EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR001451 Bacterial transferase hexapeptide repeat

Protein matches Help

UniProtKB

Matches:

14765 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001451 Hexapep_transf

Type

Repeat

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00132	Hexapep	14765
Signatures in BioMart

InterPro Relationships Help

Found in

IPR005664 2,3,4,5-tetrahydropyridine-2-carboxylate N-succinyltransferase
IPR005881 Serine O-acetyltransferase
IPR005882 Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase
IPR007691 UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase
IPR010137 Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
IPR011004 Trimeric LpxA-like
IPR011974 Phenylacetic acid degradation protein PaaY
IPR012728 Non-ribosomal peptide synthetase C-terminal
IPR017156 Carbon dioxide concentrating mechanism protein, CcmM
IPR017694 Phosphonate metabolim protein, transferase hexapeptide repeat family
IPR019873 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-acetyltransferase
IPR019876 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase, gammaproteobacteria
IPR020019 Sialic acid O-acyltransferase, NeuD

Contains

IPR018357 Hexapeptide transferase, conserved site

GO Term annotation Help

Function

GO:0016740 transferase activity

InterPro annotation

Entry Details in BioMart

Abstract

A variety of bacterial transferases contain a repeat structure composed of tandem repeats of a [LIV]-G-X(4) hexapeptide, which, in the tertiary structure of LpxA (UDP N-acetylglucosamine acyltransferase) [1], has been shown to form a left-handed parallel beta helix. A number of different transferase protein families contain this repeat, such as galactoside acetyltransferase-like proteins [2], the gamma-class of carbonic anhydrases [3], and tetrahydrodipicolinate-N-succinlytransferases (DapD), the latter containing an extra N-terminal 3-helical domain [4].

Structural links Help

PDB - click here

SCOP: b.81.1.1 , b.81.1.2 , b.81.1.3 , b.81.1.4 , b.81.1.5 , b.81.1.6

CATH: 1.10.3130.10 , 2.160.10.10

Database links Help

PDBe-motif: PS00101

Enzyme: EC:2.3.1

PROSITE doc: PDOC00094

PANDIT: PF00132

Blocks: IPB001451

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001451

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A3QMC8 Mannose-1-phosphate guanyltransferase beta

P32501 Translation initiation factor eIF-2B subunit epsilon

Q13144 Translation initiation factor eIF-2B subunit epsilon

Q7JZB4 Mannose-1-phosphate guanyltransferase beta

Q8BTZ7 Mannose-1-phosphate guanyltransferase beta

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR003307	eIF4-gamma/eIF5/eIF2-epsilon
IPR018357	Hexapeptide transferase, conserved site
IPR001451	Bacterial transferase hexapeptide repeat
IPR005835	Nucleotidyl transferase
IPR011004	Trimeric LpxA-like
IPR016024	Armadillo-type fold
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Raetz CR, Roderick SL. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 270 997-1000 1995 [PubMed: 7481807] http://www.sciencemag.org/cgi/content/abstract/270/5238/997
2.	Wang XG, Olsen LR, Roderick SL. Structure of the lac operon galactoside acetyltransferase. Structure 10 581-8 2002 [PubMed: 11937062] http://dx.doi.org/10.1016/S0969-2126(02)00741-4
3.	Iverson TM, Alber BE, Kisker C, Ferry JG, Rees DC. A closer look at the active site of gamma-class carbonic anhydrases: high-resolution crystallographic studies of the carbonic anhydrase from Methanosarcina thermophila. Biochemistry 39 9222-31 2000 [PubMed: 10924115] http://dx.doi.org/10.1021/bi000204s
4.	Beaman TW, Vogel KW, Drueckhammer DG, Blanchard JS, Roderick SL. Acyl group specificity at the active site of tetrahydridipicolinate N-succinyltransferase. Protein Sci. 11 974-9 2002 [PubMed: 11910040] http://dx.doi.org/10.1110/ps.4310102

Additional Reading Open in usermanual
	Jeyakanthan J, Rangarajan S, Mridula P, Kanaujia SP, Shiro Y, Kuramitsu S, Yokoyama S, Sekar K. Observation of a calcium-binding site in the gamma-class carbonic anhydrase from Pyrococcus horikoshii. Acta Crystallogr. D Biol. Crystallogr. 64 2008 1012-9 [PubMed: 18931408] http://dx.doi.org/10.1107/S0907444908024323
	Williams AH, Raetz CR. Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase. Proc. Natl. Acad. Sci. U.S.A. 104 2007 13543-50 [PubMed: 17698807] http://dx.doi.org/10.1073/pnas.0705833104
	Nguyen L, Kozlov G, Gehring K. Structure of Escherichia coli tetrahydrodipicolinate N-succinyltransferase reveals the role of a conserved C-terminal helix in cooperative substrate binding. FEBS Lett. 582 2008 623-6 [PubMed: 18242192] http://dx.doi.org/10.1016/j.febslet.2008.01.032
	Olsen LR, Vetting MW, Roderick SL. Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Protein Sci. 16 2007 1230-5 [PubMed: 17473010] http://dx.doi.org/10.1110/ps.072779707
	Mochalkin I, Lightle S, Narasimhan L, Bornemeier D, Melnick M, Vanderroest S, McDowell L. Structure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding site. Protein Sci. 17 2008 577-82 [PubMed: 18218712] http://dx.doi.org/10.1110/ps.073271408

InterPro 23.1