| General information | | DisProt: | DP00338 | | Name: | Histo-blood group B transferase | | Synonym(s): | B0B1U2_HUMAN
ABO glycosyltransferase
B-specific alpha 1-3-galactosyltransferase
Glycoprotein-fucosylgalactoside alpha-galactosyltransferase
EC=2.4.1.37
Fucosylglycoprotein 3-alpha-galactosyltransferase
Transferase B
GTB
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | B0B1U2 | | UniGene: | Hs.654423 | | SwissProt: | B0B1U2_HUMAN | | TrEMBL: | | | NCBI (GI): | 4590454 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 354 | | Percent disordered: | 7% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MAEVLRTLAG KPKCHALRPM ILFLIMLVLV LFGYGVLSPR SLMPGSLERG FCMAVREPDH - 60
LQRVSLPRMV YPQPKVLTPC RKDVLVVTPW LAPIVWEGTF NIDILNEQFR LQNTTIGLTV - 120
FAIKKYVAFL KLFLETAEKH FMVGHRVHYY VFTDQPAAVP RVTLGTGRQL SVLEVGAYKR - 180
WQDVSMRRME MISDFCERRF LSEVDYLVCV DVDMEFRDHV GVEILTPLFG TLHPSFYGSS - 240
REAFTYERRP QSQAYIPKDE GDFYYMGAFF GGSVQEVQRL TRACHQAMMV DQANGIEAVW - 300
HDESHLNKYL LRHKPTKVLS PEYLWDQQLL GWPAVLRKLR FTAVPKNHQA VRNP
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| 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.
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| 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.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 179 - 194 | | Length: | 16 | | Region sequence: |
KRWQDVSMRRMEMISD | | Modification type: | Fragment
Monomeric
Native
| | PDB: | 1LZ7:A | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Unknown
| | Functional subclasses: | Autoregulatory
| Detection methods:
- 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:
- 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
- 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 GTB catalytic domain (residues 63 - 354) was used for the crystallization studies.
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. A M186V mutant of GTB showed that altering residues within the disordered loop can affect the activity of the enzyme.
Unlike glycosyltransferases found in other organisms, the disordered loop does not become ordered upon substrate binding.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 345 - 354 | | Length: | 10 | | Region sequence: |
PKNHQAVRNP | | Modification type: | Fragment
Monomeric
Native
| | PDB: | 1LZ7:A | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- 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:
- 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
- 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:
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| References |
- Letts JA, Persson M, Schuman B, Borisova SN, Palcic MM, Evans SV. "The effect of heavy atoms on the conformation of the active-site polypeptide loop in human ABO(H) blood-group glycosyltransferase B." Acta Crystallogr D Biol Crystallogr. 2007; 63(Pt 8): 860-5. PubMed: 17642512
- 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
- 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
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| Comments |
This protein is also connected to UniProt ID P16442 (DP00339). This entry lists GTA and GTB, but the sequence is specific to GTA. However, under natural variants, the residues that are different for GTB are listed. GTA and GTB differ by four amino acids (aa 176, 235, 266, and 268).
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