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


DP00339: Histo-blood group A transferaseFASTA viewXML view

General information
DisProt:DP00339
Name:Histo-blood group A transferase
Synonym(s):BGAT_HUMAN
NAGAT
Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase
EC=2.4.1.40
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase
Transferase A
GTA
Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase soluble form [cleavage product 1]
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P16442
UniGene:Hs.654423
SwissProt: BGAT_HUMAN
TrEMBL:  
NCBI (GI): 114949
Source organism:Homo sapiens (Human)
Sequence length:354
Percent disordered:7%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG FCMAVREPDH - 60
LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF NIDILNEQFR LQNTTIGLTV - 120
FAIKKYVAFL KLFLETAEKH FMVGHRVHYY VFTDQPAAVP RVTLGTGRQL SVLEVRAYKR - 180
WQDVSMRRME MISDFCERRF LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPGFYGSS - 240
REAFTYERRP QSQAYIPKDE GDFYYLGGFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW - 300
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA VRNP



Functional narrative    

This protein is the basis of the ABO blood group system. The histo-blood group ABO involves three carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity that converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals lack such activity.

Region 1: 179-194 Region 2: 345-354

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: 
Location:179 - 194
Length:16
Region sequence:

KRWQDVSMRRMEMISD

Modification type: Fragment
Monomeric
Native
PDB: 1LZ0:A
Structural/functional type: Function arises from the disordered state
Functional classes: Unknown
Functional subclasses: Autoregulatory
Detection methods:
  1. X-ray crystallography (291 K; pH: 7.5; 3-chloro-Hg-2-methoxy-propylurea (0.3 - 0.5 mM); ADA (pH 7.5, 70 mM); Glycerol (5%); Maganese chloride (5 - 8 mM); MPD (2.5%); PEG 4000 (2%); Sodium acetate (pH 4.6, 50 mM); Sodium chloride (40 mM))
References:
  1. Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV. "The structural basis for specificity in human ABO(H) blood group biosynthesis." Nat Struct Biol. 2002; 9(9): 685-90. PubMed: 12198488

  2. Yazer MH, Denomme GA, Rose NL, Palcic MM. "Amino-acid substitution in the disordered loop of blood group B-glycosyltransferase enzyme causes weak B phenotype." Transfusion. 2005; 45(7): 1178-82. PubMed: 15987364
Comments:
The GTA catalytic domain (residues 63 - 354) was used for the crystallization studies, which is the soluble form of the protein.

It is thought that the disordered loop may play a role in regulating the catalytic activity of the enzyme, however, it is not clear if the regulation occurs during substrate binding or product release.

Unlike glycosyltransferases found in other organisms, the disordered loop does not become ordered upon substrate binding.


Region 2
Type:Disordered
Name: 
Location:345 - 354
Length:10
Region sequence:

PKNHQAVRNP

Modification type: Fragment
Monomeric
Native
PDB: 1LZ0:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (291 K; pH: 7.5; 3-chloro-Hg-2-methoxy-propylurea (0.3 - 0.5 mM); ADA (pH 7.5, 70 mM); Glycerol (5%); Maganese chloride (5 - 8 mM); MPD (2.5%); PEG 4000 (2%); Sodium acetate (pH 4.6, 50 mM); Sodium chloride (40 mM))
References:
  1. Patenaude SI, Seto NO, Borisova SN, Szpacenko A, Marcus SL, Palcic MM, Evans SV. "The structural basis for specificity in human ABO(H) blood group biosynthesis." Nat Struct Biol. 2002; 9(9): 685-90. PubMed: 12198488

  2. Yazer MH, Denomme GA, Rose NL, Palcic MM. "Amino-acid substitution in the disordered loop of blood group B-glycosyltransferase enzyme causes weak B phenotype." Transfusion. 2005; 45(7): 1178-82. PubMed: 15987364
Comments:
 



References

  1. Yamamoto F, Clausen H, White T, Marken J, Hakomori S. "Molecular genetic basis of the histo-blood group ABO system." Nature. 1990; 345(6272): 229-33. PubMed: 2333095

  2. Yamamoto F, Hakomori S. "Sugar-nucleotide donor specificity of histo-blood group A and B transferases is based on amino acid substitutions." J Biol Chem. 1990; 265(31): 19257-62. PubMed: 2121736



Comments


A separate entry may be required for cleavage product 1.


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