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B2TW38 (ARNA_SHIB3) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Putative bifunctional polymyxin resistance protein ArnA

Including the following 2 domains:

  1. UDP-4-amino-4-deoxy-L-arabinose formyltransferase
    EC=2.1.2.13
    Alternative name(s):
    ArnAFT
    UDP-L-Ara4N formyltransferase
  2. UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating
    EC=1.1.1.305
    Alternative name(s):
    ArnADH
    UDP-GlcUA decarboxylase
    UDP-glucuronic acid dehydrogenase
Gene names
Name:arnA
Ordered Locus Names:SbBS512_E2631
OrganismShigella boydii serotype 18 (strain CDC 3083-94 / BS512) [Complete proteome] [HAMAP]
Taxonomic identifier344609 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length526 AA.
Sequence statusComplete.
Protein existenceUncertain

General annotation (Comments)

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 By similarity.

Catalytic activity

UDP-alpha-D-glucuronate + NAD+ = UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH.

10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinose = 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinose.

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.

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.

Bacterial outer membrane biogenesis; lipopolysaccharide biosynthesis.

Subunit structure

Homohexamer, formed by a dimer of trimers By similarity.

Sequence similarities

In the N-terminal section; belongs to the Fmt family. UDP-L-Ara4N formyltransferase subfamily.

In the C-terminal section; belongs to the NAD(P)-dependent epimerase/dehydratase family. UDP-glucuronic acid decarboxylase subfamily.

Caution

Could be the product of a pseudogene. The N-terminal region is truncated when compared to orthologs.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 526526Putative bifunctional polymyxin resistance protein ArnA
PRO_0000379991

Regions

Nucleotide binding234 – 2352NAD binding By similarity
Region1 – 170170Formyltransferase ArnAFT
Region2 – 6510-formyltetrahydrofolate binding By similarity
Region180 – 526347Dehydrogenase ArnADH
Region298 – 2992UDP-glucuronate binding By similarity
Region392 – 40110UDP-glucuronate binding By similarity

Sites

Active site3001Proton acceptor; for decarboxylase activity By similarity
Active site4851Proton donor; for decarboxylase activity By similarity
Binding site2131NAD By similarity
Binding site2591UDP-glucuronate; via carbonyl oxygen By similarity
Binding site2641UDP-glucuronate By similarity
Binding site3261UDP-glucuronate By similarity
Binding site3581UDP-glucuronate By similarity
Binding site4791UDP-glucuronate By similarity
Site61Raises pKa of active site His By similarity

Sequences

Sequence LengthMass (Da)Tools
B2TW38 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: AF2E061948764B2A

FASTA52659,435
        10         20         30         40         50         60 
MVKRADAGAI VAQLRVAIAP DDIAITLHHK LCHAARQLLE QTLPAIKHGN ILEIAQRENE 

        70         80         90        100        110        120 
ATCFGRRTPD DSFLEWHKPA SVLHNMVRAV ADPWPSAFSY VGNQKFTVWS SRVHPHASKA 

       130        140        150        160        170        180 
QPGSVISIAP LLIACGDGAL EIVTGQAGDG ITMQGSQLAQ TLGLVQGSRL NSQPACTARR 

       190        200        210        220        230        240 
RTRVLILGVN GFIGNHLTER LLREDHYEVY GLDIGSDAIS RFLNHPHFHF VEGDISIHSE 

       250        260        270        280        290        300 
WIEYHVKKCD VVLPLVAIAT PIEYTRNPLR VFELDFEENL RIIRYCVKYR KRIIFPSTSE 

       310        320        330        340        350        360 
VYGMCSDKYF DEDHSNLIVG PVNKPRWIYS VSKQLLDRVI WAYGEKEGLQ FTLFRPFNWM 

       370        380        390        400        410        420 
GPRLDNLNAA RIGSSRAITQ LILNLVEGSP IKLIDGGKQK RCFTDIRDGI EALYRIIENA 

       430        440        450        460        470        480 
GNRCDGEIIN IGNPENEASI EELGKMLLAS FEKHPLRHHF PPFAGFRVVE SSSYYGKGYQ 

       490        500        510        520 
DVEHRKPSIR NAHRCLDWEP KIDMQETIDE TLDFFLRTVD LTDKPS 

« Hide

References

[1]"Complete sequence of Shigella boydii serotype 18 strain BS512."
Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R., Jiang L., Ravel J., Sebastian Y.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CDC 3083-94 / BS512.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001063 Genomic DNA. Translation: ACD07332.1.
RefSeqYP_001881078.1. NC_010658.1.

3D structure databases

ProteinModelPortalB2TW38.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING344609.SbBS512_E2631.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACD07332; ACD07332; SbBS512_E2631.
GeneID6270240.
KEGGsbc:SbBS512_E2631.
PATRIC18672309. VBIShiBoy129590_2914.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0451.
HOGENOMHOG000247761.
KOK10011.
OMAVRYCVKY.
OrthoDBEOG6B09WV.

Enzyme and pathway databases

BioCycSBOY344609:GI0O-2630-MONOMER.
UniPathwayUPA00030.
UPA00032; UER00492.
UPA00032; UER00494.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
3.40.50.720. 1 hit.
InterProIPR001509. Epimerase_deHydtase.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01370. Epimerase. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
[Graphical view]
SUPFAMSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
ProtoNetSearch...

Entry information

Entry nameARNA_SHIB3
AccessionPrimary (citable) accession number: B2TW38
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways