ID E3KDR7_PUCGT Unreviewed; 631 AA.
AC E3KDR7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Proline dehydrogenase {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
DE EC=1.5.5.2 {ECO:0000256|ARBA:ARBA00012695, ECO:0000256|RuleBase:RU364054};
GN ORFNames=PGTG_08459 {ECO:0000313|EMBL:EFP82503.2};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP82503.2, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000008783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRL 75-36-700-3 / race SCCL
RC {ECO:0000313|Proteomes:UP000008783};
RX PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA Grigoriev I.V., Szabo L.J., Martin F.;
RT "Obligate biotrophy features unraveled by the genomic analysis of rust
RT fungi.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC -!- FUNCTION: Converts proline to delta-1-pyrroline-5-carboxylate.
CC {ECO:0000256|RuleBase:RU364054}.
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:0000256|RuleBase:RU364054};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|RuleBase:RU364054};
CC -!- SIMILARITY: Belongs to the proline oxidase family.
CC {ECO:0000256|ARBA:ARBA00005869, ECO:0000256|RuleBase:RU364054}.
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DR EMBL; DS178282; EFP82503.2; -; Genomic_DNA.
DR RefSeq; XP_003326922.2; XM_003326874.2.
DR AlphaFoldDB; E3KDR7; -.
DR STRING; 418459.E3KDR7; -.
DR EnsemblFungi; EFP82503; EFP82503; PGTG_08459.
DR GeneID; 10529882; -.
DR KEGG; pgr:PGTG_08459; -.
DR VEuPathDB; FungiDB:PGTG_08459; -.
DR eggNOG; KOG0186; Eukaryota.
DR HOGENOM; CLU_018202_1_1_1; -.
DR InParanoid; E3KDR7; -.
DR OrthoDB; 7218at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR GO; GO:0004657; F:proline dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IBA:GO_Central.
DR Gene3D; 3.20.20.220; -; 1.
DR InterPro; IPR029041; FAD-linked_oxidoreductase-like.
DR InterPro; IPR002872; Proline_DH_dom.
DR InterPro; IPR015659; Proline_oxidase.
DR PANTHER; PTHR13914:SF0; PROLINE DEHYDROGENASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13914; PROLINE OXIDASE; 1.
DR Pfam; PF01619; Pro_dh; 1.
DR SUPFAM; SSF51730; FAD-linked oxidoreductase; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU364054};
KW Flavoprotein {ECO:0000256|RuleBase:RU364054};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU364054};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062,
KW ECO:0000256|RuleBase:RU364054};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT DOMAIN 237..599
FT /note="Proline dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF01619"
FT REGION 16..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 631 AA; 67833 MW; 9784B65B88B84AFE CRC64;
MTLIRLGPVH MGLRNIRPSQ SFTKPSRSSP SRYLSSGSTP GFCSRRFYGS SHQQGSGPTG
ARLWAGPSPG RGSTGYTLLA TALGLGALAS GATVYALQTA DLPDDPLAAL APDALRLKAA
HVAQKAAPDL LRSYLTLLLC EIPGVATYGP LLLNHCISLR DNVPILGPAT WSVVEWFVFH
TFFSHYTGGE SAEDCQPVMK ALYEGEVGSL LNYSVEALEG AGKGSSESGL SRESVAAITR
TVESLAGYES GAKGYAASSA RMKPSAVAIK VSGLVDDPYL FKRASENLLA NGLSPFRVNG
SPFPIVNSHI PDPLSPADHL TLDGLMDSLR GVCQKAKAAD IVIMIDAEYS WFQPALDRIA
TFLSAEFNKS KSEGPGSASY SPTVFNTFQA LLRSTPERLA EYVDEGHKRD FSVGVKLVRG
AYLVSETARW REARAAGRPG VPDHPPVWAS KAETDGCFDN LASSLVQQLA SNARRAQGLT
SDPRQSRSSN SIEVAMMIAG HNPISAAKVL KQLRDEEGLA KNVDGQSIRL SDSLRGRLMF
AQLYGMADNL TSTLTQILAP SDADNQKHPQ PFVFKYLPFG PVDKVLPYLA RRAEENSSIL
EVKDGESVLS LERKLIGKEI RKRIGSLFFL S
//
