NANE2_STRPN
ID NANE2_STRPN Reviewed; 232 AA.
AC P65520; Q8DNU6; Q97PE4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase 2;
DE EC=5.1.3.9;
DE AltName: Full=ManNAc-6-P epimerase 2;
GN Name=nanE2; OrderedLocusNames=SP_1685;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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 -!- SIMILARITY: Belongs to the NanE family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005672; AAK75764.1; -; Genomic_DNA.
DR PIR; C95196; C95196.
DR RefSeq; WP_001135651.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P65520; -.
DR SMR; P65520; -.
DR STRING; 170187.SP_1685; -.
DR EnsemblBacteria; AAK75764; AAK75764; SP_1685.
DR GeneID; 60234421; -.
DR KEGG; spn:SP_1685; -.
DR eggNOG; COG3010; Bacteria.
DR OMA; QALGFDC; -.
DR PhylomeDB; P65520; -.
DR BioCyc; SPNE170187:G1FZB-1706-MON; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000585; 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:UniProtKB-UniRule.
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 PANTHER; PTHR36204; PTHR36204; 1.
DR Pfam; PF04131; NanE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Isomerase.
FT CHAIN 1..232
FT /note="Putative N-acetylmannosamine-6-phosphate 2-epimerase
FT 2"
FT /id="PRO_0000179806"
SQ SEQUENCE 232 AA; 25450 MW; 5AC19F57E6E5170A CRC64;
MPQISKEALI EQIKDGIIVS CQALPHEPLY TEAGGVIPLL VKAAEQGGAV GIRANSVRDI
KEIKEVTKLP IIGIIKRDYP PQEPFITATM KEVDELAELD IEVIALDCTK RERYDGLEIQ
EFIRQVKEKY PNQLLMADTS IFEEGLAAVE AGIDFVGTTL SGYTSYSPKV DGPDFELIKK
LCDAGVDVIA EGKIHTPEQA KQILEYGVRG IVVGGAITRP KEITERFVAS LK