(data stored in SCRATCH zone)

SWISSPROT: Q4WCU5_ASPFU

ID   Q4WCU5_ASPFU            Unreviewed;       190 AA.
AC   Q4WCU5;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=Glucosamine 6-phosphate N-acetyltransferase {ECO:0000256|RuleBase:RU365086};
DE            EC=2.3.1.4 {ECO:0000256|RuleBase:RU365086};
GN   ORFNames=AFUA_6G02460 {ECO:0000313|EMBL:EAL85793.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL85793.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL85793.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
RN   [2] {ECO:0000213|PDB:2VEZ}
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH GLUCOSE-6-PHOSPHATE.
RX   PubMed=18005663; DOI=10.1016/j.febslet.2007.10.065;
RA   Hurtado-Guerrero R., Raimi O., Shepherd S., van Aalten D.M.;
RT   "Glucose-6-phosphate as a probe for the glucosamine-6-phosphate N-
RT   acetyltransferase Michaelis complex.";
RL   FEBS Lett. 581:5597-5600(2007).
RN   [3] {ECO:0000213|PDB:2VXK}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COENZYME A.
RX   PubMed=18601654; DOI=10.1042/BJ20081000;
RA   Hurtado-Guerrero R., Raimi O.G., Min J., Zeng H., Vallius L., Shepherd S.,
RA   Ibrahim A.F., Wu H., Plotnikov A.N., van Aalten D.M.;
RT   "Structural and kinetic differences between human and Aspergillus fumigatus
RT   D-glucosamine-6-phosphate N-acetyltransferase.";
RL   Biochem. J. 415:217-223(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + D-glucosamine 6-phosphate = CoA + H(+) + N-
CC         acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:10292,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC         ChEBI:CHEBI:57513, ChEBI:CHEBI:58725; EC=2.3.1.4;
CC         Evidence={ECO:0000256|RuleBase:RU365086};
CC   -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC       glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from
CC       alpha-D-glucosamine 6-phosphate (route I): step 1/2.
CC       {ECO:0000256|RuleBase:RU365086}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GNA1 subfamily.
CC       {ECO:0000256|RuleBase:RU365086}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EAL85793.1}.
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; AAHF01000012; EAL85793.1; -; Genomic_DNA.
DR   RefSeq; XP_747831.1; XM_742738.1.
DR   PDB; 2VEZ; X-ray; 1.45 A; A=1-190.
DR   PDB; 2VXK; X-ray; 1.80 A; A=1-190.
DR   PDBsum; 2VEZ; -.
DR   PDBsum; 2VXK; -.
DR   SMR; Q4WCU5; -.
DR   STRING; 746128.CADAFUBP00009317; -.
DR   EnsemblFungi; EAL85793; EAL85793; AFUA_6G02460.
DR   GeneID; 3505194; -.
DR   KEGG; afm:AFUA_6G02460; -.
DR   EuPathDB; FungiDB:Afu6g02460; -.
DR   HOGENOM; HOG000106325; -.
DR   InParanoid; Q4WCU5; -.
DR   KO; K00621; -.
DR   OMA; FYIKCGF; -.
DR   OrthoDB; 1479446at2759; -.
DR   SABIO-RK; Q4WCU5; -.
DR   UniPathway; UPA00113; UER00529.
DR   EvolutionaryTrace; Q4WCU5; -.
DR   Proteomes; UP000002530; Chromosome 6.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0004343; F:glucosamine 6-phosphate N-acetyltransferase activity; IDA:AspGD.
DR   GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR   GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR039143; GNPNAT1.
DR   PANTHER; PTHR13355; PTHR13355; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q4WCU5.
DR   SWISS-2DPAGE; Q4WCU5.
KW   3D-structure {ECO:0000213|PDB:2VEZ, ECO:0000213|PDB:2VXK};
KW   Acyltransferase {ECO:0000256|RuleBase:RU365086,
KW   ECO:0000313|EMBL:EAL85793.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW   Transferase {ECO:0000256|RuleBase:RU365086, ECO:0000313|EMBL:EAL85793.1}.
FT   DOMAIN          48..190
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   REGION          117..120
FT                   /note="Glucose-6-phosphate binding"
FT                   /evidence="ECO:0000213|PDB:2VEZ"
FT   REGION          129..130
FT                   /note="Glucose-6-phosphate binding"
FT                   /evidence="ECO:0000213|PDB:2VEZ"
FT   REGION          139..144
FT                   /note="Coenzyme A binding"
FT                   /evidence="ECO:0000213|PDB:2VXK"
FT   REGION          160..161
FT                   /note="Glucose-6-phosphate binding"
FT                   /evidence="ECO:0000213|PDB:2VEZ"
FT   BINDING         70
FT                   /note="Glucose-6-phosphate"
FT                   /evidence="ECO:0000213|PDB:2VEZ"
FT   BINDING         133
FT                   /note="Coenzyme A; via amide nitrogen"
FT                   /evidence="ECO:0000213|PDB:2VXK"
FT   BINDING         165
FT                   /note="Glucose-6-phosphate; via carbonyl oxygen"
FT                   /evidence="ECO:0000213|PDB:2VEZ"
FT   BINDING         170
FT                   /note="Coenzyme A"
FT                   /evidence="ECO:0000213|PDB:2VXK"
FT   BINDING         176
FT                   /note="Coenzyme A"
FT                   /evidence="ECO:0000213|PDB:2VXK"
FT   BINDING         189
FT                   /note="Glucose-6-phosphate"
FT                   /evidence="ECO:0000213|PDB:2VEZ"
SQ   SEQUENCE   190 AA;  21102 MW;  F72C0FFCDD0E40A3 CRC64;
     MTNATIAPTT TAAPVTKSVD APTADENTPL FSPSLISPDV LAVLPADYTI RPLCRSDYKR
     GYLDVLRVLT TVGDINEEQW NSRYEWIRAR SDEYYLLVVC DGEGRIVGTG SLVVERKFIH
     SLGMVGHIED IAVEKGQQGK KLGLRIIQAL DYVAEKVGCY KTILDCSEAN EGFYIKCGFK
     RAGLEMAHYY
//

If you have problems or comments...

PBIL Back to PBIL home page