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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei228 – 2281Proton acceptorSequence analysis

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi30 – 301K → A: No effect on catalytic activity. 1 Publication
Mutagenesisi228 – 2281E → A: Great decrease in catalytic activity. 1 Publication
Mutagenesisi234 – 2341R → A: Decrease in catalytic activity. 1 Publication
Mutagenesisi297 – 2971H → A: No effect on catalytic activity. 1 Publication
Mutagenesisi302 – 3021K → A: No effect on catalytic activity. 1 Publication
Mutagenesisi328 – 3281Y → A: No effect on catalytic activity. 1 Publication
Mutagenesisi344 – 3441E → A: No effect on catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 368349N-acetylneuraminate epimerasePRO_0000016655Add
BLAST

Proteomic databases

PaxDbiP39371.

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 interactions.
DIPiDIP-12628N.
STRINGi511145.b4310.

Structurei

Secondary structure

1
368
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 375Combined sources
Beta strandi40 – 445Combined sources
Helixi46 – 483Combined sources
Beta strandi52 – 565Combined sources
Beta strandi59 – 613Combined sources
Beta strandi64 – 663Combined sources
Beta strandi79 – 835Combined sources
Beta strandi86 – 905Combined sources
Beta strandi93 – 953Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi107 – 1115Combined sources
Turni112 – 1154Combined sources
Beta strandi116 – 1194Combined sources
Beta strandi132 – 1365Combined sources
Beta strandi139 – 1435Combined sources
Helixi148 – 16114Combined sources
Helixi165 – 17612Combined sources
Helixi180 – 1834Combined sources
Beta strandi188 – 1925Combined sources
Turni194 – 1963Combined sources
Beta strandi199 – 2046Combined sources
Beta strandi214 – 2185Combined sources
Beta strandi221 – 2255Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi238 – 2425Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi249 – 2524Combined sources
Turni258 – 2603Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi273 – 2775Combined sources
Helixi285 – 2906Combined sources
Turni296 – 2994Combined sources
Beta strandi307 – 3104Combined sources
Beta strandi317 – 3215Combined sources
Beta strandi327 – 3348Combined sources
Beta strandi337 – 3448Combined sources
Helixi346 – 3483Combined sources
Beta strandi350 – 3589Combined sources
Beta strandi365 – 3673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2UVKX-ray1.50A/B20-368[»]
ProteinModelPortaliP39371.
SMRiP39371. Positions 20-368.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP39371.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati40 – 8445Kelch 1Add
BLAST
Repeati86 – 13752Kelch 2Add
BLAST
Repeati139 – 17335Kelch 3Add
BLAST
Repeati174 – 21946Kelch 4Add
BLAST
Repeati222 – 26544Kelch 5Add
BLAST
Repeati287 – 33650Kelch 6Add
BLAST
Repeati338 – 36730Kelch 7Add
BLAST

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
EntryMethodResolution (Å)ChainPositionsPDBsum
2UVKX-ray1.50A/B20-368[»]
ProteinModelPortaliP39371.
SMRiP39371. Positions 20-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP39371.

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: September 7, 2016
This is version 117 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.