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B2TW38

- ARNA_SHIB3

UniProt

B2TW38 - ARNA_SHIB3

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Protein

Putative bifunctional polymyxin resistance protein ArnA

Gene

arnA

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).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 HisBy similarity
Binding sitei213 – 2131NADBy similarity
Binding sitei259 – 2591UDP-glucuronate; via carbonyl oxygenBy similarity
Binding sitei264 – 2641UDP-glucuronateBy similarity
Active sitei300 – 3001Proton acceptor; for decarboxylase activityBy similarity
Binding sitei326 – 3261UDP-glucuronateBy similarity
Binding sitei358 – 3581UDP-glucuronateBy similarity
Binding sitei479 – 4791UDP-glucuronateBy similarity
Active sitei485 – 4851Proton donor; for decarboxylase activityBy similarity

Regions

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

GO - Molecular functioni

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

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 ArnAPRO_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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 170170Formyltransferase ArnAFTAdd
BLAST
Regioni2 – 6510-formyltetrahydrofolate bindingBy similarity
Regioni180 – 526347Dehydrogenase ArnADHAdd
BLAST
Regioni298 – 2992UDP-glucuronate bindingBy similarity
Regioni392 – 40110UDP-glucuronate bindingBy similarity

Sequence similaritiesi

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

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_N.
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

        10         20         30         40         50
MVKRADAGAI VAQLRVAIAP DDIAITLHHK LCHAARQLLE QTLPAIKHGN
60 70 80 90 100
ILEIAQRENE ATCFGRRTPD DSFLEWHKPA SVLHNMVRAV ADPWPSAFSY
110 120 130 140 150
VGNQKFTVWS SRVHPHASKA QPGSVISIAP LLIACGDGAL EIVTGQAGDG
160 170 180 190 200
ITMQGSQLAQ TLGLVQGSRL NSQPACTARR RTRVLILGVN GFIGNHLTER
210 220 230 240 250
LLREDHYEVY GLDIGSDAIS RFLNHPHFHF VEGDISIHSE WIEYHVKKCD
260 270 280 290 300
VVLPLVAIAT PIEYTRNPLR VFELDFEENL RIIRYCVKYR KRIIFPSTSE
310 320 330 340 350
VYGMCSDKYF DEDHSNLIVG PVNKPRWIYS VSKQLLDRVI WAYGEKEGLQ
360 370 380 390 400
FTLFRPFNWM GPRLDNLNAA RIGSSRAITQ LILNLVEGSP IKLIDGGKQK
410 420 430 440 450
RCFTDIRDGI EALYRIIENA GNRCDGEIIN IGNPENEASI EELGKMLLAS
460 470 480 490 500
FEKHPLRHHF PPFAGFRVVE SSSYYGKGYQ DVEHRKPSIR NAHRCLDWEP
510 520
KIDMQETIDE TLDFFLRTVD LTDKPS
Length:526
Mass (Da):59,435
Last modified:July 1, 2008 - v1
Checksum:iAF2E061948764B2A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
CP001063 Genomic DNA. Translation: ACD07332.1 .
RefSeqi YP_001881078.1. NC_010658.1.

3D structure databases

ProteinModelPortali B2TW38.
ModBasei Search...
MobiDBi 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_N.
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: October 29, 2014
This is version 51 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.Curated

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