ID NANE_CORGL Reviewed; 232 AA.
AC Q8NMD0;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 02-OCT-2024, entry version 113.
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};
GN OrderedLocusNames=Cgl2648, cg2933;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC
OS 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 /
OS 534).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG
RC 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG
RC 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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; BA000036; BAC00042.1; -; Genomic_DNA.
DR EMBL; BX927155; CAF21310.1; -; Genomic_DNA.
DR RefSeq; NP_601848.1; NC_003450.3.
DR RefSeq; WP_011015278.1; NC_006958.1.
DR AlphaFoldDB; Q8NMD0; -.
DR SMR; Q8NMD0; -.
DR STRING; 196627.cg2933; -.
DR KEGG; cgb:cg2933; -.
DR KEGG; cgl:Cgl2648; -.
DR PATRIC; fig|196627.13.peg.2585; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_1_0_11; -.
DR OrthoDB; 9781704at2; -.
DR BioCyc; CORYNE:G18NG-12265-MONOMER; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000582; Chromosome.
DR Proteomes; UP000001009; 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..232
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179769"
SQ SEQUENCE 232 AA; 24361 MW; C5A30E4ECB149FE8 CRC64;
MDLNTQRSKL YAQLQGQLIV SVQAPDGHAM RDTHTLTHVA AACVDGGAPA IRCGGYGGLE
DIRSISNRVD VPVFGLTKEG SEGVYITPTR DSVRAVAESG ATVVCADATF RPRPDGSTFA
ELVTVAHDSG ILIMADCATP EEVLSAHKAG ADFVSTTLAG YTEHREKTVG PDFDCLREAR
ELVPDAFLIG EGRFSNPADV AHGRLIGANA IIVGTAITDP GFITGQFASL LH
//
