HAMAP rule MF_01166
General rule information
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Accession | MF_01166 |
Dates | 11-NOV-2005 (Created)
18-JUL-2023 (Last updated, Version 33) |
Name | ArnA |
Scope(s) |
Bacteria Gammaproteobacteria |
Template(s) | P77398 (ARNA_ECOLI); O52325 (ARNA_SALTY); [ Recover all ] |
Triggered by |
HAMAP; MF_01166 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | ARNA |
Protein name | RecName: Full=Bifunctional polymyxin resistance protein ArnA; Includes: RecName: Full=UDP-4-amino-4-deoxy-L-arabinose formyltransferase; EC=2.1.2.13; AltName: Full=ArnAFT; AltName: Full=UDP-L-Ara4N formyltransferase; Includes: RecName: Full=UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating; EC=1.1.1.305; AltName: Full=ArnADH; AltName: Full=UDP-GlcUA decarboxylase; AltName: Full=UDP-glucuronic acid dehydrogenase; |
Gene name | Name=arnA; |
Comments
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FUNCTION | Bifunctional 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=1.1.1.305; |
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=2.1.2.13; |
PATHWAY | Nucleotide-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. |
PATHWAY | Nucleotide-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. |
PATHWAY | Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis. |
SUBUNIT | Homohexamer, formed by a dimer of trimers. |
SIMILARITY | In the N-terminal section; belongs to the Fmt family. UDP- L-Ara4N formyltransferase subfamily. |
SIMILARITY | In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily. |
Keywords
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Antibiotic resistance |
Lipid A biosynthesis |
Lipid biosynthesis |
Lipid metabolism |
Lipopolysaccharide biosynthesis |
Multifunctional enzyme |
NAD |
Oxidoreductase |
Transferase |
Gene Ontology
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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
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Features
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From: ARNA_ECOLI (P77398) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
BINDING | 368 | 369 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
D-[IV] | ||||||||
REGION | Nter | 304 | /note="Formyltransferase ArnAFT" | |||||||||
BINDING | 86 | 88 | /ligand="(6R)-10-formyltetrahydrofolate" /ligand_id="ChEBI:CHEBI:195366" |
H-x-I | ||||||||
BINDING | 136 | 140 | /ligand="(6R)-10-formyltetrahydrofolate" /ligand_id="ChEBI:CHEBI:195366" |
[VIT]-x(3)-D | ||||||||
REGION | 314 | Cter | /note="Dehydrogenase ArnADH" | |||||||||
BINDING | 432 | 433 | /ligand="UDP-alpha-D-glucuronate" /ligand_id="ChEBI:CHEBI:58052" |
T-S | ||||||||
BINDING | 526 | 535 | /ligand="UDP-alpha-D-glucuronate" /ligand_id="ChEBI:CHEBI:58052" |
[KRQ]-x(6)-Q-x-R | ||||||||
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" /ligand_id="ChEBI:CHEBI:195366" |
R | ||||||||
BINDING | 347 | 347 | /ligand="NAD(+)" /ligand_id="ChEBI:CHEBI:57540" |
D | ||||||||
BINDING | 393 | 393 | /ligand="UDP-alpha-D-glucuronate" /ligand_id="ChEBI:CHEBI:58052" |
A | ||||||||
BINDING | 398 | 398 | /ligand="UDP-alpha-D-glucuronate" /ligand_id="ChEBI:CHEBI:58052" |
Y | ||||||||
BINDING | 460 | 460 | /ligand="UDP-alpha-D-glucuronate" /ligand_id="ChEBI:CHEBI:58052" |
R | ||||||||
BINDING | 492 | 492 | /ligand="UDP-alpha-D-glucuronate" /ligand_id="ChEBI:CHEBI:58052" |
N | ||||||||
BINDING | 613 | 613 | /ligand="UDP-alpha-D-glucuronate" /ligand_id="ChEBI:CHEBI:58052" |
Y | ||||||||
SITE | 102 | 102 | /note="Transition state stabilizer" | N | ||||||||
SITE | 140 | 140 | /note="Raises pKa of active site His" | D |
Additional information
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Size range | 654-687 amino acids |
Related rules |
MF_00182 |
Fusion | Nter: None Cter: None |