ID A0A420REI7_FUSOX Unreviewed; 343 AA.
AC A0A420REI7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|RuleBase:RU003903};
DE EC=1.5.1.2 {ECO:0000256|RuleBase:RU003903};
GN ORFNames=BFJ68_g5659 {ECO:0000313|EMBL:RKL15445.1}, BFJ69_g14381
GN {ECO:0000313|EMBL:RKK67578.1}, FOXYS1_11157
GN {ECO:0000313|EMBL:KAF5258275.1};
OS Fusarium oxysporum (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=5507 {ECO:0000313|EMBL:RKL15445.1, ECO:0000313|Proteomes:UP000285860};
RN [1] {ECO:0000313|Proteomes:UP000285084, ECO:0000313|Proteomes:UP000285860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo_A13 {ECO:0000313|EMBL:RKK67578.1,
RC ECO:0000313|Proteomes:UP000285084}, and Fo_A28
RC {ECO:0000313|EMBL:RKL15445.1, ECO:0000313|Proteomes:UP000285860};
RX PubMed=30202022; DOI=10.1038/s41598-018-30335-7;
RA Armitage A.D., Taylor A., Sobczyk M.K., Baxter L., Greenfield B.P.,
RA Bates H.J., Wilson F., Jackson A.C., Ott S., Harrison R.J., Clarkson J.P.;
RT "Characterisation of pathogen-specific regions and novel effector
RT candidates in Fusarium oxysporum f. sp. cepae.";
RL Sci. Rep. 8:13530-13530(2018).
RN [2] {ECO:0000313|EMBL:KAF5258275.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 39464 {ECO:0000313|EMBL:KAF5258275.1};
RA Kim H.-S., Busman M., Brown D.W., Divon H., Uhlig S., Proctor R.H.;
RT "Identification and distribution of gene clusters putatively required for
RT synthesis of sphingolipid metabolism inhibitors in phylogenetically diverse
RT species of the filamentous fungus Fusarium.";
RL Submitted (FEB-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NADP(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADPH; Xref=Rhea:RHEA:14109, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000256|RuleBase:RU003903};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000256|RuleBase:RU003903}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|RuleBase:RU003903}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RKL15445.1}.
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DR EMBL; JAAFOW010002043; KAF5258275.1; -; Genomic_DNA.
DR EMBL; MRCX01000223; RKK67578.1; -; Genomic_DNA.
DR EMBL; MRCY01000021; RKL15445.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:FOC1_g10013596; -.
DR VEuPathDB; FungiDB:FOC4_g10010503; -.
DR VEuPathDB; FungiDB:FOIG_05641; -.
DR VEuPathDB; FungiDB:FOMG_04897; -.
DR VEuPathDB; FungiDB:FOXG_02162; -.
DR VEuPathDB; FungiDB:FOZG_05068; -.
DR VEuPathDB; FungiDB:HZS61_010061; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000285084; Unassembled WGS sequence.
DR Proteomes; UP000285860; Unassembled WGS sequence.
DR Proteomes; UP000558688; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.3730.10; ProC C-terminal domain-like; 1.
DR HAMAP; MF_01925; P5C_reductase; 1.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR028939; P5C_Rdtase_cat_N.
DR InterPro; IPR029036; P5CR_dimer.
DR InterPro; IPR000304; Pyrroline-COOH_reductase.
DR NCBIfam; TIGR00112; proC; 1.
DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR PANTHER; PTHR11645:SF0; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00521; P5CR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|RuleBase:RU003903};
KW Membrane {ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU003903};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003903};
KW Proline biosynthesis {ECO:0000256|RuleBase:RU003903};
KW Reference proteome {ECO:0000313|Proteomes:UP000558688};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 97..147
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 223..321
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 35729 MW; 1FA1B5EA434601C3 CRC64;
MSPNTMALTP YGSNGSTDLT MAVLGCGTMG VAILSGILNS LAEMQGPKPL QSLPRSGTST
PGDEVPERLP SRFVASVATA AGAKRVKGAL WEHSSILKVV HNDNIGAVQQ AEVVLLTCKP
WMVKEILSEP GISKALHGKL LVSVCAGITV EDIEIALHGA VPSKDPEEDG RCRIVRAMCN
TAAVIRESMT VIASPSSPLD HATESLVTWI FRRIGDVVYL PTRHMDASTA LCASGPAFFA
LVLEAAIDGA VAMGIPRADA QRMATQSMRG TAGLVQNGEH PALLREKVCT SGGCTIGGVL
VLEEGRVRGS VSRAVREAAV VAGQIGKGAD GVNGTRFPGA RYE
//
