(data stored in ACNUC7421 zone)

SWISSPROT: NANE_EDWI9

ID   NANE_EDWI9              Reviewed;         235 AA.
AC   C5B754;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 49.
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=NT01EI_0599;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to
CC       N-acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000255|HAMAP-
CC       Rule:MF_01235}.
CC   -!- CATALYTIC ACTIVITY: N-acyl-D-glucosamine 6-phosphate = N-acyl-D-
CC       mannosamine 6-phosphate. {ECO:0000255|HAMAP-Rule:MF_01235}.
CC   -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation;
CC       D-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}.
DR   EMBL; CP001600; ACR67828.1; -; Genomic_DNA.
DR   RefSeq; WP_015870025.1; NC_012779.2.
DR   ProteinModelPortal; C5B754; -.
DR   SMR; C5B754; -.
DR   STRING; 634503.NT01EI_0599; -.
DR   EnsemblBacteria; ACR67828; ACR67828; NT01EI_0599.
DR   GeneID; 7960367; -.
DR   KEGG; eic:NT01EI_0599; -.
DR   PATRIC; fig|634503.3.peg.543; -.
DR   eggNOG; ENOG4105C9S; Bacteria.
DR   eggNOG; COG3010; LUCA.
DR   HOGENOM; HOG000236669; -.
DR   KO; K01788; -.
DR   OMA; IIGLWKR; -.
DR   OrthoDB; POG091H0GWT; -.
DR   UniPathway; UPA00629; UER00682.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:InterPro.
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   Pfam; PF04131; NanE; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B754.
DR   SWISS-2DPAGE; C5B754.
KW   Carbohydrate metabolism; Complete proteome; Isomerase;
KW   Reference proteome.
FT   CHAIN         1    235       Putative N-acetylmannosamine-6-phosphate
FT                                2-epimerase.
FT                                /FTId=PRO_1000214034.
SQ   SEQUENCE   235 AA;  25239 MW;  C726D2A2FA07B62F CRC64;
     MSVFTTLQQH IQRNGALIVS CQPVPGSPMD SPEIVAAMAT AAAQAGAAAL RIEGVANLQA
     VRPHVSLPII GIIKRDLDES PVRITPFLRD IDDLVQAGAD IIAFDGTQRP RPERREALLA
     RIQHHGRLAM ADCSSLEDGL YCQRLGCDFI GTTLSGYTHG ETPCEPDFAL VHALSNAGCR
     VIAEGRYNTP AQAAQALSQG AWAVTVGSAI TRIEHICQWY CQALQAEAHH EYAGH
//

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