3QNM

Haloalkane Dehalogenase Family Member from Bacteroides thetaiotaomicron of Unknown Function

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3qnma1	Alpha and beta proteins (a/b)	HAD-like	HAD-like	automated matches	automated matches	(Bacteroides thetaiotaomicron ) [TaxId: 818 ],	SCOPe (2.08)
A	d3qnma3	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Bacteroides thetaiotaomicron ) [TaxId: 818 ],	SCOPe (2.08)
A	d3qnma2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Bacteroides thetaiotaomicron ) [TaxId: 818 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	beta-Phosphoglucomutase-like	8088535	4002304	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	HAD-like	8088536	3001890	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	HAD_2	e3qnmA1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: HAD_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
A	1.10.150.240	Mainly Alpha	Orthogonal Bundle	DNA polymerase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00702	haloacid dehalogenase-like hydrolase (Hydrolase)	haloacid dehalogenase-like hydrolase	This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted fo ...	This family is structurally different from the alpha/beta hydrolase family (Pfam:PF00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain [1]. Those members with the characteristic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Haloacid dehalogenase-like hydrolase	phosphoric ester hydrolase activity nucleotidase activity hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity 5'-nucleotidase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR052550	Pyrimidine 5'-nucleotidase YjjG	Family
A	IPR036412	HAD-like superfamily	Homologous Superfamily
A	IPR023214	HAD superfamily	Homologous Superfamily
A	IPR006439	HAD hydrolase, subfamily IA	Family
A	IPR011951	HAD-superfamily hydrolase, subfamily IA, YjjG/PynA	Family
A	IPR023198	Phosphoglycolate phosphatase-like, domain 2	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.