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Protein

Carboxy-S-adenosyl-L-methionine synthase

Gene

cmoA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).UniRule annotation1 Publication

Catalytic activityi

Prephenate + S-adenosyl-L-methionine = phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391S-adenosyl-L-methionineUniRule annotation2 Publications
Binding sitei132 – 1321S-adenosyl-L-methionineUniRule annotation2 Publications
Binding sitei199 – 1991S-adenosyl-L-methionineUniRule annotation2 Publications

GO - Molecular functioni

GO - Biological processi

  • methylation Source: GO_Central
  • tRNA wobble uridine modification Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciEcoCyc:G7020-MONOMER.
ECOL316407:JW1859-MONOMER.
MetaCyc:G7020-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxy-S-adenosyl-L-methionine synthaseUniRule annotationCurated (EC:2.1.3.-UniRule annotation1 Publication)
Short name:
Cx-SAM synthase1 PublicationUniRule annotation
Gene namesi
Name:cmoA2 PublicationsUniRule annotation
Synonyms:yecO
Ordered Locus Names:b1870, JW1859
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14033. cmoA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi89 – 891D → L: Lack of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247Carboxy-S-adenosyl-L-methionine synthasePRO_0000169083Add
BLAST

Proteomic databases

PaxDbiP76290.
PRIDEiP76290.

2D gel databases

SWISS-2DPAGEP76290.

Interactioni

Subunit structurei

Homodimer.UniRule annotation1 Publication

Protein-protein interaction databases

BioGridi4263500. 11 interactions.
IntActiP76290. 6 interactions.
MINTiMINT-7290797.
STRINGi511145.b1870.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 3516Combined sources
Helixi39 – 5315Combined sources
Beta strandi59 – 646Combined sources
Turni66 – 683Combined sources
Helixi69 – 768Combined sources
Beta strandi80 – 823Combined sources
Beta strandi84 – 907Combined sources
Helixi92 – 10312Combined sources
Beta strandi111 – 1166Combined sources
Turni118 – 1203Combined sources
Beta strandi125 – 1339Combined sources
Helixi135 – 1373Combined sources
Helixi140 – 15314Combined sources
Beta strandi154 – 16613Combined sources
Helixi171 – 18717Combined sources
Helixi190 – 1923Combined sources
Helixi196 – 2038Combined sources
Helixi211 – 22111Combined sources
Beta strandi224 – 2329Combined sources
Beta strandi235 – 2417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GEKX-ray1.50A/G1-247[»]
4IWNX-ray1.73A/B19-247[»]
ProteinModelPortaliP76290.
SMRiP76290. Positions 15-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni64 – 663S-adenosyl-L-methionine bindingUniRule annotation2 Publications
Regioni89 – 902S-adenosyl-L-methionine bindingUniRule annotation2 Publications
Regioni117 – 1182S-adenosyl-L-methionine bindingUniRule annotation2 Publications

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. Cx-SAM synthase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiENOG4105DA6. Bacteria.
COG0500. LUCA.
HOGENOMiHOG000218457.
InParanoidiP76290.
KOiK15256.
OMAiMIELYYL.
OrthoDBiEOG628F44.
PhylomeDBiP76290.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01589. Cx_SAM_synthase.
InterProiIPR029063. SAM-dependent_MTases.
IPR005271. tRNA_cmo5U34_MeTrfase.
[Graphical view]
PIRSFiPIRSF006325. MeTrfase_bac. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00740. TIGR00740. 1 hit.

Sequencei

Sequence statusi: Complete.

P76290-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHRDTLFSA PIARLGDWTF DERVAEVFPD MIQRSVPGYS NIISMIGMLA
60 70 80 90 100
ERFVQPGTQV YDLGCSLGAA TLSVRRNIHH DNCKIIAIDN SPAMIERCRR
110 120 130 140 150
HIDAYKAPTP VDVIEGDIRD IAIENASMVV LNFTLQFLEP SERQALLDKI
160 170 180 190 200
YQGLNPGGAL VLSEKFSFED AKVGELLFNM HHDFKRANGY SELEISQKRS
210 220 230 240
MLENVMLTDS VETHKARLHN AGFEHSELWF QCFNFGSLVA LKAEDAA
Length:247
Mass (Da):27,777
Last modified:February 1, 1997 - v1
Checksum:i2930565435F5A7F4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74940.1.
AP009048 Genomic DNA. Translation: BAA15680.1.
PIRiF64949.
RefSeqiNP_416384.1. NC_000913.3.
WP_000019590.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74940; AAC74940; b1870.
BAA15680; BAA15680; BAA15680.
GeneIDi946380.
KEGGiecj:JW1859.
eco:b1870.
PATRICi32119063. VBIEscCol129921_1949.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74940.1.
AP009048 Genomic DNA. Translation: BAA15680.1.
PIRiF64949.
RefSeqiNP_416384.1. NC_000913.3.
WP_000019590.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4GEKX-ray1.50A/G1-247[»]
4IWNX-ray1.73A/B19-247[»]
ProteinModelPortaliP76290.
SMRiP76290. Positions 15-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263500. 11 interactions.
IntActiP76290. 6 interactions.
MINTiMINT-7290797.
STRINGi511145.b1870.

2D gel databases

SWISS-2DPAGEP76290.

Proteomic databases

PaxDbiP76290.
PRIDEiP76290.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74940; AAC74940; b1870.
BAA15680; BAA15680; BAA15680.
GeneIDi946380.
KEGGiecj:JW1859.
eco:b1870.
PATRICi32119063. VBIEscCol129921_1949.

Organism-specific databases

EchoBASEiEB3787.
EcoGeneiEG14033. cmoA.

Phylogenomic databases

eggNOGiENOG4105DA6. Bacteria.
COG0500. LUCA.
HOGENOMiHOG000218457.
InParanoidiP76290.
KOiK15256.
OMAiMIELYYL.
OrthoDBiEOG628F44.
PhylomeDBiP76290.

Enzyme and pathway databases

BioCyciEcoCyc:G7020-MONOMER.
ECOL316407:JW1859-MONOMER.
MetaCyc:G7020-MONOMER.

Miscellaneous databases

PROiP76290.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01589. Cx_SAM_synthase.
InterProiIPR029063. SAM-dependent_MTases.
IPR005271. tRNA_cmo5U34_MeTrfase.
[Graphical view]
PIRSFiPIRSF006325. MeTrfase_bac. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
TIGRFAMsiTIGR00740. TIGR00740. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "S-adenosyl-S-carboxymethyl-L-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA."
    Byrne R.T., Whelan F., Aller P., Bird L.E., Dowle A., Lobley C.M., Reddivari Y., Nettleship J.E., Owens R.J., Antson A.A., Waterman D.G.
    Acta Crystallogr. D 69:1090-1098(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 19-247 IN COMPLEX WITH CARBOXY-S-ADENOSYL-METHIONINE, SUBUNIT.
  5. "Structure-guided discovery of the metabolite carboxy-SAM that modulates tRNA function."
    Kim J., Xiao H., Bonanno J.B., Kalyanaraman C., Brown S., Tang X., Al-Obaidi N.F., Patskovsky Y., Babbitt P.C., Jacobson M.P., Lee Y.S., Almo S.C.
    Nature 498:123-126(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH CARBOXY-S-ADENOSYL-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-89.

Entry informationi

Entry nameiCMOA_ECOLI
AccessioniPrimary (citable) accession number: P76290
Secondary accession number(s): O07982
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: May 11, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Mechanistic analyses show the involvement of a unique ylide intermediate as the carboxyl acceptor in the conversion of SAM to Cx-SAM.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.