NANE_ECOLI
ID NANE_ECOLI Reviewed; 229 AA.
AC P0A761; P45426; Q2M8Z0;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase;
DE EC=5.1.3.9;
DE AltName: Full=ManNAc-6-P epimerase;
GN Name=nanE; Synonyms=yhcJ; OrderedLocusNames=b3223, JW3192;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PUTATIVE FUNCTION.
RX PubMed=9864311; DOI=10.1128/jb.181.1.47-54.1999;
RA Plumbridge J., Vimr E.;
RT "Convergent pathways for utilization of the amino sugars N-
RT acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by
RT Escherichia coli.";
RL J. Bacteriol. 181:47-54(1999).
RN [4]
RP INDUCTION.
RX PubMed=23935044; DOI=10.1128/jb.00692-13;
RA Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT NanR.";
RL J. Bacteriol. 195:4689-4701(2013).
CC -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000305}.
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;
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC -!- INTERACTION:
CC P0A761; P06709: birA; NbExp=2; IntAct=EBI-561432, EBI-545740;
CC P0A761; P76316: dcyD; NbExp=2; IntAct=EBI-561432, EBI-562060;
CC -!- INDUCTION: Negatively regulated by the transcriptional repressor NanR.
CC Induced by N-acetylneuraminate, via inactivation of NanR.
CC {ECO:0000269|PubMed:23935044}.
CC -!- SIMILARITY: Belongs to the NanE family. {ECO:0000305}.
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DR EMBL; U18997; AAA58025.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76255.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77266.1; -; Genomic_DNA.
DR PIR; A65114; A65114.
DR RefSeq; NP_417690.1; NC_000913.3.
DR RefSeq; WP_000054239.1; NZ_STEB01000012.1.
DR AlphaFoldDB; P0A761; -.
DR SMR; P0A761; -.
DR BioGRID; 4261228; 117.
DR DIP; DIP-48021N; -.
DR IntAct; P0A761; 8.
DR STRING; 511145.b3223; -.
DR jPOST; P0A761; -.
DR PaxDb; P0A761; -.
DR PRIDE; P0A761; -.
DR EnsemblBacteria; AAC76255; AAC76255; b3223.
DR EnsemblBacteria; BAE77266; BAE77266; BAE77266.
DR GeneID; 66672881; -.
DR GeneID; 947745; -.
DR KEGG; ecj:JW3192; -.
DR KEGG; eco:b3223; -.
DR PATRIC; fig|1411691.4.peg.3505; -.
DR EchoBASE; EB2667; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_0_0_6; -.
DR InParanoid; P0A761; -.
DR OMA; TRPMEIT; -.
DR PhylomeDB; P0A761; -.
DR BioCyc; EcoCyc:NANE-MON; -.
DR BioCyc; MetaCyc:NANE-MON; -.
DR UniPathway; UPA00629; UER00682.
DR PRO; PR:P0A761; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; NAS:EcoCyc.
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:0006053; P:N-acetylmannosamine catabolic process; IMP:EcoCyc.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IMP:EcoCyc.
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 PANTHER; PTHR36204; PTHR36204; 1.
DR Pfam; PF04131; NanE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..229
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179770"
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
