ID NANE_ACTP2 Reviewed; 229 AA.
AC A3N350;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 02-OCT-2024, entry version 93.
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=APL_1752;
OS Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=416269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L20;
RX PubMed=18065534; DOI=10.1128/jb.01845-07;
RA Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA Nash J.H.E.;
RT "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT (serotype 5b).";
RL J. Bacteriol. 190:1495-1496(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000569; ABN74836.1; -; Genomic_DNA.
DR RefSeq; WP_005599263.1; NC_009053.1.
DR AlphaFoldDB; A3N350; -.
DR SMR; A3N350; -.
DR STRING; 416269.APL_1752; -.
DR EnsemblBacteria; ABN74836; ABN74836; APL_1752.
DR GeneID; 69419045; -.
DR KEGG; apl:APL_1752; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_0_0_6; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000001432; 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_0000301465"
SQ SEQUENCE 229 AA; 24161 MW; 730650AE6B8C383D CRC64;
MSKLSHSEVL NTIRNGLIAS CQPVDDGPMD KPEIVAAMAQ ASLIGGAAGL RIEGVDNLKA
TRPTVKAPII AIVKRDLPDS PVRITPFLQD IDDLAAAGAD IIAVDGTDRV RPVTIEAALK
RIHELGCLAM ADCSTLAEGL YCQQLGFDIV GSTMSGYTGG EVPNEPDYQL VKDLKAAGCF
VMAEGRYNSP QLAKTAIEIG ADCVTVGSAL TRLEHIVGWF ADEIKTAKV
//
