NANEK_BRUME
ID NANEK_BRUME Reviewed; 518 AA.
AC Q8YBP2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=BMEII0857;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; AE008918; AAL54099.1; -; Genomic_DNA.
DR PIR; AH3616; AH3616.
DR AlphaFoldDB; Q8YBP2; -.
DR SMR; Q8YBP2; -.
DR STRING; 224914.BMEII0857; -.
DR EnsemblBacteria; AAL54099; AAL54099; BMEII0857.
DR KEGG; bme:BMEII0857; -.
DR eggNOG; COG1940; Bacteria.
DR eggNOG; COG3010; Bacteria.
DR OMA; DCTRRER; -.
DR UniPathway; UPA00629; UER00681.
DR UniPathway; UPA00629; UER00682.
DR Proteomes; UP000000419; 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..518
FT /note="Bifunctional enzyme NanE/NanK"
FT /id="PRO_0000179823"
FT REGION 1..234
FT /note="ManNAc-6-P epimerase"
FT REGION 235..518
FT /note="ManNAc kinase"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 365..372
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 518 AA; 53106 MW; E6A11DCCD032100D CRC64;
MCRVQGMIEE IVNRLRGKLI VSCQPVPESP FDNVASVVAY ARAAEASGAS GLRIEGAANV
AAAAQASTLP VIGLIKRDLD DSPVRITPFL EDVAALCDAG AAIVAVDATD RRRPVPAAEL
IGEIKRRGRI AMADISTLAE ARNALAAGAD IIGTTMSGYT GEGPTPKDPD LDLVAHCSRL
GSFLIAEGRY NSPQQAGEAI RAGADAVVVG SAITRPEHIT GWFRDAVESA AKPSSPVLAF
DIGGTKTLAA LVRGREILER RVMTTPASVG SESWIGAIAS LSADWQGRYQ RAAIAVTGRV
DGEIWSSLNP ETLAIPPDYP LGRRMGAALG APVEVINDAQ AAAWGEYRFG AARGRDMVFL
TISSGIGGGI VLGGRLIRGA RGIAGSLGQV LVAGPSGFVR LETLASGFGI AKMALEAGHA
GDARSVFSAA AAGEGWARRI LLDAASQLAA AVAGLQAIVD PECIVIGGGV GMADGFLDML
REALGSHSAV MRPDIVAAEL GADAGIIGVA DLAATYFS
