NANE2_SALPA
ID NANE2_SALPA Reviewed; 229 AA.
AC Q5PLF1;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01235};
GN Name=nanE2 {ECO:0000255|HAMAP-Rule:MF_01235}; OrderedLocusNames=SPA3205;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV79029.1; -; Genomic_DNA.
DR RefSeq; WP_011233189.1; NC_006511.1.
DR AlphaFoldDB; Q5PLF1; -.
DR SMR; Q5PLF1; -.
DR EnsemblBacteria; AAV79029; AAV79029; SPA3205.
DR KEGG; spt:SPA3205; -.
DR HOGENOM; CLU_086300_0_0_6; -.
DR OMA; TRPMEIT; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000008185; 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..229
FT /note="Putative N-acetylmannosamine-6-phosphate 2-epimerase
FT 2"
FT /id="PRO_0000179792"
SQ SEQUENCE 229 AA; 23984 MW; D6EBC18AEB10DD78 CRC64;
MSLLEQLDKN IAASGGLIVS CQPVPGSPLD KPEIVAAMAL AAEQAGAVAV RIEGIDNLRV
ARSLVSVPII GIIKRDLDDS PVRITPFLDD VDALAQAGAA IIAVDGTARQ RPVAVEALLA
RIHHHHLLAM ADCSSVDDGL ACQRLGADII GTTMSGYTTP DTPEEPDLPL VKALHDAGCR
VIAEGRYNSP TLAAEAIRYG AWAVTVGSAI TRLEHICGWY NDALKKAAS
