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InterPro: IPR005932 Delta-1-pyrroline-5-carboxylate dehydrogenase 2

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UniProtKB

Matches:

222 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR005932 d-1-pyrroline-5-COlate_DH-2

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01237	D1pyr5carbox2	222
Signatures in BioMart

InterPro Relationships Help

Contains

IPR015590 Aldehyde dehydrogenase
IPR016162 Aldehyde dehydrogenase, N-terminal

GO Term annotation Help

Process

GO:0006561 proline biosynthetic process
GO:0055114 oxidation reduction

Function

GO:0003842 1-pyrroline-5-carboxylate dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

The delta(1)-pyrroline-5-carboxylate synthetase (EC:1.5.1.12) a mitochondrial inner membrane, ATP- and NADPH-dependent, bifunctional enzyme, catalyzes the reduction of glutamate to delta1-pyrroline-5-carboxylate, a critical step in the de novo biosynthesis of proline and ornithine. It is the rate-limiting enzyme in proline biosynthesis and is subject to feedback inhibition by proline.

1-pyrroline-5-carboxylate + NAD+ + H2O = L-glutamate + NADH

This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase.

Structural links Help

PDB - click here

SCOP: c.82.1.1

CATH: 3.40.309.10 , 3.40.605.10

Database links Help

Enzyme: EC:1.5.1.12

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005932

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A0R909 1-pyrroline-5-carboxylate dehydrogenase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR015590	Aldehyde dehydrogenase
IPR005932	Delta-1-pyrroline-5-carboxylate dehydrogenase 2
IPR016162	Aldehyde dehydrogenase, N-terminal
IPR016161	Aldehyde/histidinol dehydrogenase
IPR016160	Aldehyde dehydrogenase, conserved site
	SWISS-MODEL
	ModBase

Publications Help

Additional Reading Open in usermanual
	Inagaki E, Ohshima N, Takahashi H, Kuroishi C, Yokoyama S, Tahirov TH. Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase. J. Mol. Biol. 362 2006 490-501 [PubMed: 16934832] http://dx.doi.org/10.1016/j.jmb.2006.07.048
	Inagaki E, Ohshima N, Sakamoto K, Babayeva ND, Kato H, Yokoyama S, Tahirov TH. New insights into the binding mode of coenzymes: structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase complexed with NADP+. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 462-5 [PubMed: 17554163]

InterPro 23.1