EC number:2.1.2.13

Enzyme

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     2. Transferases
        2.1 Transferring one-carbon groups
            2.1.2 Hydroxymethyl-, formyl- and related transferases
ID:2.1.2.13
Description:UDP-4-amino-4-deoxy-L-arabinose formyltransferase.
Alternative Name: UDP-L-Ara4N formyltransferase.
ArnAFT.
Cath: 3.40.50.720; 3.90.25.10; 3.40.50.12230; 3.40.50.170; 3.10.25.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.1.2.13
BRENDA Enzyme Link: BRENDA 2.1.2.13
KEGG Enzyme Link: KEGG2.1.2.13
BioCyc Enzyme Link: BioCyc 2.1.2.13
ExPASy Enzyme Link: ExPASy2.1.2.13
EC2PDB Enzyme Link: EC2PDB 2.1.2.13
ExplorEnz Enzyme Link: ExplorEnz 2.1.2.13
PRIAM enzyme-specific profiles Link: PRIAM 2.1.2.13
IntEnz Enzyme Link: IntEnz 2.1.2.13
MEDLINE Enzyme Link: MEDLINE 2.1.2.13

EC number:2.1.2.13

MSA:

2.1.2.13;
Phylogenetic Tree:

2.1.2.13;
Uniprot:
M-CSA:
RHEA:24706 (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H(+) + UDP-4-deoxy-4-formamido-beta-L-arabinose
RULE(radius=1) [*:1]-[NH2;+0:2].[*:3]=[CH;+0:4]-[N;H0;+0:5](-[*:6])-[*:7]>>[*:6]-[NH;+0:5]-[*:7].[*:1]-[NH;+0:2]-[CH;+0:4]=[*:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structure and function of both domains of ArnA, a dual function decarboxylase and a formyltransferase, involved in 4-amino-4-deoxy-L-arabinose biosynthesis.Williams GJ, Breazeale SD, Raetz CR, Naismith JH2005 Jun 1715809294
A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose.Breazeale SD, Ribeiro AA, McClerren AL, Raetz CR2005 Apr 815695810