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HAMAP rule MF_01166

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General rule information [?]

Accession MF_01166
Dates 11-NOV-2005 (Created)
18-JUL-2023 (Last updated, Version 33)
Name ArnA
Scope(s) Bacteria
Template(s) P77398 (ARNA_ECOLI); O52325 (ARNA_SALTY); [ Recover all ]
Triggered by HAMAP; MF_01166 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier ARNA
Protein name RecName: Full=Bifunctional polymyxin resistance protein ArnA;
RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase;
AltName: Full=ArnAFT;
AltName: Full=UDP-L-Ara4N formyltransferase;
RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating;
AltName: Full=ArnADH;
AltName: Full=UDP-GlcUA decarboxylase;
AltName: Full=UDP-glucuronic acid dehydrogenase;
Gene name Name=arnA;

Comments [?]

FUNCTIONBifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto- arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4- amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido- arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
CATALYTIC ACTIVITY Reaction=NAD(+) + UDP-alpha-D-glucuronate = CO2 + NADH + UDP-beta-L- threo-pentopyranos-4-ulose; Xref=Rhea:RHEA:24702, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58052, ChEBI:CHEBI:58710; EC=;
CATALYTIC ACTIVITY Reaction=(6R)-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; Xref=Rhea:RHEA:24706, ChEBI:CHEBI:15378, ChEBI:CHEBI:57453, ChEBI:CHEBI:58708, ChEBI:CHEBI:58709, ChEBI:CHEBI:195366; EC=;
PATHWAYNucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L- arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 1/3.
PATHWAYNucleotide-sugar biosynthesis; UDP-4-deoxy-4-formamido-beta-L- arabinose biosynthesis; UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate: step 3/3.
PATHWAYBacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.
SUBUNITHomohexamer, formed by a dimer of trimers.
SIMILARITYIn the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily.
SIMILARITYIn the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.

Keywords [?]

Gene Ontology [?]

GO:0016616; Molecular function:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016742; Molecular function:hydroxymethyl-, formyl- and related transferase activity
GO:0046493; Biological process:lipid A metabolic process

Cross-references [?]

Pfam PF02911; Formyl_trans_C; 1;
Pfam PF00551; Formyl_trans_N; 1;
Pfam PF01370; Epimerase; 1;

Features [?]

From: ARNA_ECOLI (P77398)
Key From To Description Tag Condition FTGroup
BINDING 368 369 /ligand="NAD(+)"
REGION Nter 304 /note="Formyltransferase ArnAFT"
BINDING 86 88 /ligand="(6R)-10-formyltetrahydrofolate"
BINDING 136 140 /ligand="(6R)-10-formyltetrahydrofolate"
REGION 314 Cter /note="Dehydrogenase ArnADH"
BINDING 432 433 /ligand="UDP-alpha-D-glucuronate"
BINDING 526 535 /ligand="UDP-alpha-D-glucuronate"
ACT_SITE 104 104 /note="Proton donor; for formyltransferase activity" H
ACT_SITE 434 434 /note="Proton acceptor; for decarboxylase activity" E
ACT_SITE 619 619 /note="Proton donor; for decarboxylase activity" R
BINDING 114 114 /ligand="(6R)-10-formyltetrahydrofolate"
BINDING 347 347 /ligand="NAD(+)"
BINDING 393 393 /ligand="UDP-alpha-D-glucuronate"
BINDING 398 398 /ligand="UDP-alpha-D-glucuronate"
BINDING 460 460 /ligand="UDP-alpha-D-glucuronate"
BINDING 492 492 /ligand="UDP-alpha-D-glucuronate"
BINDING 613 613 /ligand="UDP-alpha-D-glucuronate"
SITE 102 102 /note="Transition state stabilizer" N
SITE 140 140 /note="Raises pKa of active site His" D

Additional information [?]

Size range 654-687 amino acids
Related rules MF_00182
Fusion Nter: None Cter: None

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