ID NANE_PASMU Reviewed; 228 AA.
AC Q9L6B4;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 02-OCT-2024, entry version 122.
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=PM1711;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10873488; DOI=10.1006/mpat.2000.0365;
RA Fuller T.E., Kennedy M.J., Lowery D.E.;
RT "Identification of Pasteurella multocida virulence genes in a septicemic
RT mouse model using signature-tagged mutagenesis.";
RL Microb. Pathog. 29:25-38(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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 ---------------------------------------------------------------------------
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; AF237924; AAF68410.1; -; Genomic_DNA.
DR EMBL; AE004439; AAK03795.1; -; Genomic_DNA.
DR RefSeq; WP_005724602.1; NC_002663.1.
DR AlphaFoldDB; Q9L6B4; -.
DR SMR; Q9L6B4; -.
DR STRING; 272843.PM1711; -.
DR EnsemblBacteria; AAK03795; AAK03795; PM1711.
DR GeneID; 77206632; -.
DR KEGG; pmu:PM1711; -.
DR HOGENOM; CLU_086300_0_0_6; -.
DR OrthoDB; 9810372at2; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000809; 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..228
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179788"
SQ SEQUENCE 228 AA; 24316 MW; 8B7EBFCB74F613A1 CRC64;
MSKLSHPQVL EQIKYGLIAS CQPVDNGPMD SPEIVAAMAQ ASVIGGAAGL RIEGIENLKA
TRNVVNVPII GIVKRDLPDS PVRISPFLQD IEELAAAGAD IIAFDGTDRV RPTTREAIIK
RIKELGCLAM ADCSNFEEGM YCHNLGVEII GSTMSGYTGG EIPAEPDYQL VKDLNAAGCR
VMAEGRYNTP ELAKTAIEIG AYSVTVGSAL TRLEHIVSWF ADAVKSAK
//
