NMT_USTMA
ID NMT_USTMA Reviewed; 706 AA.
AC Q4PB56; A0A0D1E0A8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Glycylpeptide N-tetradecanoyltransferase;
DE EC=2.3.1.97;
DE AltName: Full=Myristoyl-CoA:protein N-myristoyltransferase;
DE Short=NMT;
DE AltName: Full=Peptide N-myristoyltransferase;
GN Name=NMT1; ORFNames=UMAG_02657;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of
CC certain cellular proteins. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) +
CC N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-
CC COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723,
CC ChEBI:CHEBI:133050; EC=2.3.1.97;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NMT family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM003145; KIS69316.1; -; Genomic_DNA.
DR RefSeq; XP_011389045.1; XM_011390743.1.
DR AlphaFoldDB; Q4PB56; -.
DR SMR; Q4PB56; -.
DR STRING; 5270.UM02657P0; -.
DR EnsemblFungi; KIS69316; KIS69316; UMAG_02657.
DR GeneID; 23563355; -.
DR KEGG; uma:UMAG_02657; -.
DR VEuPathDB; FungiDB:UMAG_02657; -.
DR eggNOG; KOG2779; Eukaryota.
DR HOGENOM; CLU_022882_2_0_1; -.
DR InParanoid; Q4PB56; -.
DR OMA; IPHELRV; -.
DR OrthoDB; 1025421at2759; -.
DR Proteomes; UP000000561; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004379; F:glycylpeptide N-tetradecanoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018008; P:N-terminal peptidyl-glycine N-myristoylation; IBA:GO_Central.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000903; NMT.
DR InterPro; IPR022677; NMT_C.
DR InterPro; IPR022678; NMT_CS.
DR InterPro; IPR022676; NMT_N.
DR PANTHER; PTHR11377; PTHR11377; 1.
DR Pfam; PF01233; NMT; 1.
DR Pfam; PF02799; NMT_C; 1.
DR SUPFAM; SSF55729; SSF55729; 2.
DR PROSITE; PS00975; NMT_1; 1.
DR PROSITE; PS00976; NMT_2; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..706
FT /note="Glycylpeptide N-tetradecanoyltransferase"
FT /id="PRO_0000064245"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 706
FT /note="Proton acceptor; via carboxylate"
FT /evidence="ECO:0000250"
FT BINDING 180..183
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 317..319
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
FT BINDING 325..329
FT /ligand="tetradecanoyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57385"
FT /evidence="ECO:0000250|UniProtKB:P14743"
SQ SEQUENCE 706 AA; 77562 MW; C2E3B38B6650D6F7 CRC64;
MSGIAGTSQD TSVAASASSS STRPAAASSS IAPPSPSLTT APVKEQEQDD DDDQENDDEE
EEEEGTAAIT GADGLTAKQR KKKKSKAAAK LRKKLGLGGS PTDASEGKLL ASGSSREGKI
SDEVVSQVQR AVQAEHGSVA ANAVTKANLA KVMAMMNLER DAMLKSQDSK QKAQKAIADH
KFWKTQPVMK PTDAPVVKSD QEGSIEASVP PEQVRQEPYP LPADFEWVMI DVDNEGELKE
VYDLLSANYV EDDDATFRFD YSPEFLHWVL KHPGYQKTWH IGVRVASTKK LVAFISGIPH
ELRVREKSYQ STEINFLCVH KKLRSKRLAP VLIKEVTRQC HLTGVFHAIY TVGSVLPTPV
SCSRYYHRTI NAKKLAEIGF SAIPHNMSME AHVKRFELPA KTNLPGLREM ERRDVAQVGK
LMRRYMRRFD MAPRFSDHEV EHILLSGRGE ACQGGRGRKG QVTWTYVVEN SEGRITDMFA
FYSLPSSILD SDKHQSLNAA YLFYYATDVV FQGDCDCDSD SSGVCDAETG RASTSQPSSE
RAVALAAGKA AWQCNSLTNL TSCELADEAR VAAWDSEPAH IKTALKTRLN LLINTLLIIA
RDHDFDVVNC VTVMDNALFL QQQKFGPGDG FLRFYLFNWR TKPVAGGMGA RPGEAELDPV
QAYARSMAKR AAHTDDDDVK RLAEQLIRNA AINPAEVGSG NGIVMV
