Annotation for this protein is in progress - please check future releases for more complete information


DP00363: UDP-N-acetylhexosamine pyrophosphorylase [Isoform AGX2]FASTA viewXML view

General information
DisProt:DP00363
Name:UDP-N-acetylhexosamine pyrophosphorylase [Isoform AGX2]
Synonym(s):UAP1_HUMAN
Antigen X
AGX
Sperm-associated antigen 2
UDP-N-acetylglucosamine pyrophosphorylase [Isoform AGX2]
AGX-2
UDP-N-acetylglucosamine diphosphorylase
N-acetylglucosamine-1-phosphate uridyltransferase
EC 2.7.7.23
First appeared in release:Release 3.0 (02/17/2006)
UniProt:Q16222-1
UniGene:Hs.492859
SwissProt: UAP1_HUMAN
TrEMBL:  
NCBI (GI): 68846235
Source organism:Homo sapiens (Human)
Sequence length:522
Percent disordered:3%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MNINDLKLTL SKAGQEHLLR FWNELEEAQQ VELYAELQAM NFEELNFFFQ KAIEGFNQSS - 60
HQKNVDARME PVPREVLGSA TRDQDQLQAW ESEGLFQISQ NKVAVLLLAG GQGTRLGVAY - 120
PKGMYDVGLP SRKTLFQIQA ERILKLQQVA EKYYGNKCII PWYIMTSGRT MESTKEFFTK - 180
HKYFGLKKEN VIFFQQGMLP AMSFDGKIIL EEKNKVSMAP DGNGGLYRAL AAQNIVEDME - 240
QRGIWSIHVY CVDNILVKVA DPRFIGFCIQ KGADCGAKVV EKTNPTEPVG VVCRVDGVYQ - 300
VVEYSEISLA TAQKRSSDGR LLFNAGNIAN HFFTVPFLRD VVNVYEPQLQ HHVAQKKIPY - 360
VDTQGQLIKP DKPNGIKMEK FVFDIFQFAK KFVVYEVLRE DEFSPLKNAD SQNGKDNPTT - 420
ARHALMSLHH CWVLNAGGHF IDENGSRLPA IPRSATNGKS ETITADVNHN LKDANDVPIQ - 480
CEISPLISYA GEGLESYVAD KEFHAPLIID ENGVHELVKN GI



Functional narrative    

Converts UDP and GlcNAc-1-P into UDP-GlcNAc, and UDP and GalNAc-1-P into UDP-GalNAc. Isoform AGX1 has 2 to 3 times higher activity towards GalNAc-1-P, while isoform AGX2 has 8 times more activity towards GlcNAc-1-P.

Region 1: 454-470

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:I Loop
Location:454 - 470
Length:17
Region sequence:

SATNGKSETITADVNHN

Modification type: Isoform
Monomeric
Native
PDB: 1JVD:A, 1JVD:B, 1JVG:A, 1JVG:B
Structural/functional type: Relationship to function unknown
Functional classes:  
Functional subclasses: Protein-protein binding
Detection methods:
  1. X-ray crystallography (293 K; pH: 5.7; imidazole/malate 0.2 M; PEG600 34 %)
References:
  1. Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y. "Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture." Embo J. 2001; 20(22): 6191-202. PubMed: 11707391
Comments:
 



Comments


Insertion of the I loop disrupts the ability of the protein to dimerize in solution. Dimerization leads to an occluded active site, thus in isoform AGX2 the active site remains open to the environment.


Previous entry DP00363 has been split into canonical isoform (DP00363) and the alternatively-spliced isoform 2 DP00363_A002. Disorder is characterized on the alternatively-spliced product.


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