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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)DescriptionActionsGraphical viewLength
Active sitei451Proton acceptor; via carboxylateBy similarity1

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)DescriptionActionsGraphical viewLength
Mutagenesisi447G → D: Causes temperature-dependent reduction in catalytic activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3548.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000642361 – 451Glycylpeptide N-tetradecanoyltransferaseAdd BLAST451

Proteomic databases

PRIDEiP30418.

Interactioni

Subunit structurei

Monomer.1 Publication

Chemistry databases

BindingDBiP30418.

Structurei

Secondary structure

1451
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi69 – 71Combined sources3
Beta strandi82 – 87Combined sources6
Helixi93 – 106Combined sources14
Beta strandi113 – 117Combined sources5
Helixi121 – 128Combined sources8
Helixi135 – 137Combined sources3
Beta strandi138 – 143Combined sources6
Turni144 – 146Combined sources3
Beta strandi149 – 162Combined sources14
Turni163 – 166Combined sources4
Beta strandi167 – 179Combined sources13
Helixi181 – 183Combined sources3
Beta strandi185 – 187Combined sources3
Helixi189 – 201Combined sources13
Turni202 – 204Combined sources3
Beta strandi208 – 212Combined sources5
Beta strandi220 – 231Combined sources12
Helixi232 – 237Combined sources6
Helixi249 – 256Combined sources8
Beta strandi267 – 269Combined sources3
Helixi272 – 274Combined sources3
Helixi275 – 286Combined sources12
Beta strandi289 – 294Combined sources6
Helixi297 – 305Combined sources9
Beta strandi309 – 311Combined sources3
Beta strandi314 – 322Combined sources9
Beta strandi328 – 336Combined sources9
Beta strandi339 – 343Combined sources5
Beta strandi348 – 350Combined sources3
Beta strandi352 – 360Combined sources9
Turni361 – 364Combined sources4
Helixi368 – 383Combined sources16
Helixi384 – 386Combined sources3
Beta strandi389 – 395Combined sources7
Helixi399 – 401Combined sources3
Turni402 – 407Combined sources6
Beta strandi409 – 420Combined sources12
Turni433 – 435Combined sources3
Beta strandi445 – 447Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP30418.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 45Myristoyl CoA-binding4
Regioni174 – 210Myristoyl CoA-bindingAdd BLAST37

Sequence similaritiesi

Belongs to the NMT family.Curated

Phylogenomic databases

InParanoidiP30418.
KOiK00671.
OrthoDBiEOG092C3LZ4.

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)DescriptionActionsGraphical viewLength
Sequence conflicti327I → V in EAL04131 (PubMed:15123810).Curated1
Sequence conflicti327I → V in EAL03976 (PubMed:15123810).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IYKX-ray2.30A/B60-451[»]
1IYLX-ray3.20A/B/C/D60-451[»]
1NMTX-ray2.45A/B/C60-451[»]
ProteinModelPortaliP30418.
SMRiP30418.
ModBaseiSearch...
MobiDBiSearch...

Chemistry databases

BindingDBiP30418.
ChEMBLiCHEMBL3548.

Proteomic databases

PRIDEiP30418.

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.
OrthoDBiEOG092C3LZ4.

Enzyme and pathway databases

BRENDAi2.3.1.97. 1096.

Miscellaneous databases

EvolutionaryTraceiP30418.
PROiP30418.

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...

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: November 2, 2016
This is version 107 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.