NANE_SALTI
ID NANE_SALTI Reviewed; 226 AA.
AC P60668; Q8XG90;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase;
DE EC=5.1.3.9;
DE AltName: Full=ManNAc-6-P epimerase;
GN Name=nanE; OrderedLocusNames=STY1166, t1791;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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}.
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DR EMBL; AL513382; CAD08254.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO69413.1; -; Genomic_DNA.
DR RefSeq; NP_455624.1; NC_003198.1.
DR RefSeq; WP_000054243.1; NZ_WSUR01000018.1.
DR PDB; 3Q58; X-ray; 1.80 A; A/B=1-226.
DR PDBsum; 3Q58; -.
DR AlphaFoldDB; P60668; -.
DR SMR; P60668; -.
DR STRING; 220341.16502301; -.
DR EnsemblBacteria; AAO69413; AAO69413; t1791.
DR KEGG; stt:t1791; -.
DR KEGG; sty:STY1166; -.
DR PATRIC; fig|220341.7.peg.1166; -.
DR eggNOG; COG3010; Bacteria.
DR HOGENOM; CLU_086300_0_0_6; -.
DR OMA; TRPMEIT; -.
DR UniPathway; UPA00629; UER00682.
DR EvolutionaryTrace; P60668; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase.
FT CHAIN 1..226
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179793"
FT HELIX 1..14
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 17..20
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 32..44
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 115..124
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 136..144
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:3Q58"
FT TURN 153..156
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:3Q58"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 181..186
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 190..198
FT /evidence="ECO:0007829|PDB:3Q58"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 208..211
FT /evidence="ECO:0007829|PDB:3Q58"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:3Q58"
SQ SEQUENCE 226 AA; 23973 MW; 547F4985086536CA CRC64;
MSLLARLEQS VHENGGLIVS CQPVPGSPMD KPEIVAAMAQ AAASAGAVAV RIEGIENLRT
VRPHLSVPII GIIKRDLTGS PVRITPYLQD VDALAQAGAD IIAFDASFRS RPVDIDSLLT
RIRLHGLLAM ADCSTVNEGI SCHQKGIEFI GTTLSGYTGP ITPVEPDLAM VTQLSHAGCR
VIAEGRYNTP ALAANAIEHG AWAVTVGSAI TRIEHICQWF SHAVKR
