Pseudomonas aeruginosa PAO1, PA4417 (murE)

Gene Ontology

Ontology	Accession	Term	GO Evidence	Evidence Ontology (ECO) Code	Reference	Comments
Biological Process	GO:0008360	regulation of cell shape	ISM Inferred from Sequence Model Term mapped from: InterPro:TIGR01085	ECO:0000259 match to InterPro signature evidence used in automatic assertion
Molecular Function	GO:0005524	ATP binding	ISM Inferred from Sequence Model Term mapped from: InterPro:SSF53623	ECO:0000259 match to InterPro signature evidence used in automatic assertion
Biological Process	GO:0009058	biosynthetic process	ISM Inferred from Sequence Model Term mapped from: InterPro:SSF53623	ECO:0000259 match to InterPro signature evidence used in automatic assertion
Biological Process	GO:0051301	cell division	ISM Inferred from Sequence Model Term mapped from: InterPro:TIGR01085	ECO:0000259 match to InterPro signature evidence used in automatic assertion
Cellular Component	GO:0005737	cytoplasm	ISM Inferred from Sequence Model Term mapped from: InterPro:TIGR01085	ECO:0000259 match to InterPro signature evidence used in automatic assertion
Molecular Function	GO:0016881	acid-amino acid ligase activity	ISM Inferred from Sequence Model Term mapped from: InterPro:TIGR01085	ECO:0000259 match to InterPro signature evidence used in automatic assertion

Functional Classifications Manually Assigned by PseudoCAP

Cell wall / LPS / capsule Other PAO1 genes in this class

Pathways

Database	Xref	Pathway	Version	Evidence	PMID
PseudoCyc	PEP-LIPA-SYN-PWY	peptidoglycan and lipid A precursor biosynthesis	19.5	ECO:0000250 sequence similarity evidence used in manual assertion	12867747
KEGG	pae00550	Peptidoglycan biosynthesis	81.0+/01-23, Jan 17	ECO:0000249 sequence similarity evidence used in automatic assertion
PseudoCyc	PWY-6387	UDP-N-acetylmuramoyl-pentapeptide biosynthesis I (meso-DAP-containing)	19.5	ECO:0000250 sequence similarity evidence used in manual assertion	12867747
PseudoCAP		Peptideglycan biosynthesis		ECO:0000037 not_recorded
PseudoCyc	PEPTIDOGLYCANSYN-PWY	peptidoglycan biosynthesis I (meso-diaminopimelate containing)	19.5	ECO:0000250 sequence similarity evidence used in manual assertion	12867747
PseudoCyc	KDO-PEP-LIPASYN-PWY	KDO<SUB>2</SUB>-lipid A and peptidoglycan biosynthesis	19.5	ECO:0000250 sequence similarity evidence used in manual assertion	12867747
KEGG	pae00300	Lysine biosynthesis	81.0+/01-23, Jan 17	ECO:0000249 sequence similarity evidence used in automatic assertion

Functional Predictions from Interpro

Analysis	Accession	Description	Interpro Accession	Interpro Description	Amino Acid Start	Amino Acid Stop	E-value
PANTHER	PTHR23135	MUR LIGASE FAMILY MEMBER	-	-	3	482	0.0
Pfam	PF02875	Mur ligase family, glutamate ligase domain	IPR004101	Mur ligase, C-terminal	329	412	8.9E-23
Gene3D	G3DSA:3.40.1390.10	-	-	-	3	96	1.7E-23
SUPERFAMILY	SSF53623	MurD-like peptide ligases, catalytic domain	IPR036565	Mur-like, catalytic domain superfamily	97	326	6.41E-77
Gene3D	G3DSA:3.40.1190.10	-	IPR036565	Mur-like, catalytic domain superfamily	97	329	1.9E-63
Gene3D	G3DSA:3.90.190.20	-	IPR036615	Mur ligase, C-terminal domain superfamily	330	483	2.1E-57
Hamap	MF_00208	UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase [murE].	IPR005761	UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase	3	479	35.0854
NCBIfam	TIGR01085	JCVI: UDP-N-acetylmuramyl-tripeptide synthetase	IPR005761	UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase	17	479	0.0
Pfam	PF08245	Mur ligase middle domain	IPR013221	Mur ligase, central	106	306	2.6E-53
Pfam	PF01225	Mur ligase family, catalytic domain	IPR000713	Mur ligase, N-terminal catalytic domain	18	94	1.7E-10
SUPERFAMILY	SSF63418	MurE/MurF N-terminal domain	IPR035911	MurE/MurF, N-terminal	11	95	6.28E-21
SUPERFAMILY	SSF53244	MurD-like peptide ligases, peptide-binding domain	IPR036615	Mur ligase, C-terminal domain superfamily	329	480	1.45E-47

Search for additional functional domains at the NCBI CDD database website. Go to this protein's amino acid sequence and follow the link.