NANEK_BRUSU
ID NANEK_BRUSU Reviewed; 525 AA.
AC Q8FWN5; G0KCE9;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Bifunctional enzyme NanE/NanK;
DE Includes:
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase;
DE EC=5.1.3.9;
DE AltName: Full=ManNAc-6-P epimerase;
DE Includes:
DE RecName: Full=N-acetylmannosamine kinase;
DE EC=2.7.1.60;
DE AltName: Full=ManNAc kinase;
DE AltName: Full=N-acetyl-D-mannosamine kinase;
GN Name=nanEK; OrderedLocusNames=BRA0411, BS1330_II0408;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
CC -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000305}.
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc)
CC to ManNAc-6-P. {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine
CC 6-phosphate + H(+); Xref=Rhea:RHEA:23832, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16062, ChEBI:CHEBI:30616, ChEBI:CHEBI:57666,
CC ChEBI:CHEBI:456216; EC=2.7.1.60;
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 2/5.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC -!- SIMILARITY: In the N-terminal section; belongs to the NanE family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ROK (NagC/XylR)
CC family. NanK subfamily. {ECO:0000305}.
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DR EMBL; AE014292; AAN33608.1; -; Genomic_DNA.
DR EMBL; CP002998; AEM19887.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FWN5; -.
DR SMR; Q8FWN5; -.
DR EnsemblBacteria; AEM19887; AEM19887; BS1330_II0408.
DR KEGG; bms:BRA0411; -.
DR KEGG; bsi:BS1330_II0408; -.
DR HOGENOM; CLU_536235_0_0_5; -.
DR OMA; DCTRRER; -.
DR UniPathway; UPA00629; UER00681.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000007104; Chromosome II.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009385; F:N-acylmannosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
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; IPR043129; ATPase_NBD.
DR InterPro; IPR007260; NanE.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR36204; PTHR36204; 1.
DR Pfam; PF04131; NanE; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 3: Inferred from homology;
KW ATP-binding; Carbohydrate metabolism; Isomerase; Kinase;
KW Multifunctional enzyme; Nucleotide-binding; Transferase.
FT CHAIN 1..525
FT /note="Bifunctional enzyme NanE/NanK"
FT /id="PRO_0000179824"
FT REGION 1..241
FT /note="ManNAc-6-P epimerase"
FT REGION 242..525
FT /note="ManNAc kinase"
FT BINDING 246..253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 372..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 525 AA; 53867 MW; D403CAE499AB9486 CRC64;
MRGSPRNLCR VQGMIEEIVN RLRGKLIVSC QPVPESPFDN VASVVAYARA AEASGASGLR
IEGAANVAAT AQASTLPVIG LIKRDLDDSP VRITPFLEDV AALCDAGAAI VAVDATDRRR
PVPAAELIGE IKRRGRIAMA DISTLAEARN ALAAGADIIG TTMSGYTGEG PTPKDPDLDL
VAHCSRLGSF LIAEGRYNSP QQAGEAIRAG ADAVVVGSAI TRPEHITGWF RDAVESAAKP
SSPVLAFDIG GTKTLAALVR GREILERRVM TTPASVGSES WIGAIASLSA DWQGRYQRAA
IAVTGRVDGE IWSSLNPETL AIPPDYPLGR RMGAALGAPV EVINDAQAAA WGENRFGAAR
GRDMVFLTIS SGIGGGIVLG GRLIRGARGI AGSLGQVLVA GPSGFVRLET LASGFGIAKM
ALEAGHAGDA RSVFSAAAAG EGWARRILLD AASQLAAAVA GLQAIVDPEC IVIGGGVGMA
DGFLDMLREA LGSHSAVMRP DIVAAELGAD AGIIGVADLA ATYFS
