Q8FWN5 (NANEK_BRUSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional enzyme NanE/NanK

Including the following 2 domains:

1. Putative N-acetylmannosamine-6-phosphate 2-epimerase
   EC=5.1.3.9
   Alternative name(s):
   ManNAc-6-P epimerase
2. N-acetylmannosamine kinase
   EC=2.7.1.60
   Alternative name(s):
   ManNAc kinase
   N-acetyl-D-mannosamine kinase

Gene names

Name:	nanEK
Ordered Locus Names:	BRA0411, BS1330_II0408

Organism

Brucella suis biovar 1 (strain 1330) [Complete proteome] [HAMAP]

Taxonomic identifier

204722 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella › Brucella suis

Protein attributes

Sequence length	525 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P) Potential. HAMAP-Rule MF_01234 Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P By similarity. HAMAP-Rule MF_01234
Catalytic activity	N-acyl-D-glucosamine 6-phosphate = N-acyl-D-mannosamine 6-phosphate. HAMAP-Rule MF_01234 ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate. HAMAP-Rule MF_01234
Pathway	Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 2/5. HAMAP-Rule MF_01234 Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 3/5.
Sequence similarities	In the N-terminal section; belongs to the NanE family. In the C-terminal section; belongs to the ROK (NagC/XylR) family. NanK subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Isomerase Kinase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological_process	N-acetylmannosamine metabolic process Inferred from electronic annotation. Source: InterPro N-acetylneuraminate catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acylglucosamine-6-phosphate 2-epimerase activity Inferred from electronic annotation. Source: EC N-acylmannosamine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 525	525	Bifunctional enzyme NanE/NanK HAMAP-Rule MF_01234		PRO_0000179824
Regions
	Nucleotide binding	246 – 253	8	ATP Potential
	Nucleotide binding	372 – 379	8	ATP Potential
	Region	1 – 241	241	ManNAc-6-P epimerase HAMAP-Rule MF_01234
	Region	242 – 525	284	ManNAc kinase HAMAP-Rule MF_01234

Sequences

	Sequence		Length	Mass (Da)
	Q8FWN5 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: D403CAE499AB9486	FASTA	525	53,867
	10 20 30 40 50 60 MRGSPRNLCR VQGMIEEIVN RLRGKLIVSC QPVPESPFDN VASVVAYARA AEASGASGLR 70 80 90 100 110 120 IEGAANVAAT AQASTLPVIG LIKRDLDDSP VRITPFLEDV AALCDAGAAI VAVDATDRRR 130 140 150 160 170 180 PVPAAELIGE IKRRGRIAMA DISTLAEARN ALAAGADIIG TTMSGYTGEG PTPKDPDLDL 190 200 210 220 230 240 VAHCSRLGSF LIAEGRYNSP QQAGEAIRAG ADAVVVGSAI TRPEHITGWF RDAVESAAKP 250 260 270 280 290 300 SSPVLAFDIG GTKTLAALVR GREILERRVM TTPASVGSES WIGAIASLSA DWQGRYQRAA 310 320 330 340 350 360 IAVTGRVDGE IWSSLNPETL AIPPDYPLGR RMGAALGAPV EVINDAQAAA WGENRFGAAR 370 380 390 400 410 420 GRDMVFLTIS SGIGGGIVLG GRLIRGARGI AGSLGQVLVA GPSGFVRLET LASGFGIAKM 430 440 450 460 470 480 ALEAGHAGDA RSVFSAAAAG EGWARRILLD AASQLAAAVA GLQAIVDPEC IVIGGGVGMA 490 500 510 520 DGFLDMLREA LGSHSAVMRP DIVAAELGAD AGIIGVADLA ATYFS

References

[1]

"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts." Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M. , Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M. Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

[2]

"Revised genome sequence of Brucella suis 1330." Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R. J. Bacteriol. 193:6410-6410(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1330.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014292 Genomic DNA. Translation: AAN33608.1. CP002998 Genomic DNA. Translation: AEM19887.1.
RefSeq	NP_699603.1. NC_004311.2. YP_005614113.1. NC_017250.1.
3D structure databases
ProteinModelPortal	Q8FWN5.
ModBase	Search...
Protein-protein interaction databases
STRING	204722.BRA0411.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAN33608; AAN33608; BRA0411. AEM19887; AEM19887; BS1330_II0408.
GeneID	1164849. 12139843.
KEGG	bms:BRA0411. bsi:BS1330_II0408.
PATRIC	17793616. VBIBruSui107850_2624.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1940.
HOGENOM	HOG000289284.
KO	K13967.
OMA	REDIANC.
ProtClustDB	CLSK898967.
Enzyme and pathway databases
UniPathway	UPA00629; UER00681. UPA00629; UER00682.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_01234. ManNAc_kinase. Fused. MF_01235. ManNAc6P_epimer. Fused.
InterPro	IPR013785. Aldolase_TIM. IPR007260. NanE. IPR011060. RibuloseP-bd_barrel. IPR000600. ROK. [Graphical view]
Pfam	PF04131. NanE. 1 hit. PF00480. ROK. 1 hit. [Graphical view]
SUPFAM	SSF51366. RibP_bind_barrel. 1 hit.
PROSITE	PS01125. ROK. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NANEK_BRUSU

Accession

Primary (citable) accession number: Q8FWN5
Secondary accession number(s): G0KCE9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 28, 2003
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program