1HZZ

THE ASYMMETRIC COMPLEX OF THE TWO NUCLEOTIDE-BINDING COMPONENTS (DI, DIII) OF PROTON-TRANSLOCATING TRANSHYDROGENASE

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1hzza1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Formate/glycerate dehydrogenases, NAD-domain	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
A	d1hzza2	Alpha and beta proteins (a/b)	Flavodoxin-like	Formate/glycerate dehydrogenase catalytic domain-like	L-alanine dehydrogenase-like	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
B	d1hzzb1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Formate/glycerate dehydrogenases, NAD-domain	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
B	d1hzzb2	Alpha and beta proteins (a/b)	Flavodoxin-like	Formate/glycerate dehydrogenase catalytic domain-like	L-alanine dehydrogenase-like	Nicotinamide nucleotide transhydrogenase dI component	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)
C	d1hzzc_	Alpha and beta proteins (a/b)	DHS-like NAD/FAD-binding domain	DHS-like NAD/FAD-binding domain	Transhydrogenase domain III (dIII)	Transhydrogenase domain III (dIII)	(Rhodospirillum rubrum ) [TaxId: 1085 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	D-2-hydroxyacid dehydrogenase-like	8057721	3000044	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	D-2-hydroxyacid dehydrogenase-like	8057721	3000044	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	DHS-like NAD/FAD-binding domain	8039024	3001728	SCOP2B (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	PF01262	e1hzzA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF01262	ECOD (1.6)
A	PF05222	e1hzzA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: PF05222	ECOD (1.6)
B	PF01262	e1hzzB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: PF01262	ECOD (1.6)
B	PF05222	e1hzzB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: PF05222	ECOD (1.6)
C	PF02233	e1hzzC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: DHS-like NAD/FAD-binding domain	F: PF02233	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C	3.40.50.1220	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	TPP-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF05222	Alanine dehydrogenase/PNT, N-terminal domain (AlaDh_PNT_N)	Alanine dehydrogenase/PNT, N-terminal domain	This family now also contains the lysine 2-oxoglutarate reductases.	Domain
A, B	PF01262	Alanine dehydrogenase/PNT, C-terminal domain (AlaDh_PNT_C)	Alanine dehydrogenase/PNT, C-terminal domain	This family now also contains the lysine 2-oxoglutarate reductases.	Domain
C	PF02233	NAD(P) transhydrogenase beta subunit (PNTB)	NAD(P) transhydrogenase beta subunit	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTON-TRANSLOCATING NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT PNTAA	NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding NADH binding oxidoreductase activity NAD+ binding NAD binding binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding heterocyclic compound binding small molecule binding NADH binding oxidoreductase activity NAD(P)+ transhydrogenase (AB-specific) activity oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor NAD(P)+ transhydrogenase activity oxidoreductase activity, acting on NAD(P)H catalytic activity monoatomic cation transmembrane transporter activity proton transmembrane transporter activity inorganic molecular entity transmembrane transporter activity inorganic cation transmembrane transporter activity monoatomic ion transmembrane transporter activity transporter activity NAD(P)+ transhydrogenase (B-specific) activity transmembrane transporter activity protein binding protein dimerization activity	nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process organic cyclic compound metabolic process NADPH regeneration organophosphate metabolic process metabolic process cellular process	-
C	PROTON-TRANSLOCATING NICOTINAMIDE NUCLEOTIDE TRANSHYDROGENASE SUBUNIT PNTB	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding oxidoreductase activity NAD(P)+ transhydrogenase (AB-specific) activity oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor NAD(P)+ transhydrogenase activity oxidoreductase activity, acting on NAD(P)H binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding oxidoreductase activity NAD(P)+ transhydrogenase (AB-specific) activity oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor NAD(P)+ transhydrogenase activity oxidoreductase activity, acting on NAD(P)H catalytic activity	-	cell periphery plasma membrane membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR007886	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, N-terminal	Domain
A, B	IPR008142	Alanine dehydrogenase/NAD(P) transhydrogenase, conserved site-1	Conserved Site
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR008143	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, conserved site-2	Conserved Site
A, B	IPR007698	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain	Domain
C	IPR034300	NADP transhydrogenase beta-like domain	Domain
C	IPR029035	DHS-like NAD/FAD-binding domain superfamily	Homologous Superfamily
C	IPR012136	NADP transhydrogenase, beta subunit	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
B, C	NAD(P)+ transhydrogenase (AB-specific) M-CSA #116	Transhydrogenase, isolated from Rhodospirillum rubrum, is a transmembrane protein that catalyses the hydride transfer from NADH to NADP+. The driving force for this reaction is the movement of a proton down a proton electrochemical gradient, with one proton transfer per hydride transfer, from the periplasm to the cytoplasm. Domain I (located in the PDB file) binds NADH and contains the catalytic residues for the reaction. Domain II facilitates proton translocation and domain III binds NADP+. Proton transfer through domain II propagates a conformational change from domain II through domain III to domain I. These conformational changes are required to align the substrates correctly and so couples proton translocation to hydride transfer.	Defined by 6 residues: ARG:B-127GLN:B-132ASP:B-135SER:B-138TYR:B-235ASP:C-132 Some residues are not modelled and lack atomic coordinates. Visualization is not available. Some residues are not modelled and lack atomic coordinates. Structure Motif searching is not available. EC: 1.6.1.1 (PDB Primary Data)

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 R01GM133198.