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Q96EK6 (GNA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucosamine 6-phosphate N-acetyltransferase
EC=2.3.1.4
Alternative name(s):
Phosphoglucosamine acetylase
Phosphoglucosamine transacetylase
Gene names
Name:GNPNAT1
Synonyms:GNA1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length184 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 1/2.

Subunit structure

Homodimer. Ref.4

Subcellular location

Golgi apparatus membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein By similarity.

Sequence similarities

Belongs to the acetyltransferase family. GNA1 subfamily.

Contains 1 N-acetyltransferase domain.

Biophysicochemical properties

Kinetic parameters:

KM=26 µM for acetyl-coenzyme A Ref.5

KM=97 µM for glucosamine-6-phosphate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 184184Glucosamine 6-phosphate N-acetyltransferase
PRO_0000074553

Regions

Domain39 – 184146N-acetyltransferase
Region108 – 1114Substrate binding
Region120 – 1223Substrate binding
Region130 – 1356Acetyl-CoA binding
Region151 – 1522Substrate binding
Region165 – 1673Acetyl-CoA binding

Sites

Binding site611Substrate
Binding site1751Substrate
Binding site1811Substrate

Experimental info

Mutagenesis1561E → A: Reduces affinity for glucosamine-6-phosphate 6-fold. Ref.4
Mutagenesis1561E → D: Slightly reduced catalytic activity. Ref.4

Secondary structure

1 .................................... 184
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96EK6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: E9F31803CF633BBF

FASTA18420,749
        10         20         30         40         50         60 
MKPDETPMFD PSLLKEVDWS QNTATFSPAI SPTHPGEGLV LRPLCTADLN RGFFKVLGQL 

        70         80         90        100        110        120 
TETGVVSPEQ FMKSFEHMKK SGDYYVTVVE DVTLGQIVAT ATLIIEHKFI HSCAKRGRVE 

       130        140        150        160        170        180 
DVVVSDECRG KQLGKLLLST LTLLSKKLNC YKITLECLPQ NVGFYKKFGY TVSEENYMCR 


RFLK

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[3]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[4]"Acceptor substrate binding revealed by crystal structure of human glucosamine-6-phosphate N-acetyltransferase 1."
Wang J., Liu X., Liang Y.-H., Li L.-F., Su X.-D.
FEBS Lett. 582:2973-2978(2008) [PubMed: 18675810] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH GLUCOSAMINE-6-PHOSPHATE, MUTAGENESIS OF GLU-156, SUBUNIT.
[5]"Structural and kinetic differences between human and Aspergillus fumigatus D-glucosamine-6-phosphate N-acetyltransferase."
Hurtado-Guerrero R., Raimi O.G., Min J., Zeng H., Vallius L., Shepherd S., Ibrahim A.F.M., Wu H., Plotnikov A.N., van Aalten D.M.F.
Biochem. J. 415:217-223(2008) [PubMed: 18601654] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH COENZYME A AND N-ACETYLGLUCOSAMINE-6-PHOSPHATE, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK090577 mRNA. Translation: BAC03482.1.
BC012179 mRNA. Translation: AAH12179.1.
IPIIPI00061525.
RefSeqNP_932332.1. NM_198066.3.
UniGeneHs.702056.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HUZX-ray2.67A/B1-184[»]
2O28X-ray1.80A/B1-184[»]
3CXPX-ray2.01A1-184[»]
3CXQX-ray2.30A1-184[»]
3CXSX-ray2.70A1-184[»]
ProteinModelPortalQ96EK6.
SMRQ96EK6. Positions 3-184.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96EK6. 2 interactions.
MINTMINT-2813920.
STRINGQ96EK6.

PTM databases

PhosphoSiteQ96EK6.

Polymorphism databases

DMDM47116568.

Proteomic databases

PeptideAtlasQ96EK6.
PRIDEQ96EK6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216410; ENSP00000216410; ENSG00000100522.
GeneID64841.
KEGGhsa:64841.
UCSCuc001xab.1. human.

Organism-specific databases

CTD64841.
GeneCardsGC14M053241.
H-InvDBHIX0202048.
HGNCHGNC:19980. GNPNAT1.
HPAHPA044647.
neXtProtNX_Q96EK6.
PharmGKBPA134901326.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06793.
GeneTreeENSGT00390000008666.
HOGENOMHBG736206.
HOVERGENHBG048986.
InParanoidQ96EK6.
OMAGCYKMSL.
OrthoDBEOG4PNXJ3.
PhylomeDBQ96EK6.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ96EK6.
BgeeQ96EK6.
CleanExHS_GNPNAT1.
GenevestigatorQ96EK6.
GermOnlineENSG00000100522. Homo sapiens.

Family and domain databases

InterProIPR000182. AcTrfase_GCN5-related_dom.
IPR016181. Acyl_CoA_acyltransferase.
[Graphical view]
Gene3DG3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
KOK00621.
PfamPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITEPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio66946.

Entry information

Entry nameGNA1_HUMAN
AccessionPrimary (citable) accession number: Q96EK6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 1, 2001
Last modified: January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents