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InterPro: IPR002872 Proline dehydrogenase

Protein matches Help

UniProtKB

Matches:

1322 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

IPR002872 Proline_DH

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01619	Pro_dh	1322
Signatures in BioMart

InterPro Relationships Help

Found in

IPR008219 Proline dehydrogenase, predicted
IPR015659 Proline oxidase

GO Term annotation Help

Process

GO:0006537 glutamate biosynthetic process
GO:0006562 proline catabolic process
GO:0055114 oxidation reduction

Function

GO:0004657 proline dehydrogenase activity

InterPro annotation

Entry Details in BioMart

Abstract

The proline oxidase/dehydrogenase EC:1.5.99.8 is responsible for the first step in the conversion of proline to glutamate for use as a carbon and nitrogen source. The enzyme requires FAD as a cofactor, and is induced by proline. It is found in combination with IPR002086 in bacteria.

Structural links Help

PDB - click here

SCOP: a.176.1.1 , c.1.23.2

CATH: 1.10.2060.10 , 3.20.20.220

Database links Help

Enzyme: EC:1.5.99.8

PANDIT: PF01619

Blocks: IPB002872

COMe: PRX000710

Pfam Clan: CL0086.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR002872

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O43272 Proline dehydrogenase, mitochondrial

O45228 Proline dehydrogenase, mitochondrial

P09368 Proline dehydrogenase, mitochondrial

Q04499 Proline dehydrogenase, mitochondrial

Q8VCZ9 Probable proline dehydrogenase 2

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002872	Proline dehydrogenase
IPR011992	EF-hand-like domain
IPR015659	Proline oxidase
	SWISS-MODEL
	ModBase

Publications Help

Additional Reading Open in usermanual
	Zhang M, White TA, Schuermann JP, Baban BA, Becker DF, Tanner JJ. Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. Biochemistry 43 2004 12539-48 [PubMed: 15449943] http://dx.doi.org/10.1021/bi048737e
	Ling M, Allen SW, Wood JM. Sequence analysis identifies the proline dehydrogenase and delta 1-pyrroline-5-carboxylate dehydrogenase domains of the multifunctional Escherichia coli PutA protein. J. Mol. Biol. 243 1994 950-6 [PubMed: 7966312] http://dx.doi.org/10.1006/jmbi.1994.1696
	Zhang W, Zhang M, Zhu W, Zhou Y, Wanduragala S, Rewinkel D, Tanner JJ, Becker DF. Redox-induced changes in flavin structure and roles of flavin N(5) and the ribityl 2'-OH group in regulating PutA--membrane binding. Biochemistry 46 2007 483-91 [PubMed: 17209558] http://dx.doi.org/10.1021/bi061935g
	Lee YH, Nadaraia S, Gu D, Becker DF, Tanner JJ. Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein. Nat. Struct. Biol. 10 2003 109-14 [PubMed: 12514740] http://dx.doi.org/10.1038/nsb885

InterPro 23.1