ID   NANE_STAA8              Reviewed;         222 AA.
AC   Q2G157;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
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=SAOUHSC_00298;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; CP000253; ABD29467.1; -; Genomic_DNA.
DR   RefSeq; WP_000936720.1; NZ_LS483365.1.
DR   RefSeq; YP_498888.1; NC_007795.1.
DR   PDB; 6VVA; X-ray; 1.84 A; A/B=1-222.
DR   PDBsum; 6VVA; -.
DR   AlphaFoldDB; Q2G157; -.
DR   SMR; Q2G157; -.
DR   STRING; 1280.SAXN108_0302; -.
DR   EnsemblBacteria; ABD29467; ABD29467; SAOUHSC_00298.
DR   GeneID; 3919525; -.
DR   KEGG; sao:SAOUHSC_00298; -.
DR   PATRIC; fig|93061.5.peg.271; -.
DR   eggNOG; COG3010; Bacteria.
DR   HOGENOM; CLU_086300_1_0_9; -.
DR   OMA; TRPMEIT; -.
DR   UniPathway; UPA00629; UER00682.
DR   PRO; PR:Q2G157; -.
DR   Proteomes; UP000008816; Chromosome.
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..222
FT                   /note="Putative N-acetylmannosamine-6-phosphate 2-
FT                   epimerase"
FT                   /id="PRO_0000301485"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           21..34
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          37..43
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           77..86
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          89..94
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           105..115
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          119..124
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           128..136
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          140..143
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   TURN            145..148
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           160..172
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          175..181
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           186..195
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           204..207
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   HELIX           209..218
FT                   /evidence="ECO:0007829|PDB:6VVA"
FT   TURN            219..221
FT                   /evidence="ECO:0007829|PDB:6VVA"
SQ   SEQUENCE   222 AA;  24545 MW;  7417D8DD1A48A041 CRC64;
     MLPHGLIVSC QALPDEPLHS SFIMSKMALA AYEGGAVGIR ANTKEDILAI KETVDLPVIG
     IVKRDYDHSD VFITATSKEV DELIESQCEV IALDATLQQR PKETLDELVS YIRTHAPNVE
     IMADIATVEE AKNAARLGFD YIGTTLHGYT SYTQGQLLYQ NDFQFLKDVL QSVDAKVIAE
     GNVITPDMYK RVMDLGVHCS VVGGAITRPK EITKRFVQIM ED