.
OMATPIASVK.

Enzyme and pathway databases

BioCycMMAR368407:GH7L-1088-MONOMER.
UniPathwayUPA00047; UER00066.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01028. CimA.
InterProIPR013709. 2-isopropylmalate_synth_dimer.
IPR002034. AIPM/Hcit_synth_CS.
IPR013785. Aldolase_TIM.
IPR024890. Citramalate_synthase_CimA.
IPR011830. LEU1_arch.
IPR000891. PYR_CT.
[Graphical view]
PfamPF00682. HMGL-like. 1 hit.
PF08502. LeuA_dimer. 1 hit.
[Graphical view]
SMARTSM00917. LeuA_dimer. 1 hit.
[Graphical view]
SUPFAMSSF110921. SSF110921. 1 hit.
TIGRFAMsTIGR02090. LEU1_arch. 1 hit.
PROSITEPS00815. AIPM_HOMOCIT_SYNTH_1. 1 hit.
PS00816. AIPM_HOMOCIT_SYNTH_2. 1 hit.
PS50991. PYR_CT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCIMA_METMJ
AccessionPrimary (citable) accession number: A3CUF2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: March 20, 2007
Last modified: May 14, 2014
This is version 45 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