C9QRK9 (C9QRK9_ECOD1) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase HAMAP-Rule MF_00523
Short name=UDP-3-O-(3-OHC14)-GlcN N-acyltransferase HAMAP-Rule MF_00523
EC=2.3.1.191 HAMAP-Rule MF_00523

Gene names

Name:	lpxD HAMAP-Rule MF_00523 EMBL BAJ42028.1
Ordered Locus Names:	EcDH1_3424, ECDH1ME8569_0172 EMBL BAJ42028.1

Organism

Escherichia coli (strain ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1) [Complete proteome] [HAMAP] EMBL ACX41039.1

Taxonomic identifier

536056 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	341 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the N-acylation of UDP-3-O-(hydroxymyristoyl)glucosamine using 3-hydroxymyristoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell By similarity. HAMAP-Rule MF_00523
Catalytic activity	(3R)-3-hydroxymyristoyl-[acyl-carrier-protein] + UDP-3-O-((3R)-hydroxymyristoyl)-alpha-D-glucosamine = UDP-2,3-bis(O-(3R)-3-hydroxymyristoyl)-alpha-D-glucosamine + a holo-[acyl-carrier-protein]. HAMAP-Rule MF_00523
Pathway	Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 3/6. HAMAP-Rule MF_00523
Subunit structure	Homotrimer By similarity. HAMAP-Rule MF_00523 SAAS SAAS007691
Sequence similarities	Belongs to the transferase hexapeptide repeat family. LpxD subfamily. HAMAP-Rule MF_00523

Ontologies

Keywords
Biological process	Lipid A biosynthesis HAMAP-Rule MF_00523 SAAS SAAS007691 Lipid biosynthesis Lipid metabolism
Domain	Repeat HAMAP-Rule MF_00523 SAAS SAAS007691
Molecular function	Acyltransferase HAMAP-Rule MF_00523 SAAS SAAS007691 EMBL ACX41039.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP
Molecular_function	transferase activity, transferring acyl groups other than amino-acyl groups Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Sites
	Active site	239	1	Proton acceptor By similarity HAMAP-Rule MF_00523

Sequences

	Sequence		Length	Mass (Da)
	C9QRK9 [UniParc]. Last modified November 24, 2009. Version 1. Checksum: B0ADFED5B17C649D	FASTA	341	36,038
	10 20 30 40 50 60 MPSIRLADLA QQLDAELHGD GDIVITGVAS MQSAQTGHIT FMVNPKYREH LGLCQASAVV 70 80 90 100 110 120 MTQDDLPFAK SAALVVKNPY LTYARMAQIL DTTPQPAQNI APSAVIDATA KLGNNVSIGA 130 140 150 160 170 180 NAVIESGVEL GDNVIIGAGC FVGKNSKIGA GSRLWANVTI YHEIQIGQNC LIQSGTVVGA 190 200 210 220 230 240 DGFGYANDRG NWVKIPQIGR VIIGDRVEIG ACTTIDRGAL DDTIIGNGVI IDNQCQIAHN 250 260 270 280 290 300 VVIGDNTAVA GGVIMAGSLK IGRYCMIGGA SVINGHMEIC DKVTVTGMGM VMRPITEPGV 310 320 330 340 YSSGIPLQPN KVWRKTAALV MNIDDMSKRL KSLERKVNQQ D

References

[1]

"Complete sequence of Escherichia coli DH1." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Keasling J.D. Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1.

[2]

"Comparison of sequence reads obtained from three next-generation sequencing platforms." Suzuki S., Ono N., Furusawa C., Ying B.W., Yomo T. PLoS ONE 6:E19534-E19534(2011) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33849 / DSM 4235 / NCIB 12045 / K12 / DH1 and DH1 EMBL BAJ42028.1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001637 Genomic DNA. Translation: ACX41039.1. AP012030 Genomic DNA. Translation: BAJ42028.1.
RefSeq	YP_006093328.1. NC_017625.1. YP_006127573.1. NC_017638.1.
3D structure databases
SMR	C9QRK9. Positions 1-341.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ACX41039; ACX41039; EcDH1_3424. BAJ42028; BAJ42028; ECDH1ME8569_0172.
GeneID	12707058. 12873174.
KEGG	edh:EcDH1_3424. edj:ECDH1ME8569_0172.
PATRIC	36699361. VBIEscCol36761_3617.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HOG000294339.
KO	K02536.
OMA	SHAFKIP.
Enzyme and pathway databases
UniPathway	UPA00359; UER00479.
Family and domain databases
HAMAP	MF_00523. LpxD.
InterPro	IPR001451. Hexapep_transf. IPR018357. Hexapep_transf_CS. IPR011004. Trimer_LpxA-like. IPR007691. UDP-3-O_GlcNAc_AcTrfase. IPR020573. UDP_GlcNAc_AcTrfase_non-rep. [Graphical view]
Pfam	PF00132. Hexapep. 3 hits. PF04613. LpxD. 1 hit. [Graphical view]
SUPFAM	SSF51161. Trimer_LpxA_like. 1 hit.
TIGRFAMs	TIGR01853. lipid_A_lpxD. 1 hit.
PROSITE	PS00101. HEXAPEP_TRANSFERASES. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

C9QRK9_ECOD1

Accession

Primary (citable) accession number: C9QRK9

Entry history

Integrated into UniProtKB/TrEMBL:	November 24, 2009
Last sequence update:	November 24, 2009
Last modified:	May 1, 2013
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)