HNMTL_CHICK
ID HNMTL_CHICK Reviewed; 322 AA.
AC U3NEE3;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Carnosine N-methyltransferase 2 {ECO:0000305};
DE EC=2.1.1.22 {ECO:0000269|PubMed:23705015};
DE AltName: Full=Histamine N-methyltransferase-like {ECO:0000303|PubMed:23705015};
DE Short=HNMT-like {ECO:0000303|PubMed:23705015};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC TISSUE=Pectoralis muscle {ECO:0000312|EMBL:AGW32084.1};
RX PubMed=23705015; DOI=10.1371/journal.pone.0064805;
RA Drozak J., Chrobok L., Poleszak O., Jagielski A.K., Derlacz R.;
RT "Molecular identification of carnosine N-methyltransferase as chicken
RT histamine N-methyltransferase-like protein (hnmt-like).";
RL PLoS ONE 8:E64805-E64805(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: N-methyltransferase that mediates the formation of anserine
CC (beta-alanyl-N(Pi)-methyl-L-histidine) from carnosine. Anserine, a
CC methylated derivative of carnosine (beta-alanyl-L-histidine), is an
CC abundant constituent of vertebrate skeletal muscles.
CC {ECO:0000269|PubMed:23705015}.
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:23705015};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.628 mM for carnosine {ECO:0000269|PubMed:23705015};
CC KM=0.014 mM for S-adenosyl-L-methionine
CC {ECO:0000269|PubMed:23705015};
CC Vmax=51.87 nmol/min/mg enzyme with carnosine as substrate
CC {ECO:0000269|PubMed:23705015};
CC Vmax=786 nmol/min/mg enzyme with S-adenosyl-L-methionine as substrate
CC {ECO:0000269|PubMed:23705015};
CC Note=kcat is 0.034 sec(-1) for carnosine. kcat is 0.519 sec(-1) for
CC S-adenosyl-L-methionine. {ECO:0000269|PubMed:23705015};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23705015}.
CC -!- MISCELLANEOUS: Two different proteins belonging to two different
CC protein families are able to mediate carnosine N-methyltransferase
CC activity in chicken. This protein, which is not conserved in mammals,
CC and another protein (AC F1N9S8), which is conserved from human to
CC yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. HNMT family. {ECO:0000255|PROSITE-ProRule:PRU00929}.
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DR EMBL; KF271750; AGW32084.1; -; mRNA.
DR EMBL; AADN03005426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001305361.1; NM_001318432.1.
DR RefSeq; XP_001234740.1; XM_001234739.3.
DR AlphaFoldDB; U3NEE3; -.
DR SMR; U3NEE3; -.
DR Ensembl; ENSGALT00000062046; ENSGALP00000056487; ENSGALG00000033461.
DR GeneID; 771456; -.
DR KEGG; gga:771456; -.
DR VEuPathDB; HostDB:LOC771456; -.
DR GeneTree; ENSGT00390000002862; -.
DR OMA; HSCLDHH; -.
DR OrthoDB; 870728at2759; -.
DR BRENDA; 2.1.1.22; 1306.
DR PRO; PR:U3NEE3; -.
DR Proteomes; UP000000539; Chromosome 7.
DR Bgee; ENSGALG00000033461; Expressed in cerebellum and 4 other tissues.
DR GO; GO:0030735; F:carnosine N-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0035498; P:carnosine metabolic process; IDA:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR016673; HHMT-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PIRSF; PIRSF016616; HHMT; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51597; SAM_HNMT; 1.
PE 1: Evidence at protein level;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase.
FT CHAIN 1..322
FT /note="Carnosine N-methyltransferase 2"
FT /id="PRO_0000433614"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 119
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 150
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 172
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00929"
SQ SEQUENCE 322 AA; 36375 MW; B8D1E9F8CA46E8C7 CRC64;
MEPTPEMKRN RLPSMNFEAE ILADPHDNSE LYVIPSMRSL TAEEYVEAFQ SFLDHSTEHQ
CMDEFNKEVM PHIMAGLGNG KSTINILGVG SGTGEQDLKM IQILQAAHPG VLINNEIIEP
NPQHVAAYKE LVNRAPDLQG VSFTWHQLTS SEYEQQVKEK NTHKKFDFIH MIQMLYRVED
IPNTIKFFHS CLNHQGKLLI IILSDSSGWA SLWKKYRHCL PSTDSGHYIT SDSITAVLRK
LGIKYHVYEF PSGWDITECF IEGDPAGGHM MDFLTGTKNF LGTAPAALRS RLQEALCQPE
CSSRKDGRVI FCNNLSMIVA ES
