6JQN

Structure of PaaZ, a bifunctional enzyme in complex with NADP+ and OCoA

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	MaoC_dehydratas	e6jqnA3	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: MaoC_dehydratas	ECOD (1.6)
A	Aldedh_2nd	e6jqnA2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
A	Aldedh_1st_1	e6jqnA1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
C	MaoC_dehydratas	e6jqnC3	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: MaoC_dehydratas	ECOD (1.6)
C	Aldedh_2nd	e6jqnC2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
C	Aldedh_1st_1	e6jqnC1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
D	MaoC_dehydratas	e6jqnD3	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: MaoC_dehydratas	ECOD (1.6)
D	Aldedh_2nd	e6jqnD2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
D	Aldedh_1st_1	e6jqnD1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
B	MaoC_dehydratas	e6jqnB3	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: MaoC_dehydratas	ECOD (1.6)
B	Aldedh_2nd	e6jqnB2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
B	Aldedh_1st_1	e6jqnB1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
E	MaoC_dehydratas	e6jqnE3	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: MaoC_dehydratas	ECOD (1.6)
E	Aldedh_2nd	e6jqnE2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
E	Aldedh_1st_1	e6jqnE1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
F	MaoC_dehydratas	e6jqnF3	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: MaoC_dehydratas	ECOD (1.6)
F	Aldedh_2nd	e6jqnF2	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
F	Aldedh_1st_1	e6jqnF1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF00171	Aldehyde dehydrogenase family (Aldedh)	Aldehyde dehydrogenase family	-	Family
A, B, C, D, E A, B, C, D, E, F	PF01575	MaoC like domain (MaoC_dehydratas)	MaoC like domain	The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase [1]. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydroge ...	The maoC gene is part of a operon with maoA which is involved in the synthesis of monoamine oxidase [1]. The MaoC protein is found to share similarity with a wide variety of enzymes; estradiol 17 beta-dehydrogenase 4, peroxisomal hydratase-dehydrogenase-epimerase, fatty acid synthase beta subunit. Several bacterial proteins that are composed solely of this domain have (R)-specific enoyl-CoA hydratase activity [2]. This domain is also present in the NodN nodulation protein N.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	Bifunctional protein PaaZ	oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor hydrolase activity, acting on acid carbon-carbon bonds hydrolase activity hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances oxidoreductase activity, acting on CH or CH2 groups oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor enoyl-CoA hydratase activity hydro-lyase activity lyase activity carbon-oxygen lyase activity ether hydrolase activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor hydrolase activity, acting on acid carbon-carbon bonds hydrolase activity hydrolase activity, acting on acid carbon-carbon bonds, in ketonic substances oxidoreductase activity, acting on CH or CH2 groups oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor enoyl-CoA hydratase activity hydro-lyase activity lyase activity carbon-oxygen lyase activity ether hydrolase activity hydrolase activity, acting on ether bonds identical protein binding protein binding binding	cellular response to stimulus catabolic process response to stimulus oxoacid metabolic process organic acid catabolic process organic acid metabolic process response to xenobiotic stimulus cellular catabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process benzene-containing compound metabolic process cellular response to xenobiotic stimulus carboxylic acid metabolic process cellular response to stimulus catabolic process response to stimulus oxoacid metabolic process organic acid catabolic process organic acid metabolic process response to xenobiotic stimulus cellular catabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process small molecule metabolic process benzene-containing compound metabolic process cellular response to xenobiotic stimulus carboxylic acid metabolic process xenobiotic catabolic process xenobiotic metabolic process cellular response to chemical stimulus response to chemical phenylacetate catabolic process metabolic process cellular process monocarboxylic acid metabolic process small molecule catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR011966	Phenylacetic acid degradation protein PaaN	Family
A, B, C, D, E A, B, C, D, E, F	IPR015590	Aldehyde dehydrogenase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR016162	Aldehyde dehydrogenase, N-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR029069	HotDog domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR002539	MaoC-like dehydratase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR016163	Aldehyde dehydrogenase, C-terminal	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.