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UniProtKB - P77398 (ARNA_ECOLI)
Protein
Bifunctional polymyxin resistance protein ArnA
Gene
arnA
Organism
Escherichia coli (strain K12)
Status
Functioni
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.
4 PublicationsCatalytic activityi
- EC:1.1.1.3051 PublicationThis reaction proceeds in the forward1 Publication direction.
- (6S)-10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-β-L-arabinose = (6S)-5,6,7,8-tetrahydrofolate + H+ + UDP-4-deoxy-4-formamido-β-L-arabinose1 PublicationEC:2.1.2.131 PublicationThis reaction proceeds in the forward1 Publication direction.
Kineticsi
- KM=0.76 mM for NAD+1 Publication
- KM=0.086 mM for UDP-GlcUA1 Publication
: UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis Pathwayi
This protein is involved in step 1 and 3 of the subpathway that synthesizes UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate.1 Publication This subpathway is part of the pathway UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis, which is itself part of Nucleotide-sugar biosynthesis.View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP-4-deoxy-4-formamido-beta-L-arabinose from UDP-alpha-D-glucuronate, the pathway UDP-4-deoxy-4-formamido-beta-L-arabinose biosynthesis and in Nucleotide-sugar biosynthesis.
Pathwayi: lipopolysaccharide biosynthesis
This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.1 PublicationView all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 102 | Transition state stabilizer | 1 | |
Active sitei | 104 | Proton donor; for formyltransferase activity | 1 | |
Binding sitei | 114 | 10-formyltetrahydrofolate | 1 | |
Sitei | 140 | Raises pKa of active site His | 1 | |
Binding sitei | 347 | NAD | 1 | |
Binding sitei | 393 | UDP-glucuronate; via carbonyl oxygen | 1 | |
Binding sitei | 398 | UDP-glucuronate | 1 | |
Active sitei | 434 | Proton acceptor; for decarboxylase activity | 1 | |
Binding sitei | 460 | UDP-glucuronate | 1 | |
Binding sitei | 492 | UDP-glucuronate | 1 | |
Binding sitei | 613 | UDP-glucuronate | 1 | |
Active sitei | 619 | Proton donor; for decarboxylase activity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 368 – 369 | NAD binding | 2 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
- NAD+ binding Source: UniProtKB
- UDP-4-amino-4-deoxy-L-arabinose formyltransferase activity Source: EcoCyc
- UDP-glucuronate decarboxylase activity Source: UniProtKB
- UDP-glucuronic acid dehydrogenase activity Source: EcoCyc
GO - Biological processi
- lipid A biosynthetic process Source: UniProtKB-KW
- lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway
- response to antibiotic Source: EcoCyc
- UDP-4-deoxy-4-formamido-beta-L-arabinopyranose biosynthetic process Source: EcoCyc
- UDP-D-xylose biosynthetic process Source: UniProtKB
Keywordsi
Molecular function | Multifunctional enzyme, Oxidoreductase, Transferase |
Biological process | Antibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis |
Ligand | NAD |
Enzyme and pathway databases
BioCyci | EcoCyc:G7168-MONOMER |
BRENDAi | 1.1.1.305, 2026 2.1.2.13, 2026 |
SABIO-RKi | P77398 |
UniPathwayi | UPA00030 UPA00032;UER00492 UPA00032;UER00494 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional polymyxin resistance protein ArnAAlternative name(s): Polymyxin resistance protein PmrI Including the following 2 domains: UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC:2.1.2.131 Publication) Alternative name(s): ArnAFT UDP-L-Ara4N formyltransferase UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating (EC:1.1.1.3051 Publication) Alternative name(s): ArnADH UDP-GlcUA decarboxylase UDP-glucuronic acid dehydrogenase |
Gene namesi | Name:arnA Synonyms:pmrI, yfbG Ordered Locus Names:b2255, JW2249 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 102 | N → A: No formyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 104 | H → A: 25-fold lower formyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 104 | H → K: Less than 1% residual formyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 140 | D → A or N: Less than 1% residual formyltransferase activity. 1 Publication | 1 | |
Mutagenesisi | 433 | S → A: 40-fold lower specific activity. 2 Publications | 1 | |
Mutagenesisi | 433 | S → T: No activity. 2 Publications | 1 | |
Mutagenesisi | 434 | E → A: 100-fold lower specific activity. 1 Publication | 1 | |
Mutagenesisi | 434 | E → Q: No activity. 1 Publication | 1 | |
Mutagenesisi | 619 | R → E or Y: No activity. 1 Publication | 1 | |
Mutagenesisi | 619 | R → M: 400-fold lower activity. 1 Publication | 1 |
Chemistry databases
DrugBanki | DB03256, (6R)-Folinic acid DB03685, Uridine monophosphate |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000083098 | 1 – 660 | Bifunctional polymyxin resistance protein ArnAAdd BLAST | 660 |
Proteomic databases
PaxDbi | P77398 |
PRIDEi | P77398 |
Expressioni
Inductioni
Induced by BasR.1 Publication
Interactioni
Subunit structurei
Homohexamer, formed by a dimer of trimers.
2 PublicationsBinary interactionsi
P77398
With | #Exp. | IntAct |
---|---|---|
itself | 3 | EBI-545305,EBI-545305 |
ynbC [P76092] | 2 | EBI-545305,EBI-544837 |
GO - Molecular functioni
- identical protein binding Source: EcoCyc
Protein-protein interaction databases
BioGRIDi | 4260497, 265 interactors 851996, 2 interactors |
DIPi | DIP-11961N |
IntActi | P77398, 15 interactors |
STRINGi | 511145.b2255 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
AlphaFoldDBi | P77398 |
SMRi | P77398 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P77398 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 304 | Formyltransferase ArnAFTAdd BLAST | 304 | |
Regioni | 86 – 88 | 10-formyltetrahydrofolate binding | 3 | |
Regioni | 136 – 140 | 10-formyltetrahydrofolate binding | 5 | |
Regioni | 314 – 660 | Dehydrogenase ArnADHAdd BLAST | 347 | |
Regioni | 432 – 433 | UDP-glucuronate binding | 2 | |
Regioni | 526 – 535 | UDP-glucuronate binding | 10 |
Sequence similaritiesi
In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily.Curated
In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.Curated
Phylogenomic databases
eggNOGi | COG0223, Bacteria COG0451, Bacteria |
HOGENOMi | CLU_007383_23_1_6 |
InParanoidi | P77398 |
OMAi | VRYCVKY |
PhylomeDBi | P77398 |
Family and domain databases
CDDi | cd05257, Arna_like_SDR_e, 1 hit |
HAMAPi | MF_01166, ArnA, 1 hit |
InterProi | View protein in InterPro IPR045869, Arna-like_SDR_e IPR021168, Bifun_polymyxin_resist_ArnA IPR001509, Epimerase_deHydtase IPR005793, Formyl_trans_C IPR002376, Formyl_transf_N IPR036477, Formyl_transf_N_sf IPR011034, Formyl_transferase-like_C_sf IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF01370, Epimerase, 1 hit PF02911, Formyl_trans_C, 1 hit PF00551, Formyl_trans_N, 1 hit |
PIRSFi | PIRSF036506, Bifun_polymyxin_resist_ArnA, 1 hit |
SUPFAMi | SSF50486, SSF50486, 1 hit SSF51735, SSF51735, 1 hit SSF53328, SSF53328, 1 hit |
i Sequence
Sequence statusi: Complete.
P77398-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MKTVVFAYHD MGCLGIEALL AAGYEISAIF THTDNPGEKA FYGSVARLAA
60 70 80 90 100
ERGIPVYAPD NVNHPLWVER IAQLSPDVIF SFYYRHLIYD EILQLAPAGA
110 120 130 140 150
FNLHGSLLPK YRGRAPLNWV LVNGETETGV TLHRMVKRAD AGAIVAQLRI
160 170 180 190 200
AIAPDDIAIT LHHKLCHAAR QLLEQTLPAI KHGNILEIAQ RENEATCFGR
210 220 230 240 250
RTPDDSFLEW HKPASVLHNM VRAVADPWPG AFSYVGNQKF TVWSSRVHPH
260 270 280 290 300
ASKAQPGSVI SVAPLLIACG DGALEIVTGQ AGDGITMQGS QLAQTLGLVQ
310 320 330 340 350
GSRLNSQPAC TARRRTRVLI LGVNGFIGNH LTERLLREDH YEVYGLDIGS
360 370 380 390 400
DAISRFLNHP HFHFVEGDIS IHSEWIEYHV KKCDVVLPLV AIATPIEYTR
410 420 430 440 450
NPLRVFELDF EENLRIIRYC VKYRKRIIFP STSEVYGMCS DKYFDEDHSN
460 470 480 490 500
LIVGPVNKPR WIYSVSKQLL DRVIWAYGEK EGLQFTLFRP FNWMGPRLDN
510 520 530 540 550
LNAARIGSSR AITQLILNLV EGSPIKLIDG GKQKRCFTDI RDGIEALYRI
560 570 580 590 600
IENAGNRCDG EIINIGNPEN EASIEELGEM LLASFEKHPL RHHFPPFAGF
610 620 630 640 650
RVVESSSYYG KGYQDVEHRK PSIRNAHRCL DWEPKIDMQE TIDETLDFFL
660
RTVDLTDKPS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY057445 Genomic DNA Translation: AAL23678.1 U00096 Genomic DNA Translation: AAC75315.1 AP009048 Genomic DNA Translation: BAA16078.1 |
PIRi | E64996 |
RefSeqi | NP_416758.1, NC_000913.3 WP_000860273.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC75315; AAC75315; b2255 BAA16078; BAA16078; BAA16078 |
GeneIDi | 947683 |
KEGGi | ecj:JW2249 eco:b2255 |
PATRICi | fig|1411691.4.peg.4482 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY057445 Genomic DNA Translation: AAL23678.1 U00096 Genomic DNA Translation: AAC75315.1 AP009048 Genomic DNA Translation: BAA16078.1 |
PIRi | E64996 |
RefSeqi | NP_416758.1, NC_000913.3 WP_000860273.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1U9J | X-ray | 2.40 | A | 306-660 | [»] | |
1YRW | X-ray | 1.70 | A | 1-300 | [»] | |
1Z73 | X-ray | 2.50 | A | 306-660 | [»] | |
1Z74 | X-ray | 2.70 | A | 306-660 | [»] | |
1Z75 | X-ray | 2.40 | A | 306-660 | [»] | |
1Z7B | X-ray | 2.31 | A | 306-660 | [»] | |
1Z7E | X-ray | 3.00 | A/B/C/D/E/F | 1-660 | [»] | |
2BLL | X-ray | 2.30 | A | 317-660 | [»] | |
2BLN | X-ray | 1.20 | A/B | 1-305 | [»] | |
4WKG | X-ray | 2.70 | A/B/C/D/E/F | 1-660 | [»] | |
6PIH | electron microscopy | 6.60 | A/B/C/D/E/F | 1-300 | [»] | |
G/H/I/J/K/L | 317-660 | [»] | ||||
6PIK | electron microscopy | 7.80 | A/B/C/D | 1-300 | [»] | |
E/F/G/H | 317-660 | [»] | ||||
AlphaFoldDBi | P77398 | |||||
SMRi | P77398 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4260497, 265 interactors 851996, 2 interactors |
DIPi | DIP-11961N |
IntActi | P77398, 15 interactors |
STRINGi | 511145.b2255 |
Chemistry databases
DrugBanki | DB03256, (6R)-Folinic acid DB03685, Uridine monophosphate |
Proteomic databases
PaxDbi | P77398 |
PRIDEi | P77398 |
Genome annotation databases
EnsemblBacteriai | AAC75315; AAC75315; b2255 BAA16078; BAA16078; BAA16078 |
GeneIDi | 947683 |
KEGGi | ecj:JW2249 eco:b2255 |
PATRICi | fig|1411691.4.peg.4482 |
Organism-specific databases
EchoBASEi | EB3844 |
Phylogenomic databases
eggNOGi | COG0223, Bacteria COG0451, Bacteria |
HOGENOMi | CLU_007383_23_1_6 |
InParanoidi | P77398 |
OMAi | VRYCVKY |
PhylomeDBi | P77398 |
Enzyme and pathway databases
UniPathwayi | UPA00030 UPA00032;UER00492 UPA00032;UER00494 |
BioCyci | EcoCyc:G7168-MONOMER |
BRENDAi | 1.1.1.305, 2026 2.1.2.13, 2026 |
SABIO-RKi | P77398 |
Miscellaneous databases
EvolutionaryTracei | P77398 |
PROi | PR:P77398 |
Family and domain databases
CDDi | cd05257, Arna_like_SDR_e, 1 hit |
HAMAPi | MF_01166, ArnA, 1 hit |
InterProi | View protein in InterPro IPR045869, Arna-like_SDR_e IPR021168, Bifun_polymyxin_resist_ArnA IPR001509, Epimerase_deHydtase IPR005793, Formyl_trans_C IPR002376, Formyl_transf_N IPR036477, Formyl_transf_N_sf IPR011034, Formyl_transferase-like_C_sf IPR036291, NAD(P)-bd_dom_sf |
Pfami | View protein in Pfam PF01370, Epimerase, 1 hit PF02911, Formyl_trans_C, 1 hit PF00551, Formyl_trans_N, 1 hit |
PIRSFi | PIRSF036506, Bifun_polymyxin_resist_ArnA, 1 hit |
SUPFAMi | SSF50486, SSF50486, 1 hit SSF51735, SSF51735, 1 hit SSF53328, SSF53328, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ARNA_ECOLI | |
Accessioni | P77398Primary (citable) accession number: P77398 Secondary accession number(s): Q56VX0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1999 |
Last sequence update: | February 1, 1997 | |
Last modified: | May 25, 2022 | |
This is version 185 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families