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Protein

Carnosine N-methyltransferase

Gene

YNL092W

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

N-methyltransferase that mediates the formation of anserine (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Also methylates other L-histidine-containing di- and tripeptides such as Gly-Gly-His, Gly-His and homocarnosine (GABA-His).1 Publication

Catalytic activityi

S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + anserine.1 Publication

Kineticsi

kcat is 0.38 min(-1) for carnosine. kcat is 0.74 min(-1) for S-adenosyl-L-methionine.1 Publication

  1. KM=21.50 mM for carnosine1 Publication
  2. KM=0.002 mM for S-adenosyl-L-methionine1 Publication
  1. Vmax=7.89 nmol/min/mg enzyme with carnosine as substrate1 Publication

pH dependencei

Optimum pH is 7.0-7.5.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius.1 Publication

GO - Molecular functioni

  • S-adenosylmethionine-dependent methyltransferase activity Source: SGD

GO - Biological processi

  • protein methylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciYEAST:G3O-33120-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Carnosine N-methyltransferase1 Publication (EC:2.1.1.221 Publication)
Gene namesi
Ordered Locus Names:YNL092W
ORF Names:N2227
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL092w.
EuPathDBiFungiDB:YNL092W.
SGDiS000005036. YNL092W.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 400400Carnosine N-methyltransferasePRO_0000203441Add
BLAST

Proteomic databases

PaxDbiP53934.
PRIDEiP53934.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself1EBI-28794,EBI-28794
BZZ1P388221EBI-28794,EBI-3889
FIP1P459761EBI-28794,EBI-6940
JJJ3P471381EBI-28794,EBI-25576
KGD2P192621EBI-28794,EBI-12464
SCD5P347581EBI-28794,EBI-16685
YAP6Q039351EBI-28794,EBI-37603
YML037CQ037031EBI-28794,EBI-27772

Protein-protein interaction databases

BioGridi35732. 18 interactions.
DIPiDIP-1880N.
IntActiP53934. 10 interactions.
MINTiMINT-391242.

Structurei

3D structure databases

ProteinModelPortaliP53934.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG323736.
GeneTreeiENSGT00390000005323.
HOGENOMiHOG000204444.
InParanoidiP53934.
OrthoDBiEOG7ZKSMD.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR012901. N2227.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF07942. N2227. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.

Sequencei

Sequence statusi: Complete.

P53934-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDENEFDNQR ENKAVARVII SFLKYEEYAL KEIYNLRVKK WASISDRQKD
60 70 80 90 100
MVPNYTKYLA NLKAAIIENG KFFRSVAEYA LQSISFEPGE IVQPNDLDMS
110 120 130 140 150
KTCSLLTQVY REWSAEAISE RNCLNSRLVP FLKTLSPPKA DILIPGCGTG
160 170 180 190 200
RLLVDLSRMG YNCEGNEFSY HMLLVSQYML NAGLLQNQII IYPFIHCFSH
210 220 230 240 250
WKKIEDQLSP IKVPDIEAWS SNKGMGSMSI CAGSFVDCYG RNQGTKISSH
260 270 280 290 300
YTFSRRMQLS RAKAENSKDV VVTNFFIDTG SNILDYLDTI GHVLKPGGIW
310 320 330 340 350
CNFGPLLYHF ENDHGVETTY EVNPYSGFQD KINDYTPLMG LELSSDDIIS
360 370 380 390 400
IATNHLDFEL IRRESGILCG YGRYAGPESC AMPGYMCHYW ILKSNPTNES
Length:400
Mass (Da):45,497
Last modified:October 1, 1996 - v1
Checksum:i6B6C051891F075EE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421A → E in strain: SK1.
Natural varianti154 – 1541V → M in strain: SK1.
Natural varianti317 – 3171E → D in strain: SK1.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85811 Genomic DNA. Translation: CAA59825.1.
DQ115393 Genomic DNA. Translation: AAZ22516.1.
Z71368 Genomic DNA. Translation: CAA95968.1.
BK006947 Genomic DNA. Translation: DAA10454.1.
PIRiS52733.
RefSeqiNP_014307.1. NM_001182930.1.

Genome annotation databases

EnsemblFungiiYNL092W; YNL092W; YNL092W.
GeneIDi855632.
KEGGisce:YNL092W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X85811 Genomic DNA. Translation: CAA59825.1.
DQ115393 Genomic DNA. Translation: AAZ22516.1.
Z71368 Genomic DNA. Translation: CAA95968.1.
BK006947 Genomic DNA. Translation: DAA10454.1.
PIRiS52733.
RefSeqiNP_014307.1. NM_001182930.1.

3D structure databases

ProteinModelPortaliP53934.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35732. 18 interactions.
DIPiDIP-1880N.
IntActiP53934. 10 interactions.
MINTiMINT-391242.

Proteomic databases

PaxDbiP53934.
PRIDEiP53934.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL092W; YNL092W; YNL092W.
GeneIDi855632.
KEGGisce:YNL092W.

Organism-specific databases

CYGDiYNL092w.
EuPathDBiFungiDB:YNL092W.
SGDiS000005036. YNL092W.

Phylogenomic databases

eggNOGiNOG323736.
GeneTreeiENSGT00390000005323.
HOGENOMiHOG000204444.
InParanoidiP53934.
OrthoDBiEOG7ZKSMD.

Enzyme and pathway databases

BioCyciYEAST:G3O-33120-MONOMER.

Miscellaneous databases

NextBioi979845.
PROiP53934.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR012901. N2227.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PfamiPF07942. N2227. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of a 14.2 kb fragment of Saccharomyces cerevisiae chromosome XIV that includes the ypt53, tRNALeu and gsr m2 genes and four new open reading frames."
    Garcia-Cantalejo J.M., Boskovic J., Jimenez A.
    Yeast 12:599-608(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "Quantitative trait loci mapped to single-nucleotide resolution in yeast."
    Deutschbauer A.M., Davis R.W.
    Nat. Genet. 37:1333-1340(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: SK1.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "UPF0586 protein C9orf41 homolog is anserine-producing methyltransferase."
    Drozak J., Piecuch M., Poleszak O., Kozlowski P., Chrobok L., Baelde H.J., de Heer E.
    J. Biol. Chem. 0:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiCARME_YEAST
AccessioniPrimary (citable) accession number: P53934
Secondary accession number(s): D6W188, Q45TZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 952 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

External Data

Dasty 3

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 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.