CARME_YEAST
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 03-AUG-2022, entry version 153.
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=21.50 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 S-
CC 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; 38.
DR DIP; DIP-1880N; -.
DR IntAct; P53934; 3.
DR MINT; P53934; -.
DR STRING; 4932.YNL092W; -.
DR PaxDb; P53934; -.
DR PRIDE; P53934; -.
DR EnsemblFungi; YNL092W_mRNA; YNL092W; YNL092W.
DR GeneID; 855632; -.
DR KEGG; sce:YNL092W; -.
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; VREWSSE; -.
DR BioCyc; YEAST:G3O-33120-MON; -.
DR BRENDA; 2.1.1.22; 984.
DR Reactome; R-SCE-70921; Histidine catabolism.
DR SABIO-RK; P53934; -.
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; -; 1.
DR InterPro; IPR012901; CARME.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR12303; PTHR12303; 1.
DR Pfam; PF07942; N2227; 1.
DR SMART; SM01296; N2227; 1.
DR SUPFAM; SSF53335; SSF53335; 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
