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Protein

Glycylpeptide N-tetradecanoyltransferase

Gene

NMT1

Organism
Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Ser is present at position 5 in almost all known N-myristoyl proteins and Lys is commonly encountered at postion 6. Basic residues are preferred at positions 7 and 8.3 Publications

Catalytic activityi

Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.

Enzyme regulationi

Competitively inhibited by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei451 – 4511Proton acceptor; via carboxylateBy similarity

GO - Molecular functioni

  • drug binding Source: CGD
  • glycylpeptide N-tetradecanoyltransferase activity Source: CGD

GO - Biological processi

  • N-terminal peptidyl-glycine N-myristoylation Source: CGD
  • pathogenesis Source: CGD
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.97. 1096.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycylpeptide N-tetradecanoyltransferase (EC:2.3.1.97)
Alternative name(s):
Myristoyl-CoA:protein N-myristoyltransferase
Short name:
NMT
Peptide N-myristoyltransferase
Gene namesi
Name:NMT1
ORF Names:CaO19.12111, CaO19.4641
OrganismiCandida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Taxonomic identifieri237561 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeCandida/Lodderomyces cladeCandida
Proteomesi
  • UP000000559 Componenti: Unassembled WGS sequence

Organism-specific databases

CGDiCAL0000201559. NMT1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi447 – 4471G → D: Causes temperature-dependent reduction in catalytic activity. 1 Publication

Chemistry

ChEMBLiCHEMBL3548.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 451451Glycylpeptide N-tetradecanoyltransferasePRO_0000064236Add
BLAST

Interactioni

Subunit structurei

Monomer.1 Publication

Chemistry

BindingDBiP30418.

Structurei

Secondary structure

1
451
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi69 – 713Combined sources
Beta strandi82 – 876Combined sources
Helixi93 – 10614Combined sources
Beta strandi113 – 1175Combined sources
Helixi121 – 1288Combined sources
Helixi135 – 1373Combined sources
Beta strandi138 – 1436Combined sources
Turni144 – 1463Combined sources
Beta strandi149 – 16214Combined sources
Turni163 – 1664Combined sources
Beta strandi167 – 17913Combined sources
Helixi181 – 1833Combined sources
Beta strandi185 – 1873Combined sources
Helixi189 – 20113Combined sources
Turni202 – 2043Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi220 – 23112Combined sources
Helixi232 – 2376Combined sources
Helixi249 – 2568Combined sources
Beta strandi267 – 2693Combined sources
Helixi272 – 2743Combined sources
Helixi275 – 28612Combined sources
Beta strandi289 – 2946Combined sources
Helixi297 – 3059Combined sources
Beta strandi309 – 3113Combined sources
Beta strandi314 – 3229Combined sources
Beta strandi328 – 3369Combined sources
Beta strandi339 – 3435Combined sources
Beta strandi348 – 3503Combined sources
Beta strandi352 – 3609Combined sources
Turni361 – 3644Combined sources
Helixi368 – 38316Combined sources
Helixi384 – 3863Combined sources
Beta strandi389 – 3957Combined sources
Helixi399 – 4013Combined sources
Turni402 – 4076Combined sources
Beta strandi409 – 42012Combined sources
Turni433 – 4353Combined sources
Beta strandi445 – 4473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYKX-ray2.30A/B60-451[»]
1IYLX-ray3.20A/B/C/D60-451[»]
1NMTX-ray2.45A/B/C60-451[»]
ProteinModelPortaliP30418.
SMRiP30418. Positions 60-451.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30418.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 454Myristoyl CoA-binding
Regioni174 – 21037Myristoyl CoA-bindingAdd
BLAST

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

InParanoidiP30418.
KOiK00671.
OrthoDBiEOG78SQSW.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 1 hit.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30418-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGDNTGNKS NSAPSKSIEE LLKLLAMGQE LSPAQQKEMK DYKFWKTQPV
60 70 80 90 100
PSLSETVTEE GPIDKLKTPE DVPNDPLPLI SDFEWSTLDI DDNLQLDELY
110 120 130 140 150
KLLYDNYVED IDATFRFKYS HEFFQWALKP PGWRKDWHVG VRVKSTGKLV
160 170 180 190 200
AFIAATPVTF KLNKSNKVID SVEINFLCIH KKLRNKRLAP VLIKEITRRV
210 220 230 240 250
NKQNIWQALY TGGSILPTPL TTCRYQHRPI NWSKLHDVGF SHLPPNQTKS
260 270 280 290 300
SMVASYTLPN NPKLKGLRPM TGKDVSTVLS LLYKYQERFD IVQLFTEEEF
310 320 330 340 350
KHWMLGHDEN SDSNVVKSYV VEDENGIITD YFSYYLLPFT VLDNAQHDEL
360 370 380 390 400
GIAYLFYYAS DSFEKPNYKK RLNELITDAL ITSKKFGVDV FNCLTCQDNT
410 420 430 440 450
YFLKDCKFGS GDGFLNYYLF NYRTFPMDGG IDKKTKEVVE DQTSGIGVVL

L
Length:451
Mass (Da):51,877
Last modified:April 1, 1993 - v1
Checksum:i7D107CBC05458D2D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti327 – 3271I → V in EAL04131 (PubMed:15123810).Curated
Sequence conflicti327 – 3271I → V in EAL03976 (PubMed:15123810).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80544 Genomic DNA. Translation: AAA34351.1.
AACQ01000005 Genomic DNA. Translation: EAL04131.1.
AACQ01000006 Genomic DNA. Translation: EAL03976.1.
PIRiA38099.
RefSeqiXP_722713.1. XM_717620.1.
XP_722859.1. XM_717766.1.

Genome annotation databases

EnsemblFungiiEAL03976; EAL03976; CaO19.4641.
EAL04131; EAL04131; CaO19.12111.
GeneIDi3635457.
3635624.
KEGGical:CaO19.12111.
cal:CaO19.4641.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80544 Genomic DNA. Translation: AAA34351.1.
AACQ01000005 Genomic DNA. Translation: EAL04131.1.
AACQ01000006 Genomic DNA. Translation: EAL03976.1.
PIRiA38099.
RefSeqiXP_722713.1. XM_717620.1.
XP_722859.1. XM_717766.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IYKX-ray2.30A/B60-451[»]
1IYLX-ray3.20A/B/C/D60-451[»]
1NMTX-ray2.45A/B/C60-451[»]
ProteinModelPortaliP30418.
SMRiP30418. Positions 60-451.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

BindingDBiP30418.
ChEMBLiCHEMBL3548.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiEAL03976; EAL03976; CaO19.4641.
EAL04131; EAL04131; CaO19.12111.
GeneIDi3635457.
3635624.
KEGGical:CaO19.12111.
cal:CaO19.4641.

Organism-specific databases

CGDiCAL0000201559. NMT1.

Phylogenomic databases

InParanoidiP30418.
KOiK00671.
OrthoDBiEOG78SQSW.

Enzyme and pathway databases

BRENDAi2.3.1.97. 1096.

Miscellaneous databases

EvolutionaryTraceiP30418.

Family and domain databases

Gene3Di3.40.630.30. 2 hits.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000903. MyristoylCoA_TrFase.
IPR022677. MyristoylCoA_TrFase_C.
IPR022678. MyristoylCoA_TrFase_CS.
IPR022676. MyristoylCoA_TrFase_N.
[Graphical view]
PANTHERiPTHR11377. PTHR11377. 1 hit.
PfamiPF01233. NMT. 1 hit.
PF02799. NMT_C. 1 hit.
[Graphical view]
PIRSFiPIRSF015892. N-myristl_transf. 1 hit.
SUPFAMiSSF55729. SSF55729. 2 hits.
PROSITEiPS00975. NMT_1. 1 hit.
PS00976. NMT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Candida albicans myristoyl-CoA:protein N-myristoyltransferase gene. Isolation and expression in Saccharomyces cerevisiae and Escherichia coli."
    Wiegand R.C., Carr C., Minnerly J.C., Pauley A.M., Carron C.P., Langner C.A., Duronio R.J., Gordon J.I.
    J. Biol. Chem. 267:8591-8598(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 121-132; 291-300; 341-359 AND 408-423, FUNCTION.
    Strain: ATCC 32354 / B311.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: SC5314 / ATCC MYA-2876.
  3. "Comparison of myristoyl-CoA:protein N-myristoyltransferases from three pathogenic fungi: Cryptococcus neoformans, Histoplasma capsulatum, and Candida albicans."
    Lodge J.K., Johnson R.L., Weinberg R.A., Gordon J.I.
    J. Biol. Chem. 269:2996-3009(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLY-447.
  4. "Scanning alanine mutagenesis and de-peptidization of a Candida albicans myristoyl-CoA:protein N-myristoyltransferase octapeptide substrate reveals three elements critical for molecular recognition."
    McWherter C.A., Rocque W.J., Zupec M.E., Freeman S.K., Brown D.L., Devadas B., Getman D.P., Sikorski J.A., Gordon J.I.
    J. Biol. Chem. 272:11874-11880(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
  5. Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 60-451 IN COMPLEX WITH MYRISTOYL-COA AND INHIBITORS.

Entry informationi

Entry nameiNMT_CANAL
AccessioniPrimary (citable) accession number: P30418
Secondary accession number(s): Q5AMK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: January 20, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Candida albicans
    Candida albicans: entries and gene names
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.