NANE_VIBCH
ID NANE_VIBCH Reviewed; 240 AA.
AC Q9KR62;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=VC_1781;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF94930.1; -; Genomic_DNA.
DR PIR; B82158; B82158.
DR RefSeq; NP_231416.1; NC_002505.1.
DR RefSeq; WP_001889711.1; NZ_LT906614.1.
DR PDB; 5ZJB; X-ray; 1.70 A; A/B=6-240.
DR PDB; 5ZJN; X-ray; 2.66 A; A/B=6-240.
DR PDB; 5ZJP; X-ray; 2.66 A; A/B=7-236.
DR PDBsum; 5ZJB; -.
DR PDBsum; 5ZJN; -.
DR PDBsum; 5ZJP; -.
DR AlphaFoldDB; Q9KR62; -.
DR SMR; Q9KR62; -.
DR STRING; 243277.VC_1781; -.
DR DNASU; 2613661; -.
DR EnsemblBacteria; AAF94930; AAF94930; VC_1781.
DR GeneID; 57740424; -.
DR KEGG; vch:VC_1781; -.
DR PATRIC; fig|243277.26.peg.1700; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_0_0_6; -.
DR OMA; TRPMEIT; -.
DR BioCyc; VCHO:VC1781-MON; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006053; P:N-acetylmannosamine catabolic process; IBA:GO_Central.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central.
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 3D-structure; Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..240
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179817"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 38..51
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 61..70
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:5ZJB"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:5ZJB"
FT STRAND 208..212
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:5ZJB"
FT HELIX 219..237
FT /evidence="ECO:0007829|PDB:5ZJB"
SQ SEQUENCE 240 AA; 25502 MW; 6059EC11476EA84F CRC64;
MRPVVRKNFL NIEELKRFLN GQTVVSIQPV TGSPLDKTDF IVAMAIAVEQ AGAKALRIEG
VNNVAAVSAA VTIPIIGIVK RDLPDSPIRI TPFVSDVDGL ANAGATVIAF DATDRTRPES
RERIAQAIKN TGCFAMADCS TFEDGLWANS QGVEIVGSTL SGYVGDIEPT VPDFQLVKAF
SEAGFFTMAE GRYNTPELAA KAIESGAVAV TVGSALTRLE VVTQWFNNAT QAAGERKCAH
