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Protein

UDP-N-acetylglucosamine 2-epimerase

Gene

mnaA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of UDP-N-acetylglucosamine into UDP-N-acetylmannosamine, a precursor of the teichoic acid linkage unit.1 Publication

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine.

Pathwayi: poly(glycerol phosphate) teichoic acid biosynthesis

This protein is involved in the pathway poly(glycerol phosphate) teichoic acid biosynthesis, which is part of Cell wall biogenesis.
View all proteins of this organism that are known to be involved in the pathway poly(glycerol phosphate) teichoic acid biosynthesis and in Cell wall biogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Cell wall biogenesis/degradation, Teichoic acid biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU35660-MONOMER.
MetaCyc:MONOMER-8808.
UniPathwayiUPA00827.

Names & Taxonomyi

Protein namesi
Recommended name:
UDP-N-acetylglucosamine 2-epimerase (EC:5.1.3.14)
Alternative name(s):
UDP-GlcNAc-2-epimerase
Gene namesi
Name:mnaA
Ordered Locus Names:BSU35660
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691T → I in TS-21; temperature-sensitive, develops, at the nonpermissive temperature (47 degrees Celsius), a coccoid-like morphology, i.e. a phenotype associated with a deficient synthesis of poly(glycerol phosphate) teichoic acid. 1 Publication
Mutagenesisi374 – 3741P → L in TS-21; temperature-sensitive, develops, at the nonpermissive temperature (47 degrees Celsius), a coccoid-like morphology, i.e. a phenotype associated with a deficient synthesis of poly(glycerol phosphate) teichoic acid. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 380380UDP-N-acetylglucosamine 2-epimerasePRO_0000208532Add
BLAST

Proteomic databases

PaxDbiP39131.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019286.

Structurei

Secondary structure

1
380
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi13 – 2614Combined sources
Beta strandi32 – 387Combined sources
Beta strandi41 – 433Combined sources
Helixi44 – 5310Combined sources
Beta strandi58 – 603Combined sources
Helixi70 – 8718Combined sources
Beta strandi91 – 966Combined sources
Helixi100 – 11112Combined sources
Beta strandi115 – 1195Combined sources
Turni128 – 1336Combined sources
Helixi134 – 14411Combined sources
Beta strandi146 – 1527Combined sources
Helixi153 – 1619Combined sources
Helixi166 – 1683Combined sources
Beta strandi169 – 1713Combined sources
Helixi175 – 1839Combined sources
Helixi191 – 1966Combined sources
Beta strandi199 – 2057Combined sources
Helixi209 – 2113Combined sources
Helixi214 – 22916Combined sources
Beta strandi233 – 2386Combined sources
Helixi243 – 25311Combined sources
Beta strandi259 – 2624Combined sources
Helixi267 – 27610Combined sources
Beta strandi278 – 2825Combined sources
Helixi285 – 29410Combined sources
Beta strandi298 – 3003Combined sources
Helixi308 – 3125Combined sources
Beta strandi315 – 3184Combined sources
Helixi323 – 33513Combined sources
Helixi337 – 3437Combined sources
Helixi355 – 36612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6CX-ray2.90A/B2-380[»]
4FKZX-ray1.69A/B1-380[»]
ProteinModelPortaliP39131.
SMRiP39131. Positions 1-379.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39131.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105EAG. Bacteria.
COG0381. LUCA.
HOGENOMiHOG000076048.
InParanoidiP39131.
KOiK01791.
OMAiIMKERQT.
PhylomeDBiP39131.

Family and domain databases

InterProiIPR003331. UDP_GlcNAc_Epimerase_2_dom.
IPR029767. WecB-like.
[Graphical view]
PfamiPF02350. Epimerase_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00236. wecB. 1 hit.

Sequencei

Sequence statusi: Complete.

P39131-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKLKVMTVF GTRPEAIKMA PLVLELKKYP EIDSYVTVTA QHRQMLDQVL
60 70 80 90 100
DAFHIKPDFD LNIMKERQTL AEITSNALVR LDELFKDIKP DIVLVHGDTT
110 120 130 140 150
TTFAGSLAAF YHQIAVGHVE AGLRTGNKYS PFPEELNRQM TGAIADLHFA
160 170 180 190 200
PTGQAKDNLL KENKKADSIF VTGNTAIDAL NTTVRDGYSH PVLDQVGEDK
210 220 230 240 250
MILLTAHRRE NLGEPMENMF KAIRRIVGEF EDVQVVYPVH LNPVVREAAH
260 270 280 290 300
KHFGDSDRVH LIEPLEVIDF HNFAAKSHFI LTDSGGVQEE APSLGKPVLV
310 320 330 340 350
LRDTTERPEG VEAGTLKLAG TDEENIYQLA KQLLTDPDEY KKMSQASNPY
360 370 380
GDGEASRRIV EELLFHYGYR KEQPDSFTGK
Length:380
Mass (Da):42,634
Last modified:February 1, 1995 - v1
Checksum:i63A73C8D1E7D3B5A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22516 Genomic DNA. Translation: CAA80240.1.
AL009126 Genomic DNA. Translation: CAB15583.1.
PIRiD70049.
RefSeqiNP_391446.1. NC_000964.3.
WP_003243178.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15583; CAB15583; BSU35660.
GeneIDi936209.
KEGGibsu:BSU35660.
PATRICi18979142. VBIBacSub10457_3733.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z22516 Genomic DNA. Translation: CAA80240.1.
AL009126 Genomic DNA. Translation: CAB15583.1.
PIRiD70049.
RefSeqiNP_391446.1. NC_000964.3.
WP_003243178.1. NZ_JNCM01000033.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1O6CX-ray2.90A/B2-380[»]
4FKZX-ray1.69A/B1-380[»]
ProteinModelPortaliP39131.
SMRiP39131. Positions 1-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100019286.

Proteomic databases

PaxDbiP39131.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15583; CAB15583; BSU35660.
GeneIDi936209.
KEGGibsu:BSU35660.
PATRICi18979142. VBIBacSub10457_3733.

Phylogenomic databases

eggNOGiENOG4105EAG. Bacteria.
COG0381. LUCA.
HOGENOMiHOG000076048.
InParanoidiP39131.
KOiK01791.
OMAiIMKERQT.
PhylomeDBiP39131.

Enzyme and pathway databases

UniPathwayiUPA00827.
BioCyciBSUB:BSU35660-MONOMER.
MetaCyc:MONOMER-8808.

Miscellaneous databases

EvolutionaryTraceiP39131.

Family and domain databases

InterProiIPR003331. UDP_GlcNAc_Epimerase_2_dom.
IPR029767. WecB-like.
[Graphical view]
PfamiPF02350. Epimerase_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00236. wecB. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMNAA_BACSU
AccessioniPrimary (citable) accession number: P39131
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 7, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.