NANE1_SALPA
ID NANE1_SALPA Reviewed; 226 AA.
AC Q5PG85;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase 1 {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 1 {ECO:0000255|HAMAP-Rule:MF_01235};
GN Name=nanE1 {ECO:0000255|HAMAP-Rule:MF_01235}; OrderedLocusNames=SPA1722;
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; AAV77643.1; -; Genomic_DNA.
DR RefSeq; WP_000054244.1; NC_006511.1.
DR AlphaFoldDB; Q5PG85; -.
DR SMR; Q5PG85; -.
DR EnsemblBacteria; AAV77643; AAV77643; SPA1722.
DR KEGG; spt:SPA1722; -.
DR HOGENOM; CLU_086300_0_0_6; -.
DR OMA; QALGFDC; -.
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..226
FT /note="Putative N-acetylmannosamine-6-phosphate 2-epimerase
FT 1"
FT /id="PRO_0000179791"
SQ SEQUENCE 226 AA; 24001 MW; 54687985086536CA CRC64;
MSLLARLEQS VHENGGLIVS CQPVPGSPMD KPEIVAAMAQ AAASAGAVAV RIEGIENLRT
VRPHLSVPII GIIKRDLTGS PVRITPYLQD VDALAQAGAD IIAFDASFRS RPVDIDSLLT
RIRLHGLLAM ADCSTVNEGI SCHQKGIEFI GTTLSGYTGP ITPVEPDLAM VTQLSHAGCR
VIAEGRYNTP ALAANAIEHG AWAVTVGSAI TRIEHICQWF SHAVRR
