Q53U11 (NEOK_STRFR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase
EC=2.4.1.285

Alternative name(s):
Neomycin biosynthesis protein 15
Short name=Neo-15
Neomycin biosynthesis protein K

Gene names

Name:	neoK
Synonyms:	neo15, neoF

Organism

Streptomyces fradiae (Streptomyces roseoflavus)

Taxonomic identifier

1906 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	366 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Glycosyltransferase involved in the biosynthesis of neomycin by mediating glycosylation of ribostamycin with UDP-GlcNAc as a sugar donor to generate 2'''-acetyl-6'''-hydroxyneomycin C. Ref.4
Catalytic activity	UDP-N-acetyl-alpha-D-glucosamine + ribostamycin = UDP + 2'''-acetyl-6'''-hydroxyneomycin C. Ref.4
Cofactor	Divalent cation. Ref.4
Pathway	Antibiotic biosynthesis; neomycin biosynthesis. Ref.4
Sequence similarities	Belongs to the glycosyltransferase group 1 family. Glycosyltransferase 4 subfamily.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Molecular function	Glycosyltransferase Transferase
Gene Ontology (GO)
Biological_process	neomycin biosynthetic process Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	transferase activity, transferring hexosyl groups Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 366	366	UDP-GlcNAc:ribostamycin N-acetylglucosaminyltransferase		PRO_0000421743
Experimental info
	Sequence conflict	174	1	D → H in CAH58698. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q53U11 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: C527A6FCA4F253CF	FASTA	366	39,257
	10 20 30 40 50 60 MAEAPAGRAL FEIYDEGFDS PSWGGVETAL WHLSRSLREA GTEAEFYRSS EGADLDALAA 70 80 90 100 110 120 RVERDRVDAV FPLVESDLFE GAAWRRLPAL HARTVRVWHD VSRLSADLSA PPPCPVHARV 130 140 150 160 170 180 PALPGAPVAE GCPARGAHPE GPMREVFLGE WPWTRCFPRR SVIPWAADHV PAKDLCDPSG 190 200 210 220 230 240 PVVLQLGKID TVDAERCLRR LTGAGVALRV VFATWSRRGR EARELVRAHQ GAGRRVEVLD 250 260 270 280 290 300 AYDIRTDWER VFGGASLFLL PSVFHETYNF AAAEAVQLGV PVAALGEGGN LPRFASLTAP 310 320 330 340 350 360 TPDALVDRLL AGGGAVAPRP RPAAGWRDVA ARYAEVIREH PAAGAGPAVP AGAGEGRGGR EEEHGG

References

[1]	"Biosynthesis of 2-deoxystreptamine by three crucial enzymes in Streptomyces fradiae NBRC 12773." Kudo F., Yamamoto Y., Yokoyama K., Eguchi T., Kakinuma K. J. Antibiot. 58:766-774(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB 8233 / NRRL B-1195 / VKM Ac-150.
[2]	"The neomycin biosynthetic gene cluster of Streptomyces fradiae NCIMB 8233: characterisation of an aminotransferase involved in the formation of 2-deoxystreptamine." Huang F., Haydock S.F., Mironenko T., Spiteller D., Li Y., Spencer J.B. Org. Biomol. Chem. 3:1410-1418(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB 8233 / NRRL B-1195 / VKM Ac-150.
[3]	"Analysis and comparison of biosynthetic gene clusters for the 2-deoxy-inosamine containing aminoglycoside antibiotics ribostamycin, neomycin, lividomycin, paromomycin and butirosin." Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Piepersberg W., Welzel K., Vente A. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 10745 / CBS 498.68 / DSM 40063 / JCM 4133 / NBRC 12773 / NCIMB 8233 / NRRL B-1195 / VKM Ac-150.
[4]	"Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis." Yokoyama K., Yamamoto Y., Kudo F., Eguchi T. ChemBioChem 9:865-869(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB211959 Genomic DNA. Translation: BAD95828.1. AJ843080 Genomic DNA. Translation: CAH58698.1. AJ629247 Genomic DNA. Translation: CAF33320.1.
3D structure databases
ProteinModelPortal	Q53U11.
ModBase	Search...
Protein family/group databases
CAZy	GT4. Glycosyltransferase Family 4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-17261.
UniPathway	UPA00969.
Family and domain databases
ProtoNet	Search...

Entry information

Entry name

NEOK_STRFR

Accession

Primary (citable) accession number: Q53U11
Secondary accession number(s): Q4W2N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 6, 2013
Last sequence update:	May 24, 2005
Last modified:	April 3, 2013
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program