Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phenylethanolamine N-methyltransferase

Gene

PNMT

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Converts noradrenaline to adrenaline.

Catalytic activityi

S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine.

Pathwayi: (R)-adrenaline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-adrenaline from (R)-noradrenaline.
Proteins known to be involved in this subpathway in this organism are:
  1. Phenylethanolamine N-methyltransferase (PNMT)
This subpathway is part of the pathway (R)-adrenaline biosynthesis, which is itself part of Catecholamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-adrenaline from (R)-noradrenaline, the pathway (R)-adrenaline biosynthesis and in Catecholamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei35 – 351S-adenosyl-L-methionineBy similarity
Binding sitei40 – 401S-adenosyl-L-methionineBy similarity
Binding sitei85 – 851S-adenosyl-L-methionineBy similarity
Binding sitei101 – 1011S-adenosyl-L-methionineBy similarity
Binding sitei106 – 1061S-adenosyl-L-methionineBy similarity
Binding sitei181 – 1811S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00749; UER00736.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylethanolamine N-methyltransferase (EC:2.1.1.28)
Short name:
PNMTase
Alternative name(s):
Noradrenaline N-methyltransferase
Gene namesi
Name:PNMT
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2331.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 283283Phenylethanolamine N-methyltransferasePRO_0000159708Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei7 – 71PhosphoserineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP10938.
PRIDEiP10938.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000055240.

Chemistry

BindingDBiP10938.

Structurei

3D structure databases

ProteinModelPortaliP10938.
SMRiP10938. Positions 14-279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 802S-adenosyl-L-methionine bindingBy similarity
Regioni158 – 1592S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IJGY. Eukaryota.
ENOG4111F9R. LUCA.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiP10938.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10938-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGTDRSQAA GAVPDSDPGL AAVSSAYQRF EPRAYLRNNY APPRGDLSCP
60 70 80 90 100
DGVGPWKLRC LAQTFATGEV SGRTLIDIGS GPTIYQLLSA CAHFEDITMT
110 120 130 140 150
DFLEVNRQEL RLWLREEPGA FDWSVYSQHV CLIEGKGESW QEKECQLRAR
160 170 180 190 200
VKRILPIDVH RPQPLGAGGL APLPADALVS AFCLEAVSPD LASFQRALDH
210 220 230 240 250
ITTLLRPGGH LLLIGALEES WYLAGEARLA VVPVREEEVR EALVRTATRC
260 270 280
GICARTPMPA HLQTGVDDVK GIFFTRAQKK VGV
Length:283
Mass (Da):30,918
Last modified:November 1, 1990 - v2
Checksum:iAE8B4C53E6C987E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti246 – 2483TAT → SAM in AAA30715 (PubMed:2874553).Curated
Sequence conflicti255 – 27622RTPMP…IFFTR → LHLHHACPPSDRCRRCQGHL LHL in AAA30715 (PubMed:2874553).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36706 Genomic DNA. Translation: AAA30716.1.
M14318 mRNA. Translation: AAA30715.1.
PIRiA24313.
I45962.
UniGeneiBt.451.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M36706 Genomic DNA. Translation: AAA30716.1.
M14318 mRNA. Translation: AAA30715.1.
PIRiA24313.
I45962.
UniGeneiBt.451.

3D structure databases

ProteinModelPortaliP10938.
SMRiP10938. Positions 14-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000055240.

Chemistry

BindingDBiP10938.
ChEMBLiCHEMBL2331.

Proteomic databases

PaxDbiP10938.
PRIDEiP10938.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IJGY. Eukaryota.
ENOG4111F9R. LUCA.
HOGENOMiHOG000013229.
HOVERGENiHBG000797.
InParanoidiP10938.

Enzyme and pathway databases

UniPathwayiUPA00749; UER00736.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete nucleotide and deduced amino acid sequence of bovine phenylethanolamine N-methyltransferase: partial amino acid homology with rat tyrosine hydroxylase."
    Baetge E.E., Suh Y.H., Joh T.H.
    Proc. Natl. Acad. Sci. U.S.A. 83:5454-5458(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The complete nucleotide sequence and structure of the gene encoding bovine phenylethanolamine N-methyltransferase."
    Batter D.K., D'Mello S.R., Turzai L.M., Hughes H.B. III, Gioio A.E., Kaplan B.B.
    J. Neurosci. Res. 19:367-376(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Purification and partial amino acid sequence of bovine adrenal phenylethanolamine N-methyltransferase: a comparison of nucleic acid and protein sequence data."
    Weisberg E.P., Batter D.K., Brown W.E., Kaplan B.B.
    J. Neurosci. Res. 19:377-382(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  4. "Primary structure of bovine adrenal phenylethanolamine N-methyltransferase."
    Wong D.L., Yoo Y.S., Lau K., Schilling J.W.
    Neuropsychopharmacology 3:175-180(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiPNMT_BOVIN
AccessioniPrimary (citable) accession number: P10938
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1990
Last modified: July 6, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.