PROD_CAEEL
ID PROD_CAEEL Reviewed; 616 AA.
AC O45228; A0A061AD41;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Proline dehydrogenase 1, mitochondrial;
DE EC=1.5.5.2 {ECO:0000250|UniProtKB:O43272};
DE AltName: Full=Proline oxidase;
DE Flags: Precursor;
GN Name=prdh-1 {ECO:0000312|WormBase:B0513.5a};
GN Synonyms=prodh {ECO:0000303|PubMed:27974198};
GN ORFNames=B0513.5 {ECO:0000312|WormBase:B0513.5a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27974198; DOI=10.1016/j.celrep.2016.11.038;
RA Tang H., Pang S.;
RT "Proline Catabolism Modulates Innate Immunity in Caenorhabditis elegans.";
RL Cell Rep. 17:2837-2844(2016).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate (By
CC similarity). Through proline catabolism, promotes reactive oxygen
CC species (ROS) production and the transcription of skn-1 target genes in
CC response to bacterial infection by P.aeruginosa (PubMed:27974198).
CC {ECO:0000250|UniProtKB:O43272, ECO:0000269|PubMed:27974198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a quinone + L-proline = (S)-1-pyrroline-5-carboxylate + a
CC quinol + H(+); Xref=Rhea:RHEA:23784, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17388, ChEBI:CHEBI:24646, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:132124; EC=1.5.5.2;
CC Evidence={ECO:0000250|UniProtKB:O43272};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:O43272};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:B0513.5a};
CC IsoId=O45228-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:B0513.5b};
CC IsoId=O45228-2; Sequence=VSP_060478;
CC -!- INDUCTION: Up-regulated by infection with P.aeruginosa.
CC {ECO:0000269|PubMed:27974198}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces the survival
CC incidence, results in increased bacterial load and reduces ROS
CC production following infection by P.aeruginosa (PubMed:27974198). RNAi-
CC mediated knockdown inhibits the nuclear accumulation of the
CC transcription factor skn-1 and reduces the expression of skn-1
CC transcriptional targets including gst-4 following infection by
CC P.aeruginosa (PubMed:27974198). RNAi-mediated knockdown suppresses the
CC pro-survival effects of the addition of exogenous proline following
CC infection by P.aeruginosa (PubMed:27974198).
CC {ECO:0000269|PubMed:27974198}.
CC -!- SIMILARITY: Belongs to the proline oxidase family. {ECO:0000305}.
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DR EMBL; BX284604; CAB05117.2; -; Genomic_DNA.
DR EMBL; BX284604; CDR32778.1; -; Genomic_DNA.
DR PIR; T18776; T18776.
DR RefSeq; NP_001293995.1; NM_001307066.1.
DR RefSeq; NP_502669.2; NM_070268.4. [O45228-1]
DR AlphaFoldDB; O45228; -.
DR BioGRID; 43434; 1.
DR STRING; 6239.B0513.5; -.
DR iPTMnet; O45228; -.
DR EPD; O45228; -.
DR PaxDb; O45228; -.
DR PeptideAtlas; O45228; -.
DR EnsemblMetazoa; B0513.5a.1; B0513.5a.1; WBGene00007197. [O45228-1]
DR EnsemblMetazoa; B0513.5b.1; B0513.5b.1; WBGene00007197. [O45228-2]
DR GeneID; 178350; -.
DR KEGG; cel:CELE_B0513.5; -.
DR UCSC; B0513.5; c. elegans. [O45228-1]
DR CTD; 178350; -.
DR WormBase; B0513.5a; CE37309; WBGene00007197; prdh-1. [O45228-1]
DR WormBase; B0513.5b; CE49937; WBGene00007197; prdh-1. [O45228-2]
DR eggNOG; KOG0186; Eukaryota.
DR GeneTree; ENSGT00390000006265; -.
DR HOGENOM; CLU_018202_3_1_1; -.
DR InParanoid; O45228; -.
DR OMA; YLNEASC; -.
DR OrthoDB; 948528at2759; -.
DR PhylomeDB; O45228; -.
DR Reactome; R-CEL-389661; Glyoxylate metabolism and glycine degradation.
DR Reactome; R-CEL-70688; Proline catabolism.
DR UniPathway; UPA00261; UER00373.
DR PRO; PR:O45228; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00007197; Expressed in larva and 3 other tissues.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0004657; F:proline dehydrogenase activity; ISS:UniProtKB.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR015659; Proline_oxidase.
DR PANTHER; PTHR13914; PTHR13914; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF51730; SSF51730; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; FAD; Flavoprotein; Mitochondrion; Oxidoreductase;
KW Proline metabolism; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..616
FT /note="Proline dehydrogenase 1, mitochondrial"
FT /id="PRO_0000025802"
FT VAR_SEQ 1..101
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060478"
SQ SEQUENCE 616 AA; 69823 MW; 1A3F2B280CDF5D58 CRC64;
MQAALIGLNF PLQRRFLSGV LTTTSSAKRC YSGDTGKPYD CTSAEHKKEL EECYNRLDLS
FENTKEAFKS KSNTELVRAL VVLRLCGIQT LVNQNQIILN TMRRVLGKNL FKKTLKNTFF
GHFVAGETEE EVRHVVEKLR NYGVKSILDY SVEADITSQE ATDKTVKGTS VATVKPAAMT
PVVDAKTLET TRERYTVHEE FGDRRQGVSS ARTYFYEGEE QCDKNRDIFK DSINAVASAT
KNEGFVAVKI TALGRPQLLL KLSEAIVQTQ NFFKALTGGM SLQEGRLTSQ EFYKRLGELG
VKTDTESVKK FFDEVDFDSD GIVDLHGWNH ILDDHVKLGQ LFQVLNIKTG SLEPLIQNLS
NEEEQEFRNM VRRTLDVAEY AIEKGVRIMV DAEQTYLQPA ISKITIEMMK KYNKGRGNIF
NTYQAYLKGT LQNMEADMQV ARREGWHFGA KLVRGAYMEQ ERARAKAIGY EDPINDNFEA
TSKMYESCLT RIADEVHRRG KTNVSVMVAS HNEDTVRFAL NLMKEKCISP SERVMCMAQL
YGMCDQVSFS LGQAGFSVYK YLPYGPVEEV LPYLSRRALE NGSVLKKANK ERDLLWKELK
RRISSGEFKA RSSSSS
