NANE_CLOPE
ID NANE_CLOPE Reviewed; 221 AA.
AC Q8XNZ3; O05726; Q9S4L0;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
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; Synonyms=nanP; OrderedLocusNames=CPE0184;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=NCTC 8798 / Type A;
RX PubMed=10419949; DOI=10.1128/jb.181.15.4526-4532.1999;
RA Walters D.M., Stirewalt V.L., Melville S.B.;
RT "Cloning, sequence, and transcriptional regulation of the operon encoding a
RT putative N-acetylmannosamine-6-phosphate epimerase (nanE) and sialic acid
RT lyase (nanA) in Clostridium perfringens.";
RL J. Bacteriol. 181:4526-4532(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-221.
RC STRAIN=A99;
RX PubMed=9511987; DOI=10.1023/a:1018585920853;
RA Traving C., Roggentin P., Schauer R.;
RT "Cloning, sequencing and expression of the acetylneuraminate lyase gene
RT from Clostridium perfringens A99.";
RL Glycoconj. J. 14:821-830(1997).
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 -!- INDUCTION: By N-acetylneuraminate. {ECO:0000269|PubMed:10419949}.
CC -!- SIMILARITY: Belongs to the NanE family. {ECO:0000305}.
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DR EMBL; AF130859; AAD28762.1; -; Genomic_DNA.
DR EMBL; BA000016; BAB79890.1; -; Genomic_DNA.
DR EMBL; Y12876; CAA73374.1; -; Genomic_DNA.
DR RefSeq; WP_003452659.1; NC_003366.1.
DR PDB; 4UTU; X-ray; 1.45 A; A/B=1-220.
DR PDB; 4UTW; X-ray; 1.90 A; A/B/C/D=1-220.
DR PDBsum; 4UTU; -.
DR PDBsum; 4UTW; -.
DR AlphaFoldDB; Q8XNZ3; -.
DR SMR; Q8XNZ3; -.
DR STRING; 195102.gene:10489428; -.
DR EnsemblBacteria; BAB79890; BAB79890; BAB79890.
DR GeneID; 29572701; -.
DR KEGG; cpe:CPE0184; -.
DR HOGENOM; CLU_086300_1_0_9; -.
DR OMA; TRPMEIT; -.
DR BioCyc; MetaCyc:MON-18988; -.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000818; 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; Reference proteome.
FT CHAIN 1..221
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179768"
FT VARIANT 47..48
FT /note="VN -> ID (in strain: NCTC 8798)"
FT VARIANT 95
FT /note="A -> G (in strain: NCTC 8798)"
FT VARIANT 109
FT /note="V -> I (in strain: NCTC 8798)"
FT HELIX 1..5
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 130..138
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:4UTU"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:4UTU"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:4UTU"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:4UTU"
SQ SEQUENCE 221 AA; 24153 MW; 40147518E31660B4 CRC64;
MLDVVKGNLI VSCQALSDEP LHSSFIMGRM AIAAKQGGAA AIRAQGVNDI NEIKEVTKLP
IIGIIKRNYD DSEIYITPTM KEVDELLKTD CEMIALDATK RKRPNGENVK DLVDAIHAKG
RLAMADISTL EEGIEAEKLG FDCVSTTLSG YTPYSKQSNS VDFELLEELV KTVKIPVICE
GRINTPEELK KALDLGAYSA VVGGAITRPQ QITKRFTDIL K
