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Protein

N-acetylneuraminate epimerase

Gene

nanM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts alpha-N-acetylneuranimic acid (Neu5Ac) to the beta-anomer, accelerating the equilibrium between the alpha- and beta-anomers. Probably facilitates sialidase-negative bacteria to compete sucessfully for limited amounts of extracellular Neu5Ac, which is likely taken up in the beta-anomer. In addition, the rapid removal of sialic acid from solution might be advantageous to the bacterium to damp down host responses.1 Publication

Catalytic activityi

N-acetyl-alpha-neuraminate = N-acetyl-beta-neuraminate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei228Proton acceptorSequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciEcoCyc:G7920-MONOMER.
ECOL316407:JW5777-MONOMER.
MetaCyc:G7920-MONOMER.
BRENDAi5.1.3.24. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylneuraminate epimerase (EC:5.1.3.24)
Alternative name(s):
N-acetylneuraminate mutarotase
Short name:
Neu5Ac mutarotase
Sialic acid epimerase
Gene namesi
Name:nanM
Synonyms:yjhT
Ordered Locus Names:b4310, JW5777
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12562. nanM.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi30K → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi228E → A: Great decrease in catalytic activity. 1 Publication1
Mutagenesisi234R → A: Decrease in catalytic activity. 1 Publication1
Mutagenesisi297H → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi302K → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi328Y → A: No effect on catalytic activity. 1 Publication1
Mutagenesisi344E → A: No effect on catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Add BLAST19
ChainiPRO_000001665520 – 368N-acetylneuraminate epimeraseAdd BLAST349

Proteomic databases

PaxDbiP39371.
PRIDEiP39371.

Expressioni

Inductioni

Induced by N-acetylneuraminate and modulated by N-acetylglucosamine, via the NanR and NagC regulators.1 Publication

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi4259377. 10 interactors.
DIPiDIP-12628N.
STRINGi511145.b4310.

Structurei

Secondary structure

1368
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi33 – 37Combined sources5
Beta strandi40 – 44Combined sources5
Helixi46 – 48Combined sources3
Beta strandi52 – 56Combined sources5
Beta strandi59 – 61Combined sources3
Beta strandi64 – 66Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi86 – 90Combined sources5
Beta strandi93 – 95Combined sources3
Beta strandi101 – 103Combined sources3
Beta strandi107 – 111Combined sources5
Turni112 – 115Combined sources4
Beta strandi116 – 119Combined sources4
Beta strandi132 – 136Combined sources5
Beta strandi139 – 143Combined sources5
Helixi148 – 161Combined sources14
Helixi165 – 176Combined sources12
Helixi180 – 183Combined sources4
Beta strandi188 – 192Combined sources5
Turni194 – 196Combined sources3
Beta strandi199 – 204Combined sources6
Beta strandi214 – 218Combined sources5
Beta strandi221 – 225Combined sources5
Beta strandi228 – 230Combined sources3
Beta strandi238 – 242Combined sources5
Beta strandi245 – 247Combined sources3
Beta strandi249 – 252Combined sources4
Turni258 – 260Combined sources3
Beta strandi266 – 270Combined sources5
Beta strandi273 – 277Combined sources5
Helixi285 – 290Combined sources6
Turni296 – 299Combined sources4
Beta strandi307 – 310Combined sources4
Beta strandi317 – 321Combined sources5
Beta strandi327 – 334Combined sources8
Beta strandi337 – 344Combined sources8
Helixi346 – 348Combined sources3
Beta strandi350 – 358Combined sources9
Beta strandi365 – 367Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UVKX-ray1.50A/B20-368[»]
ProteinModelPortaliP39371.
SMRiP39371.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39371.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati40 – 84Kelch 1Add BLAST45
Repeati86 – 137Kelch 2Add BLAST52
Repeati139 – 173Kelch 3Add BLAST35
Repeati174 – 219Kelch 4Add BLAST46
Repeati222 – 265Kelch 5Add BLAST44
Repeati287 – 336Kelch 6Add BLAST50
Repeati338 – 367Kelch 7Add BLAST30

Sequence similaritiesi

Belongs to the NanM family.Curated
Contains 7 Kelch repeats.Curated

Keywords - Domaini

Kelch repeat, Repeat, Signal

Phylogenomic databases

eggNOGiENOG4108MX5. Bacteria.
COG3055. LUCA.
HOGENOMiHOG000218207.
InParanoidiP39371.
KOiK17948.
OMAiGAAFTIQ.
PhylomeDBiP39371.

Family and domain databases

Gene3Di2.120.10.80. 2 hits.
HAMAPiMF_01195. NanM. 1 hit.
InterProiIPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR019936. Mutatrotase_YjhT-like.
[Graphical view]
PfamiPF01344. Kelch_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03547. muta_rot_YjhT. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P39371-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKTITALAI MMASFAANAS VLPETPVPFK SGTGAIDNDT VYIGLGSAGT
60 70 80 90 100
AWYKLDTQAK DKKWTALAAF PGGPRDQATS AFIDGNLYVF GGIGKNSEGL
110 120 130 140 150
TQVFNDVHKY NPKTNSWVKL MSHAPMGMAG HVTFVHNGKA YVTGGVNQNI
160 170 180 190 200
FNGYFEDLNE AGKDSTAIDK INAHYFDKKA EDYFFNKFLL SFDPSTQQWS
210 220 230 240 250
YAGESPWYGT AGAAVVNKGD KTWLINGEAK PGLRTDAVFE LDFTGNNLKW
260 270 280 290 300
NKLAPVSSPD GVAGGFAGIS NDSLIFAGGA GFKGSRENYQ NGKNYAHEGL
310 320 330 340 350
KKSYSTDIHL WHNGKWDKSG ELSQGRAYGV SLPWNNSLLI IGGETAGGKA
360
VTDSVLITVK DNKVTVQN
Length:368
Mass (Da):39,572
Last modified:May 30, 2000 - v2
Checksum:i1194F392C51EA204
GO

Sequence cautioni

The sequence AAA97206 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Mass spectrometryi

Molecular mass is 38685±4 Da from positions 20 - 368. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97206.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77266.2.
AP009048 Genomic DNA. Translation: BAE78303.1.
PIRiS56535.
RefSeqiNP_418730.4. NC_000913.3.
WP_001309184.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC77266; AAC77266; b4310.
BAE78303; BAE78303; BAE78303.
GeneIDi949106.
KEGGiecj:JW5777.
eco:b4310.
PATRICi32124214. VBIEscCol129921_4450.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14003 Genomic DNA. Translation: AAA97206.1. Different initiation.
U00096 Genomic DNA. Translation: AAC77266.2.
AP009048 Genomic DNA. Translation: BAE78303.1.
PIRiS56535.
RefSeqiNP_418730.4. NC_000913.3.
WP_001309184.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2UVKX-ray1.50A/B20-368[»]
ProteinModelPortaliP39371.
SMRiP39371.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259377. 10 interactors.
DIPiDIP-12628N.
STRINGi511145.b4310.

Proteomic databases

PaxDbiP39371.
PRIDEiP39371.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC77266; AAC77266; b4310.
BAE78303; BAE78303; BAE78303.
GeneIDi949106.
KEGGiecj:JW5777.
eco:b4310.
PATRICi32124214. VBIEscCol129921_4450.

Organism-specific databases

EchoBASEiEB2450.
EcoGeneiEG12562. nanM.

Phylogenomic databases

eggNOGiENOG4108MX5. Bacteria.
COG3055. LUCA.
HOGENOMiHOG000218207.
InParanoidiP39371.
KOiK17948.
OMAiGAAFTIQ.
PhylomeDBiP39371.

Enzyme and pathway databases

BioCyciEcoCyc:G7920-MONOMER.
ECOL316407:JW5777-MONOMER.
MetaCyc:G7920-MONOMER.
BRENDAi5.1.3.24. 2026.

Miscellaneous databases

EvolutionaryTraceiP39371.
PROiP39371.

Family and domain databases

Gene3Di2.120.10.80. 2 hits.
HAMAPiMF_01195. NanM. 1 hit.
InterProiIPR015915. Kelch-typ_b-propeller.
IPR006652. Kelch_1.
IPR019936. Mutatrotase_YjhT-like.
[Graphical view]
PfamiPF01344. Kelch_1. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03547. muta_rot_YjhT. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiNANM_ECOLI
AccessioniPrimary (citable) accession number: P39371
Secondary accession number(s): Q2M603
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 119 of the entry and version 2 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. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.