ID NANE_ECO45 Reviewed; 229 AA.
AC B7MBY5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 02-OCT-2024, entry version 74.
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=ECS88_3600;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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}.
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DR EMBL; CU928161; CAR04826.1; -; Genomic_DNA.
DR RefSeq; WP_000054239.1; NC_011742.1.
DR AlphaFoldDB; B7MBY5; -.
DR SMR; B7MBY5; -.
DR GeneID; 75206073; -.
DR KEGG; ecz:ECS88_3600; -.
DR HOGENOM; CLU_086300_0_0_6; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000747; 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:InterPro.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd04729; NanE; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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; N-ACETYLMANNOSAMINE-6-PHOSPHATE 2-EPIMERASE-RELATED; 1.
DR PANTHER; PTHR36204:SF1; N-ACETYLMANNOSAMINE-6-PHOSPHATE 2-EPIMERASE-RELATED; 1.
DR Pfam; PF04131; NanE; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..229
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_1000139703"
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
//
