ID   CARME_YEAST             Reviewed;         400 AA.
AC   P53934; D6W188; Q45TZ4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Carnosine N-methyltransferase {ECO:0000303|PubMed:26001783};
DE            EC=2.1.1.22 {ECO:0000269|PubMed:26001783};
GN   OrderedLocusNames=YNL092W; ORFNames=N2227;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8771715;
RX   DOI=10.1002/(sici)1097-0061(199605)12:6<599::aid-yea938>3.0.co;2-9;
RA   Garcia-Cantalejo J.M., Boskovic J., Jimenez A.;
RT   "Sequence analysis of a 14.2 kb fragment of Saccharomyces cerevisiae
RT   chromosome XIV that includes the ypt53, tRNALeu and gsr m2 genes and four
RT   new open reading frames.";
RL   Yeast 12:599-608(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SK1;
RX   PubMed=16273108; DOI=10.1038/ng1674;
RA   Deutschbauer A.M., Davis R.W.;
RT   "Quantitative trait loci mapped to single-nucleotide resolution in yeast.";
RL   Nat. Genet. 37:1333-1340(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=26001783; DOI=10.1074/jbc.m115.640037;
RA   Drozak J., Piecuch M., Poleszak O., Kozlowski P., Chrobok L., Baelde H.J.,
RA   de Heer E.;
RT   "UPF0586 protein C9orf41 homolog is anserine-producing methyltransferase.";
RL   J. Biol. Chem. 290:17190-17205(2015).
CC   -!- FUNCTION: N-methyltransferase that mediates the formation of anserine
CC       (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Also methylates
CC       other L-histidine-containing di- and tripeptides such as Gly-Gly-His,
CC       Gly-His and homocarnosine (GABA-His). {ECO:0000269|PubMed:26001783}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carnosine + S-adenosyl-L-methionine = anserine + H(+) + S-
CC         adenosyl-L-homocysteine; Xref=Rhea:RHEA:14205, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57485, ChEBI:CHEBI:57856, ChEBI:CHEBI:58445,
CC         ChEBI:CHEBI:59789; EC=2.1.1.22;
CC         Evidence={ECO:0000269|PubMed:26001783};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=21.5 mM for carnosine {ECO:0000269|PubMed:26001783};
CC         KM=0.002 mM for S-adenosyl-L-methionine
CC         {ECO:0000269|PubMed:26001783};
CC         Vmax=7.89 nmol/min/mg enzyme with carnosine as substrate
CC         {ECO:0000269|PubMed:26001783};
CC         Note=kcat is 0.38 min(-1) for carnosine. kcat is 0.74 min(-1) for
CC         S-adenosyl-L-methionine. {ECO:0000269|PubMed:26001783};
CC       pH dependence:
CC         Optimum pH is 7.0-7.5. {ECO:0000269|PubMed:26001783};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:26001783};
CC   -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the carnosine N-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; X85811; CAA59825.1; -; Genomic_DNA.
DR   EMBL; DQ115393; AAZ22516.1; -; Genomic_DNA.
DR   EMBL; Z71368; CAA95968.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10454.1; -; Genomic_DNA.
DR   PIR; S52733; S52733.
DR   RefSeq; NP_014307.1; NM_001182930.1.
DR   PDB; 5X62; X-ray; 2.20 A; A/B=1-400.
DR   PDBsum; 5X62; -.
DR   AlphaFoldDB; P53934; -.
DR   SMR; P53934; -.
DR   BioGRID; 35732; 42.
DR   DIP; DIP-1880N; -.
DR   IntAct; P53934; 3.
DR   MINT; P53934; -.
DR   STRING; 4932.YNL092W; -.
DR   PaxDb; 4932-YNL092W; -.
DR   PeptideAtlas; P53934; -.
DR   EnsemblFungi; YNL092W_mRNA; YNL092W; YNL092W.
DR   GeneID; 855632; -.
DR   KEGG; sce:YNL092W; -.
DR   AGR; SGD:S000005036; -.
DR   SGD; S000005036; YNL092W.
DR   VEuPathDB; FungiDB:YNL092W; -.
DR   eggNOG; KOG2798; Eukaryota.
DR   GeneTree; ENSGT00390000005323; -.
DR   HOGENOM; CLU_030612_1_2_1; -.
DR   InParanoid; P53934; -.
DR   OMA; KQFAREW; -.
DR   OrthoDB; 167229at2759; -.
DR   BioCyc; YEAST:G3O-33120-MONOMER; -.
DR   BRENDA; 2.1.1.22; 984.
DR   Reactome; R-SCE-70921; Histidine catabolism.
DR   SABIO-RK; P53934; -.
DR   BioGRID-ORCS; 855632; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P53934; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53934; Protein.
DR   GO; GO:0030735; F:carnosine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:SGD.
DR   GO; GO:0035498; P:carnosine metabolic process; IDA:UniProtKB.
DR   GO; GO:0006479; P:protein methylation; IDA:SGD.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR012901; CARME.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR12303:SF6; CARNOSINE N-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR12303; UNCHARACTERIZED; 1.
DR   Pfam; PF07942; CARME; 1.
DR   SMART; SM01296; N2227; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Methyltransferase; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..400
FT                   /note="Carnosine N-methyltransferase"
FT                   /id="PRO_0000203441"
FT   BINDING         108
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         111
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         146
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         167
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         235
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         278
FT                   /ligand="carnosine"
FT                   /ligand_id="ChEBI:CHEBI:57485"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         286
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         309
FT                   /ligand="carnosine"
FT                   /ligand_id="ChEBI:CHEBI:57485"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   BINDING         385
FT                   /ligand="carnosine"
FT                   /ligand_id="ChEBI:CHEBI:57485"
FT                   /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT   VARIANT         42
FT                   /note="A -> E (in strain: SK1)"
FT   VARIANT         154
FT                   /note="V -> M (in strain: SK1)"
FT   VARIANT         317
FT                   /note="E -> D (in strain: SK1)"
FT   HELIX           9..23
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           25..33
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           35..43
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           55..81
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           96..113
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           118..135
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           151..158
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           170..181
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   TURN            193..196
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           204..208
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          211..213
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          228..233
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           235..239
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          242..244
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           255..264
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          268..275
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          279..281
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           283..293
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          294..304
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   TURN            309..312
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          316..320
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          328..331
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          333..338
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   HELIX           345..355
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          358..369
FT                   /evidence="ECO:0007829|PDB:5X62"
FT   STRAND          385..394
FT                   /evidence="ECO:0007829|PDB:5X62"
SQ   SEQUENCE   400 AA;  45497 MW;  6B6C051891F075EE CRC64;
     MDENEFDNQR ENKAVARVII SFLKYEEYAL KEIYNLRVKK WASISDRQKD MVPNYTKYLA
     NLKAAIIENG KFFRSVAEYA LQSISFEPGE IVQPNDLDMS KTCSLLTQVY REWSAEAISE
     RNCLNSRLVP FLKTLSPPKA DILIPGCGTG RLLVDLSRMG YNCEGNEFSY HMLLVSQYML
     NAGLLQNQII IYPFIHCFSH WKKIEDQLSP IKVPDIEAWS SNKGMGSMSI CAGSFVDCYG
     RNQGTKISSH YTFSRRMQLS RAKAENSKDV VVTNFFIDTG SNILDYLDTI GHVLKPGGIW
     CNFGPLLYHF ENDHGVETTY EVNPYSGFQD KINDYTPLMG LELSSDDIIS IATNHLDFEL
     IRRESGILCG YGRYAGPESC AMPGYMCHYW ILKSNPTNES
//