Glycylpeptide N-tetradecanoyltransferase - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P14743 (NMT_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Glycylpeptide N-tetradecanoyltransferase
EC=2.3.1.97

Alternative name(s):
Cell division control protein 72
Myristoyl-CoA:protein N-myristoyltransferase
Short name=NMT
Peptide N-myristoyltransferase

Gene names

Name:	NMT1
Synonyms:	CDC72
Ordered Locus Names:	YLR195C
ORF Names:	L8167.14

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	455 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Uncharged amino acids are preferred at position 2 while neutral residues are favored at positions 3 and 4. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6.
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
Enzyme regulation	Inhibited by diethylpyrocarbonate. Competitively inhibited by S-(2-oxo)pentadecyl-CoA, a non hydrolysable myristoyl-CoA analog, and by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.
Subunit structure	Monomer.
Subcellular location	Cytoplasm Ref.11.
Post-translational modification	The N-terminus is blocked.
Miscellaneous	Has an ordered Bi-Bi kinetic mechanism, with myristoyl-CoA binding taking place prior to peptide binding and CoA release occurring before acylated peptide release. Cooperative interactions between the acyl-CoA and peptide binding sites of NMT contribute to its extraordinary chain-length specificity.
Sequence similarities	Belongs to the NMT family.
Biophysicochemical properties	Kinetic parameters: K_M=1.4 µM for myristoyl-CoA Ref.4 Ref.10 pH dependence: Optimum pH is 7.5-8.0.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	N-terminal peptidyl-glycine N-myristoylation Traceable author statement. Source: SGD replicative cell aging Inferred from mutant phenotype. Source: SGD
Cellular component	cytosol Inferred from direct assay. Source: SGD
Molecular function	glycylpeptide N-tetradecanoyltransferase activity Inferred from mutant phenotype. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 455

455

Glycylpeptide N-tetradecanoyltransferase

PRO_0000064248

Regions

Region

38 – 41

Myristoyl CoA-binding

Region

168 – 204

Myristoyl CoA-binding

Sites

Active site

455

Proton acceptor; via carboxylate

Experimental info

Mutagenesis

L → P in NMT1-72; temperature-sensitive mutant with myristic acid auxotrophy. Ref.7

Mutagenesis

169

N → L: Reduces the chemical transformation rate; when associated with A-205. Ref.10

Mutagenesis

170

F → A: Reduces the chemical transformation rate; when associated with A-171. Ref.10

Mutagenesis

171

L → A: Reduces the chemical transformation rate; when associated with A-170. Ref.10

Mutagenesis

202

A → T: Reduces affinity for both substrate and myristoyl-CoA. Ref.9

Mutagenesis

205

T → A: Reduces the chemical transformation rate; when associated with L-169. Ref.10

Mutagenesis

217

C → R: Reduces affinity for substrate, but not for myristoyl-CoA. Ref.9

Mutagenesis

328

S → P: Moderately reduces affinity for myristoyl-CoA, but not for substrate. Ref.9

Mutagenesis

404

N → Y: Moderately reduces affinity for substrate, but not for myristoyl-CoA. Ref.9

Mutagenesis

426

N → I: Reduces affinity for myristoyl-CoA, but not for substrate. Ref.9

Mutagenesis

451

G → D in NMT1-181; temperature-sensitive with myristic acid auxotrophy. Reduces affinity for myristoyl-CoA. Ref.6

Mutagenesis

454 – 455

Missing: Reduces chemical transformation rate 400-fold.

Secondary structure

455

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P14743 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 0424CA3978F76AE6
Show »

FASTA

455

52,838

        10         20         30         40         50         60 
MSEEDKAKKL ENLLKLLQLN NDDTSKFTQE QKKAMKDHKF WRTQPVKDFD EKVVEEGPID 

        70         80         90        100        110        120 
KPKTPEDISD KPLPLLSSFE WCSIDVDNKK QLEDVFVLLN ENYVEDRDAG FRFNYTKEFF 

       130        140        150        160        170        180 
NWALKSPGWK KDWHIGVRVK ETQKLVAFIS AIPVTLGVRG KQVPSVEINF LCVHKQLRSK 

       190        200        210        220        230        240 
RLTPVLIKEI TRRVNKCDIW HALYTAGIVL PAPVSTCRYT HRPLNWKKLY EVDFTGLPDG 

       250        260        270        280        290        300 
HTEEDMIAEN ALPAKTKTAG LRKLKKEDID QVFELFKRYQ SRFELIQIFT KEEFEHNFIG 

       310        320        330        340        350        360 
EESLPLDKQV IFSYVVEQPD GKITDFFSFY SLPFTILNNT KYKDLGIGYL YYYATDADFQ 

       370        380        390        400        410        420 
FKDRFDPKAT KALKTRLCEL IYDACILAKN ANMDVFNALT SQDNTLFLDD LKFGPGDGFL 

       430        440        450 
NFYLFNYRAK PITGGLNPDN SNDIKRRSNV GVVML

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Disruption of the yeast N-myristoyl transferase gene causes recessive lethality." Duronio R.J., Towler D.A., Heuckeroth R.O., Gordon J.I. Science 243:796-800(1989) [PubMed: 2644694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 9-15; 132-138; 198-211; 292-301; 323-337 AND 413-428. Strain: ATCC 204511 / S288c / AB972.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Purification and characterization of yeast myristoyl CoA:protein N-myristoyltransferase." Towler D.A., Adams S.P., Eubanks S.R., Towery D.S., Jackson-Machelski E., Glaser L., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 84:2708-2712(1987) [PubMed: 3106975] [Abstract] Cited for: CHARACTERIZATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[5]	Erratum Towler D.A., Adams S.P., Eubanks S.R., Towery D.S., Jackson-Machelski E., Glaser L., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 84:7523-7523(1987)
[6]	"Myristic acid auxotrophy caused by mutation of S. cerevisiae myristoyl-CoA:protein N-myristoyltransferase." Duronio R.J., Rudnick D.A., Johnson R.L., Johnson D.R., Gordon J.I. J. Cell Biol. 113:1313-1330(1991) [PubMed: 2045414] [Abstract] Cited for: MUTAGENESIS OF GLY-451.
[7]	"Genetic and biochemical studies of a mutant Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase, nmt72pLeu99-->Pro, that produces temperature-sensitive myristic acid auxotrophy." Johnson D.R., Duronio R.J., Langner C.A., Rudnick D.A., Gordon J.I. J. Biol. Chem. 268:483-494(1993) [PubMed: 8416952] [Abstract] Cited for: MUTAGENESIS OF LEU-99.
[8]	"Use of photoactivatable peptide substrates of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase (Nmt1p) to characterize a myristoyl-CoA-Nmt1p-peptide ternary complex and to provide evidence for an ordered reaction mechanism." Rudnick D.A., Rocque W.J., McWherter C.A., Toth M.V., Jackson-Machelski E., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 90:1087-1091(1993) [PubMed: 8430078] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Biochemical studies of Saccharomyces cerevisiae myristoyl-coenzyme A:protein N-myristoyltransferase mutants." Zhang L., Jackson-Machelski E., Gordon J.I. J. Biol. Chem. 271:33131-33140(1996) [PubMed: 8955162] [Abstract] Cited for: MUTAGENESIS OF ALA-202; CYS-217; SER-328; ASN-404 AND ASN-426.
[10]	"Pre-steady-state kinetic studies of Saccharomyces cerevisiae myristoylCoA:protein N-myristoyltransferase mutants identify residues involved in catalysis." Farazi T.A., Manchester J.K., Waksman G., Gordon J.I. Biochemistry 40:9177-9186(2001) [PubMed: 11478885] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-169; PHE-170; LEU-171; THR-205 AND 454-MET-LEU-455.
[11]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[12]	"Structure of N-myristoyltransferase with bound myristoyl-CoA and peptide substrate analogs." Bhatnagar R.S., Fuetterer K., Farazi T.A., Korolev S., Murray C.L., Jackson-Machelski E., Gokel G.W., Gordon J.I., Waksman G. Nat. Struct. Biol. 5:1091-1097(1998) [PubMed: 9846880] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 34-455 IN COMPLEX WITH MYRISTOYL-COA AND INHIBITOR.
[13]	"Structures of Saccharomyces cerevisiae N-myristoyltransferase with bound myristoylCoA and peptide provide insights about substrate recognition and catalysis." Farazi T.A., Waksman G., Gordon J.I. Biochemistry 40:6335-6343(2001) [PubMed: 11371195] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 34-455 IN COMPLEX WITH MYRISTOYL-COA AND SUBSTRATE.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M23726 Genomic DNA. Translation: AAA34815.1.
U14913 Genomic DNA. Translation: AAB67436.1.
BK006945 Genomic DNA. Translation: DAA09514.1.

PIR

A40163.

RefSeq

NP_013296.1. NM_001182082.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IIC	X-ray	2.20	A/B	34-455	[»]
1IID	X-ray	2.50	A	34-455	[»]
2NMT	X-ray	2.90	A	34-455	[»]
2P6E	X-ray	2.90	A/B/C/D/E/F	1-455	[»]
2P6F	X-ray	3.10	A/B/C/D/E/F	1-455	[»]
2P6G	X-ray	3.00	A/B/C/D/E/F	1-455	[»]

ProteinModelPortal

P14743.

SMR

P14743. Positions 4-455.

ModBase

Search...

Protein-protein interaction databases

STRING

P14743.

Proteomic databases

PeptideAtlas

P14743.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YLR195C; YLR195C; YLR195C.

GeneID

850892.

KEGG

sce:YLR195C.

NMPDR

fig|4932.3.peg.4306.

Organism-specific databases

CYGD

YLR195c.

SGD

S000004185. NMT1.

Phylogenomic databases

eggNOG

fuNOG07746.

GeneTree

EFGT00050000004932.

HOGENOM

HBG314670.

OMA

STCRYFH.

OrthoDB

EOG4V9XZZ.

Enzyme and pathway databases

BRENDA

2.3.1.97. 984.

Gene expression databases

ArrayExpress

P14743.

Genevestigator

P14743.

GermOnline

YLR195C. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.

K00671.

PANTHER

PTHR11377. Myristoyl_trans. 1 hit.

Pfam

PF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]

PIRSF

PIRSF015892. N-myristl_transf. 1 hit.

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 2 hits.

PROSITE

PS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

967266.

Entry information

Entry name

NMT_YEAST

Accession

Primary (citable) accession number: P14743
Secondary accession number(s): D6VYJ8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents