NANE_ECOL6
ID NANE_ECOL6 Reviewed; 229 AA.
AC P0A762; P45426;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase;
DE EC=5.1.3.9;
DE AltName: Full=ManNAc-6-P epimerase;
GN Name=nanE; OrderedLocusNames=c3977;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000305}.
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;
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC -!- SIMILARITY: Belongs to the NanE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN82417.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN82417.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000054239.1; NC_004431.1.
DR AlphaFoldDB; P0A762; -.
DR SMR; P0A762; -.
DR STRING; 199310.c3977; -.
DR EnsemblBacteria; AAN82417; AAN82417; c3977.
DR GeneID; 66672881; -.
DR KEGG; ecc:c3977; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_0_0_6; -.
DR OMA; TRPMEIT; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000001410; 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.
FT CHAIN 1..229
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179772"
SQ SEQUENCE 229 AA; 24074 MW; AB6CB3F36FEC0825 CRC64;
MSLLAQLDQK IAANGGLIVS CQPVPDSPLD KPEIVAAMAL AAEQAGAVAI RIEGVANLQA
TRAVVSVPII GIVKRDLEDS PVRITAYIED VDALAQAGAD IIAIDGTDRP RPVPVETLLA
RIHHHGLLAM TDCSTPEDGL ACQKLGAEII GTTLSGYTTP ETPEEPDLAL VKTLSDAGCR
VIAEGRYNTP AQAADAMRHG AWAVTVGSAI TRLEHICQWY NTAMKKAVL