NANE_LACLA
ID NANE_LACLA Reviewed; 231 AA.
AC Q9CGC2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
DE EC=5.1.3.9 {ECO:0000255|HAMAP-Rule:MF_01235};
DE AltName: Full=ManNAc-6-P epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
GN Name=nanE {ECO:0000255|HAMAP-Rule:MF_01235}; OrderedLocusNames=LL1175;
GN ORFNames=L191486;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
CC -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000255|HAMAP-
CC Rule:MF_01235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine
CC 6-phosphate; Xref=Rhea:RHEA:23932, ChEBI:CHEBI:57599,
CC ChEBI:CHEBI:57666; EC=5.1.3.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01235};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC {ECO:0000255|HAMAP-Rule:MF_01235}.
CC -!- SIMILARITY: Belongs to the NanE family. {ECO:0000255|HAMAP-
CC Rule:MF_01235}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK05273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE005176; AAK05273.1; ALT_INIT; Genomic_DNA.
DR PIR; G86771; G86771.
DR RefSeq; NP_267331.1; NC_002662.1.
DR RefSeq; WP_003130140.1; NC_002662.1.
DR AlphaFoldDB; Q9CGC2; -.
DR SMR; Q9CGC2; -.
DR STRING; 272623.L191486; -.
DR PaxDb; Q9CGC2; -.
DR EnsemblBacteria; AAK05273; AAK05273; L191486.
DR KEGG; lla:L191486; -.
DR PATRIC; fig|272623.7.peg.1259; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_1_0_9; -.
DR OMA; QALGFDC; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000002196; Chromosome.
DR GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0009385; F:N-acylmannosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04729; NanE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01235; ManNAc6P_epimer; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007260; NanE.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR36204; PTHR36204; 1.
DR Pfam; PF04131; NanE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..231
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179779"
SQ SEQUENCE 231 AA; 25463 MW; B9269E71E208C41B CRC64;
MKKEVFLDKV KNGIIVSCQA LPGEALYSEK GGIMPLMAKA AAQAGAVGIR ANSVRDIKEI
QKIVDLPIIG IIKRDYPPQK PFITATMKEI DELVATSCEV IALDCTSRER YDGLTINEFI
KSIKEKYPNQ LLMADCSTFE ECKNAYEAGV DFVGTTLSGY TDESPKQDEP DFTLLEKLVE
EKIPVIAEGR IHSPEQAKRV YDIGVDAMVI GGAITRPFEI ATRFIKAIGE K
