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InterPro: IPR000304 Delta 1-pyrroline-5-carboxylate reductase

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UniProtKB

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2402 proteins

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

Accession

IPR000304 P5CR

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF000193	Pyrrol-5-carb_rd	2180
PROSITE pattern	PS00521	P5CR	1479
PANTHER	PTHR11645	P5CR	2386
TIGRFAMs	TIGR00112	proC	1978
Signatures in BioMart

InterPro Relationships Help

Parent

IPR004455 NADP oxidoreductase, coenzyme F420-dependent

Contains

IPR016040 NAD(P)-binding domain

GO Term annotation Help

Process

GO:0006561 proline biosynthetic process
GO:0055114 oxidation reduction

Function

GO:0004735 pyrroline-5-carboxylate reductase activity

InterPro annotation

Entry Details in BioMart

Abstract

Delta 1-pyrroline-5-carboxylate reductase (P5CR) (EC:1.5.1.2) [1, 2] is the enzyme that catalyzes the terminal step in the biosynthesis of proline from glutamate, the NAD(P) dependent oxidation of 1-pyrroline-5-carboxylate into proline.

Structural links Help

PDB - click here

SCOP: a.100.1.10 , c.2.1.6

Database links Help

PDBe-motif: PS00521

Enzyme: EC:1.5.1.2

PROSITE doc: PDOC00451

Blocks: IPB000304

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000304

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P32263 Pyrroline-5-carboxylate reductase

P32322 Pyrroline-5-carboxylate reductase 1, mitochondrial

P54904 Pyrroline-5-carboxylate reductase

Q20848 Putative pyrroline-5-carboxylate reductase

Q922Q4 Pyrroline-5-carboxylate reductase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR000304	Delta 1-pyrroline-5-carboxylate reductase
IPR016040	NAD(P)-binding domain
IPR004455	NADP oxidoreductase, coenzyme F420-dependent
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Delauney AJ, Verma DP. A soybean gene encoding delta 1-pyrroline-5-carboxylate reductase was isolated by functional complementation in Escherichia coli and is found to be osmoregulated. Mol. Gen. Genet. 221 299-305 1990 [PubMed: 2199815] http://dx.doi.org/10.1007/BF00259392
2.	Savioz A, Jeenes DJ, Kocher HP, Haas D. Comparison of proC and other housekeeping genes of Pseudomonas aeruginosa with their counterparts in Escherichia coli. Gene 86 107-11 1990 [PubMed: 2107123] http://dx.doi.org/10.1016/0378-1119(90)90121-7

Additional Reading Open in usermanual
	Belitsky BR, Brill J, Bremer E, Sonenshein AL. Multiple genes for the last step of proline biosynthesis in Bacillus subtilis. J. Bacteriol. 183 2001 4389-92 [PubMed: 11418582] http://dx.doi.org/10.1128/JB.183.14.4389-4392.2001
	Nocek B, Chang C, Li H, Lezondra L, Holzle D, Collart F, Joachimiak A. Crystal structures of delta1-pyrroline-5-carboxylate reductase from human pathogens Neisseria meningitides and Streptococcus pyogenes. J. Mol. Biol. 354 2005 91-106 [PubMed: 16233902] http://dx.doi.org/10.1016/j.jmb.2005.08.036

InterPro 23.1