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B2TW38

- ARNA_SHIB3

UniProt

B2TW38 - ARNA_SHIB3

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Protein
Putative bifunctional polymyxin resistance protein ArnA
Gene
arnA, SbBS512_E2631
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Status
Reviewed - Annotation score: 4 out of 5 - Protein uncertaini

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 By similarity.

Catalytic activityi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei6 – 61Raises pKa of active site His By similarity
Binding sitei213 – 2131NAD By similarity
Binding sitei259 – 2591UDP-glucuronate; via carbonyl oxygen By similarity
Binding sitei264 – 2641UDP-glucuronate By similarity
Active sitei300 – 3001Proton acceptor; for decarboxylase activity By similarity
Binding sitei326 – 3261UDP-glucuronate By similarity
Binding sitei358 – 3581UDP-glucuronate By similarity
Binding sitei479 – 4791UDP-glucuronate By similarity
Active sitei485 – 4851Proton donor; for decarboxylase activity By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi234 – 2352NAD binding By similarity

GO - Molecular functioni

  1. coenzyme binding Source: InterPro
  2. hydroxymethyl-, formyl- and related transferase activity Source: InterPro
  3. oxidoreductase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. lipid A biosynthetic process Source: UniProtKB-KW
  2. lipopolysaccharide biosynthetic process Source: UniProtKB-UniPathway
  3. response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Keywords - Biological processi

Antibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciSBOY344609:GI0O-2630-MONOMER.
UniPathwayiUPA00030.
UPA00032; UER00492.
UPA00032; UER00494.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative bifunctional polymyxin resistance protein ArnA
Including the following 2 domains:
UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC:2.1.2.13)
Alternative name(s):
ArnAFT
UDP-L-Ara4N formyltransferase
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 namesi
Name:arnA
Ordered Locus Names:SbBS512_E2631
OrganismiShigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Taxonomic identifieri344609 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000001030: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 526526Putative bifunctional polymyxin resistance protein ArnA
PRO_0000379991Add
BLAST

Interactioni

Subunit structurei

Homohexamer, formed by a dimer of trimers By similarity.

Protein-protein interaction databases

STRINGi344609.SbBS512_E2631.

Structurei

3D structure databases

ProteinModelPortaliB2TW38.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 170170Formyltransferase ArnAFT
Add
BLAST
Regioni2 – 6510-formyltetrahydrofolate binding By similarity
Regioni180 – 526347Dehydrogenase ArnADH
Add
BLAST
Regioni298 – 2992UDP-glucuronate binding By similarity
Regioni392 – 40110UDP-glucuronate binding By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0451.
HOGENOMiHOG000247761.
KOiK10011.
OMAiVRYCVKY.
OrthoDBiEOG6B09WV.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
3.40.50.720. 1 hit.
InterProiIPR001509. Epimerase_deHydtase.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01370. Epimerase. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
[Graphical view]
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.

Sequencei

Sequence statusi: Complete.

B2TW38-1 [UniParc]FASTAAdd to Basket

« Hide

MVKRADAGAI VAQLRVAIAP DDIAITLHHK LCHAARQLLE QTLPAIKHGN    50
ILEIAQRENE ATCFGRRTPD DSFLEWHKPA SVLHNMVRAV ADPWPSAFSY 100
VGNQKFTVWS SRVHPHASKA QPGSVISIAP LLIACGDGAL EIVTGQAGDG 150
ITMQGSQLAQ TLGLVQGSRL NSQPACTARR RTRVLILGVN GFIGNHLTER 200
LLREDHYEVY GLDIGSDAIS RFLNHPHFHF VEGDISIHSE WIEYHVKKCD 250
VVLPLVAIAT PIEYTRNPLR VFELDFEENL RIIRYCVKYR KRIIFPSTSE 300
VYGMCSDKYF DEDHSNLIVG PVNKPRWIYS VSKQLLDRVI WAYGEKEGLQ 350
FTLFRPFNWM GPRLDNLNAA RIGSSRAITQ LILNLVEGSP IKLIDGGKQK 400
RCFTDIRDGI EALYRIIENA GNRCDGEIIN IGNPENEASI EELGKMLLAS 450
FEKHPLRHHF PPFAGFRVVE SSSYYGKGYQ DVEHRKPSIR NAHRCLDWEP 500
KIDMQETIDE TLDFFLRTVD LTDKPS 526
Length:526
Mass (Da):59,435
Last modified:July 1, 2008 - v1
Checksum:iAF2E061948764B2A
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001063 Genomic DNA. Translation: ACD07332.1.
RefSeqiYP_001881078.1. NC_010658.1.

Genome annotation databases

EnsemblBacteriaiACD07332; ACD07332; SbBS512_E2631.
GeneIDi6270240.
KEGGisbc:SbBS512_E2631.
PATRICi18672309. VBIShiBoy129590_2914.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP001063 Genomic DNA. Translation: ACD07332.1 .
RefSeqi YP_001881078.1. NC_010658.1.

3D structure databases

ProteinModelPortali B2TW38.
ModBasei Search...

Protein-protein interaction databases

STRINGi 344609.SbBS512_E2631.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACD07332 ; ACD07332 ; SbBS512_E2631 .
GeneIDi 6270240.
KEGGi sbc:SbBS512_E2631.
PATRICi 18672309. VBIShiBoy129590_2914.

Phylogenomic databases

eggNOGi COG0451.
HOGENOMi HOG000247761.
KOi K10011.
OMAi VRYCVKY.
OrthoDBi EOG6B09WV.

Enzyme and pathway databases

UniPathwayi UPA00030 .
UPA00032 ; UER00492 .
UPA00032 ; UER00494 .
BioCyci SBOY344609:GI0O-2630-MONOMER.

Family and domain databases

Gene3Di 3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
3.40.50.720. 1 hit.
InterProi IPR001509. Epimerase_deHydtase.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01370. Epimerase. 1 hit.
PF02911. Formyl_trans_C. 1 hit.
[Graphical view ]
SUPFAMi SSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiARNA_SHIB3
AccessioniPrimary (citable) accession number: B2TW38
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

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

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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