[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; DOI=10.1007/s004380050329; PubMed=9003320 [NCBI, ExPASy, EBI, Israel, Japan] Peng Z., Lu Q., Verma D.P.S.; "Reciprocal regulation of delta 1-pyrroline-5-carboxylate synthetase and proline dehydrogenase genes controls proline levels during and after osmotic stress in plants."; Mol. Gen. Genet. 253:334-341(1996).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; TISSUE=Root; DOI=10.1073/pnas.93.16.8787; PubMed=8710950 [NCBI, ExPASy, EBI, Israel, Japan] Verbruggen N., Hua X.J., May M., van Montagu M.; "Environmental and developmental signals modulate proline homeostasis: evidence for a negative transcriptional regulator."; Proc. Natl. Acad. Sci. U.S.A. 93:8787-8791(1996).
[3]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Columbia; DOI=10.1105/tpc.8.8.1323; PubMed=8776899 [NCBI, ExPASy, EBI, Israel, Japan] Kiyosue T., Yoshiba Y., Yamaguchi-Shinozaki K., Shinozaki K.; "A nuclear gene encoding mitochondrial proline dehydrogenase, an enzyme involved in proline metabolism, is upregulated by proline but downregulated by dehydration in Arabidopsis."; Plant Cell 8:1323-1335(1996).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Columbia; DOI=10.1093/dnares/7.2.131; PubMed=10819329 [NCBI, ExPASy, EBI, Israel, Japan] Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.; "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."; DNA Res. 7:131-135(2000).

Comments

FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CATALYTIC ACTIVITY: L-proline + acceptor + H₂O = (S)-1-pyrroline-5-carboxylate + reduced acceptor.
COFACTOR: FAD.
PATHWAY: Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2 .
SUBCELLULAR LOCATION: Mitochondrion matrix.
INDUCTION: By osmotic stress.
SIMILARITY: Belongs to the proline oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U59508; AAB40615.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X97075; CAA65783.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D83025; BAA11682.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB028614; BAB02917.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AP001296; BAB02917.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_189701.3; -.

UniGene

At.24174

3D structure databases

ModBase

P92983.

Organism-specific databases

TAIR

At3g30775; -.

Gene expression databases

ArrayExpress

P92983; -.

GermOnline

AT3G30775; Arabidopsis thaliana.

Ontologies

GO:0005759;	Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
QuickGo view.

Family and domain databases

InterPro

IPR002872; Proline_DHase.
IPR015659; Proline_oxidase.
Graphical view of domain structure.

PANTHER

PTHR13914; Proline_oxidase; 1.

Pfam

PF01619; Pro_dh; 1.
Pfam graphical view of domain structure.

BLOCKS

P92983.

Genome annotation databases

GeneID

822833; -.

GenomeReviews

BA000014_GR; AT3G30775.

KEGG

ath:AT3G30775; -.

NMPDR

fig|3702.1.peg.15354; -.

Other

ProtoNet

P92983.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Proline metabolism; Stress response; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 16`	`16`	`Mitochondrion (Potential).`
`CHAIN`	`17 499`	`483`	`Proline oxidase, mitochondrial.`	`PRO_0000025804`
`CONFLICT`	`30 30`		`A -> V (in Ref. 1; AAB40615).`
`CONFLICT`	`46 46`		`P -> T (in Ref. 1; AAB40615).`
`CONFLICT`	`51 51`		`H -> Q (in Ref. 1; AAB40615).`
`CONFLICT`	`91 91`		`A -> P (in Ref. 2; CAA65783).`
`CONFLICT`	`355 355`		`A -> R (in Ref. 3; BAA11682).`
`CONFLICT`	`361 361`		`L -> V (in Ref. 2; CAA65783).`
`CONFLICT`	`477 477`		`A -> P (in Ref. 1; AAB40615).`

Sequence information

Length: 499 AA [This is the length of the unprocessed precursor]

Molecular weight: 54956 Da [This is the MW of the unprocessed precursor]

CRC64: 1428611A40EFC824 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATRLLRTNF IRRSYRLPAF SPVGPPTVTA STAVVPEILS FGQQAPEPPL HHPKPTEQSH 

        70         80         90        100        110        120 
DGLDLSDQAR LFSSIPTSDL LRSTAVLHAA AIGPMVDLGT WVMSSKLMDA SVTRGMVLGL 

       130        140        150        160        170        180 
VKSTFYDHFC AGEDADAAAE RVRSVYEATG LKGMLVYGVE HADDAVSCDD NMQQFIRTIE 

       190        200        210        220        230        240 
AAKSLPTSHF SSVVVKITAI CPISLLKRVS DLLRWEYKSP NFKLSWKLKS FPVFSESSPL 

       250        260        270        280        290        300 
YHTNSEPEPL TAEEERELEA AHGRIQEICR KCQESNVPLL IDAEDTILQP AIDYMAYSSA 

       310        320        330        340        350        360 
IMFNADKDRP IVYNTIQAYL RDAGERLHLA VQNAEKENVP MGFKLVRGAY MSSEASLADS 

       370        380        390        400        410        420 
LGCKSPVHDT IQDTHSCYND CMTFLMEKAS NGSGFGVVLA THNADSGRLA SRKASDLGID 

       430        440        450        460        470        480 
KQNGKIEFAQ LYGMSDALSF GLKRAGFNVS KYMPFGPVAT AIPYLLRRAY ENRGMMATGA 

       490 
HDRQLMRMEL KRRLIAGIA

P92983 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools