CARME_DICDI
ID CARME_DICDI Reviewed; 463 AA.
AC Q54ST2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Carnosine N-methyltransferase {ECO:0000250|UniProtKB:Q5BJZ6};
DE EC=2.1.1.22 {ECO:0000250|UniProtKB:Q5BJZ6};
GN ORFNames=DDB_G0282239;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: N-methyltransferase that mediates the formation of anserine
CC (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine.
CC {ECO:0000250|UniProtKB:Q8N4J0}.
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:0000250|UniProtKB:Q8N4J0};
CC -!- SIMILARITY: Belongs to the carnosine N-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AAFI02000046; EAL66325.1; -; Genomic_DNA.
DR RefSeq; XP_640303.1; XM_635211.1.
DR AlphaFoldDB; Q54ST2; -.
DR SMR; Q54ST2; -.
DR STRING; 44689.DDB0237849; -.
DR PaxDb; Q54ST2; -.
DR EnsemblProtists; EAL66325; EAL66325; DDB_G0282239.
DR GeneID; 8623479; -.
DR KEGG; ddi:DDB_G0282239; -.
DR dictyBase; DDB_G0282239; -.
DR eggNOG; KOG2798; Eukaryota.
DR HOGENOM; CLU_030612_0_0_1; -.
DR InParanoid; Q54ST2; -.
DR OMA; VREWSSE; -.
DR PhylomeDB; Q54ST2; -.
DR Reactome; R-DDI-70921; Histidine catabolism.
DR PRO; PR:Q54ST2; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0030735; F:carnosine N-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0035498; P:carnosine metabolic process; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..463
FT /note="Carnosine N-methyltransferase"
FT /id="PRO_0000337253"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 218
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 260
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 281
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 351
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 352
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 367
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 371
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 379
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 402
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
FT BINDING 450
FT /ligand="carnosine"
FT /ligand_id="ChEBI:CHEBI:57485"
FT /evidence="ECO:0000250|UniProtKB:Q8N4J0"
SQ SEQUENCE 463 AA; 54029 MW; 09F6F3317929AE72 CRC64;
MTKNKSKNKS NNSNISNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNKNGE
SQLKNKNKNI SENQHIYDKH NHDHSHDHNH DYDDNNEDDE EKEELEHYQL IVSTLLNYSQ
YSLHWVKDMQ DFFHYKLSED EKKLLPNYNA KMEALARAVL VNSQFLKKIG NEHCNIFSQS
SDNSANSERI VDPTNLDHIK IDYFMMDQLK STIRQLVREW SEEGKLERDQ AFEPIKQQLL
EIYGHIPFQE RSKIRVYSPG AGLGRLCLEI ASLGFSSQGI EYSFMMLIVS NFMLNKVEKI
NEFKIHPYIH QTVNVLRDID QLRTVTIPDV LSSELLPKNN PALEFSMSAG DFTKNIEENS
FDCICTCFFI DTAPNILEYV DCISKILKPG GTWINFGPLL YHHAKKKDSI ELSYEQLRYL
ICKKQFQFKK EEIRDAEYCS NQKSLLRSIY KCQFFVVINN KPT
