DB code: S00845

CATH domain 1.50.10.10 : Glycosyltransferase Catalytic domain
E.C. 5.1.3.8
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.50.10.10 : Glycosyltransferase S00531 S00048 D00167 D00500 M00192 T00245 T00246

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
A4UA16
N-acetyl-D-glucosamine 2-epimerase
PF07221 (GlcNAc_2-epim)
[Graphical View]
P17560 N-acylglucosamine 2-epimerase
EC 5.1.3.8
N-acetyl-D-glucosamine 2-epimerase
GlcNAc 2-epimerase
AGE
Renin-binding protein
RnBP
PF07221 (GlcNAc_2-epim)
[Graphical View]
NP_999065.1 (Protein)
NM_213900.1 (DNA/RNA sequence)

KEGG enzyme name
N-Acylglucosamine 2-epimerase
Acylglucosamine 2-epimerase
N-Acetylglucosamine 2-epimerase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
A4UA16 A4UA16_9NOST
P17560 RENBP_PIG N-acyl-D-glucosamine = N-acyl-D-mannosamine. Homodimer.

KEGG Pathways
Map code Pathways E.C.
MAP00530 Aminosugars metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00002 C03000 C00625
E.C.
Compound ATP N-acyl-D-glucosamine N-acyl-D-mannosamine
Type amine group,nucleotide amide group,carbohydrate amide group,carbohydrate
ChEBI 15422
PubChem 5957
2gz6A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
2gz6B00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1fp3A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound
1fp3B00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [6]&[7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
2gz6A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 57;HIS 239;GLU 242;GLU 308;HIS 372
2gz6B00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 57;HIS 239;GLU 242;GLU 308;HIS 372
1fp3A00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 60;HIS 248;GLU 251;GLU 318;HIS 382
1fp3B00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ARG 60;HIS 248;GLU 251;GLU 318;HIS 382

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
Figure 5, p.904-905
[7]
Figure 6, p.1453-1455

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Medline ID
PubMed ID 11061972
Journal J Mol Biol
Year 2000
Volume 303
Pages 733-44
Authors Itoh T, Mikami B, Maru I, Ohta Y, Hashimoto W, Murata K
Title Crystal structure of N-acyl-D-glucosamine 2-epimerase from porcine kidney at 2.0 A resolution.
Related PDB 1fp3
Related UniProtKB P17560
[2]
Resource
Comments
Medline ID
PubMed ID 11706991
Journal Cell Mol Life Sci
Year 2001
Volume 58
Pages 1650-65
Authors Allard ST, Giraud MF, Naismith JH
Title Epimerases: structure, function and mechanism.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 11726282
Journal J Biochem
Year 2001
Volume 130
Pages 815-21
Authors Takahashi S, Hori K, Takahashi K, Ogasawara H, Tomatsu M, Saito K
Title Effects of nucleotides on N-acetyl-d-glucosamine 2-epimerases (renin-binding proteins): comparative biochemical studies.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 12137277
Journal Nat Prod Rep
Year 2002
Volume 19
Pages 261-77
Authors Samuel J, Tanner ME
Title Mechanistic aspects of enzymatic carbohydrate epimerization.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 16011304
Journal Biomed Res
Year 2005
Volume 26
Pages 117-21
Authors Takahashi S, Ogasawara H, Hiwatashi K, Hata K, Hori K, Koizumi Y, Sugiyama T
Title Amino acid residues conferring the nucleotide binding properties of N-acetyl-D-glucosamine 2-epimerase (renin binding protein).
Related PDB
Related UniProtKB
[6]
Resource
Comments NUCLEOTIDE SEQUENCE.
Medline ID
PubMed ID 17292397
Journal J Mol Biol
Year 2007
Volume 367
Pages 895-908
Authors Lee YC, Wu HM, Chang YN, Wang WC, Hsu WH
Title The central cavity from the (alpha/alpha)6 barrel structure of Anabaena sp. CH1 N-acetyl-D-glucosamine 2-epimerase contains two key histidine residues for reversible conversion.
Related PDB 2gz6
Related UniProtKB A4UA16
[7]
Resource
Comments
Medline ID
PubMed ID 18328504
Journal J Mol Biol
Year 2008
Volume 377
Pages 1443-59
Authors Itoh T, Mikami B, Hashimoto W, Murata K
Title Crystal structure of YihS in complex with D-mannose: structural annotation of Escherichia coli and Salmonella enterica yihS-encoded proteins to an aldose-ketose isomerase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 19330485
Journal Biotechnol Lett
Year 2009
Volume
Pages
Authors Ito S, Hamada S, Ito H, Matsui H, Ozawa T, Taguchi H, Ito S
Title Site-directed mutagenesis of possible catalytic residues of cellobiose 2-epimerase from Ruminococcus albus.
Related PDB
Related UniProtKB

Comments
Although this enzyme binds ATP at the site, which is composed of Trp56, Arg60 and Phe122 (of PDB;1fp3), its role in catalysis has not been elucidated yet (see [7]).
This enzyme catalyzes the following reactions (see [6] & [7]):
(A) Ring opening; intramolecular elimination:
(B) Isomerization; Shift of double-bond from O=C-C to O-C=C, forming an enediol intermediate:
(C) Isomerization; Shift of double-bond from C=C-O to C-C=O:
(D) Ring closure; intramolecular addition:

Created Updated
2009-06-15 2010-03-29