Reviewed, UniProtKB/Swiss-Prot P30418 (NMT_CANAL)

Names and origin

Protein names

Recommended name:
    Glycylpeptide N-tetradecanoyltransferase
    EC=2.3.1.97
Alternative name(s):
    Peptide N-myristoyltransferase
    Myristoyl-CoA:protein N-myristoyltransferase
      Short name=NMT

Gene names

Name:	NMT1
ORF Names:	CaO19.4641, CaO19.12111

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	451 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. 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. Ref.1 Ref.3 Ref.4
Catalytic activity	Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
Enzyme regulation	Competitively inhibited by SC-58272, a peptidomimetic derived from the N-terminal sequence of a natural substrate.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
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.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	N-terminal protein myristoylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycylpeptide N-tetradecanoyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 451

451

Glycylpeptide N-tetradecanoyltransferase

PRO_0000064236

Regions

Region

42 – 45

4

Myristoyl CoA-binding

Region

174 – 210

37

Myristoyl CoA-binding

Sites

Active site

451

1

Proton acceptor; via carboxylate By similarity

Experimental info

Mutagenesis

447

1

G → D: Causes temperature-dependent reduction in catalytic activity. Ref.3

Sequence conflict

327

1

I → V in EAL04131. Ref.2

Sequence conflict

327

1

I → V in EAL03976. Ref.2

Secondary structure

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451

Helix Strand Turn

Details...

Helix

69 – 71

3

Beta strand

82 – 87

6

Helix

93 – 106

14

Beta strand

113 – 117

5

Helix

121 – 128

8

Helix

135 – 137

3

Beta strand

138 – 143

6

Turn

144 – 146

3

Beta strand

149 – 162

14

Turn

163 – 166

4

Beta strand

167 – 179

13

Helix

181 – 183

3

Helix

189 – 201

13

Turn

202 – 204

3

Beta strand

208 – 212

5

Beta strand

220 – 231

12

Helix

232 – 237

6

Helix

249 – 256

8

Beta strand

267 – 269

3

Helix

272 – 274

3

Helix

275 – 286

12

Beta strand

289 – 294

6

Helix

297 – 305

9

Beta strand

309 – 311

3

Beta strand

314 – 322

9

Beta strand

328 – 336

9

Beta strand

339 – 343

5

Beta strand

348 – 350

3

Beta strand

352 – 360

9

Turn

361 – 364

4

Helix

368 – 383

16

Helix

384 – 386

3

Beta strand

389 – 395

7

Helix

399 – 401

3

Turn

402 – 407

6

Beta strand

409 – 420

12

Turn

433 – 435

3

Beta strand

445 – 447

3

Sequences

	Sequence		Length	Mass (Da)
	P30418-1 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 7D107CBC05458D2D	FASTA	451	51,877
	10 20 30 40 50 60 MSGDNTGNKS NSAPSKSIEE LLKLLAMGQE LSPAQQKEMK DYKFWKTQPV PSLSETVTEE 70 80 90 100 110 120 GPIDKLKTPE DVPNDPLPLI SDFEWSTLDI DDNLQLDELY KLLYDNYVED IDATFRFKYS 130 140 150 160 170 180 HEFFQWALKP PGWRKDWHVG VRVKSTGKLV AFIAATPVTF KLNKSNKVID SVEINFLCIH 190 200 210 220 230 240 KKLRNKRLAP VLIKEITRRV NKQNIWQALY TGGSILPTPL TTCRYQHRPI NWSKLHDVGF 250 260 270 280 290 300 SHLPPNQTKS SMVASYTLPN NPKLKGLRPM TGKDVSTVLS LLYKYQERFD IVQLFTEEEF 310 320 330 340 350 360 KHWMLGHDEN SDSNVVKSYV VEDENGIITD YFSYYLLPFT VLDNAQHDEL GIAYLFYYAS 370 380 390 400 410 420 DSFEKPNYKK RLNELITDAL ITSKKFGVDV FNCLTCQDNT YFLKDCKFGS GDGFLNYYLF 430 440 450 NYRTFPMDGG IDKKTKEVVE DQTSGIGVVL L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1569105] [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]	"The diploid genome sequence of Candida albicans." Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S. Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SC5314.
[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: 8300631] [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: 9115247] [Abstract] Cited for: FUNCTION, SUBSTRATE SPECIFICITY.
[5]	"Crystal structure of the anti-fungal target N-myristoyl transferase." Weston S.A., Camble R., Colls J., Rosenbrock G., Taylor I., Egerton M., Tucker A.D., Tunnicliffe A., Mistry A., Mancia F., de la Fortelle E., Irwin J., Bricogne G., Pauptit R.A. Nat. Struct. Biol. 5:213-221(1998) [PubMed: 9501915] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS).
[6]	"Crystal structures of Candida albicans N-myristoyltransferase with two distinct inhibitors." Sogabe S., Masubuchi M., Sakata K., Fukami T.A., Morikami K., Shiratori Y., Ebiike H., Kawasaki K., Aoki Y., Shimma N., D'Arcy A., Winkler F.K., Banner D.W., Ohtsuka T. Chem. Biol. 9:1119-1128(2002) [PubMed: 12401496] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 60-451 IN COMPLEX WITH MYRISTOYL-COA AND INHIBITORS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M80544 Genomic DNA. Translation: AAA34351.1.
AACQ01000005 Genomic DNA. Translation: EAL04131.1.
AACQ01000006 Genomic DNA. Translation: EAL03976.1.

PIR

A38099.

RefSeq

XP_722713.1.
XP_722859.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IYK	X-ray	2.30	A/B	60-451	[»]
1IYL	X-ray	3.20	A/B/C/D	60-451	[»]
1NMT	X-ray	2.45	A/B/C	60-451	[»]

ModBase

Search...

Genome annotation databases

GeneID

3635457.
3635624.

KEGG

cal:CaO19.12111.
cal:CaO19.4641.

Phylogenomic databases

OrthoDB

EOG95DZ5M.

Enzyme and pathway databases

BRENDA

2.3.1.97. 1124.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000903. Myristoyl_trans.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 2 hits.

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.

PROSITE

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

ProtoNet

Search...

Entry information

Entry name

NMT_CANAL

Accession

Primary (citable) accession number: P30418
Secondary accession number(s): Q5AMK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 24, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)