ID A0A0V1P7Z8_9BILA Unreviewed; 446 AA.
AC A0A0V1P7Z8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=pyrroline-5-carboxylate reductase {ECO:0000256|ARBA:ARBA00012855};
DE EC=1.5.1.2 {ECO:0000256|ARBA:ARBA00012855};
DE Flags: Fragment;
GN Name=PROC1 {ECO:0000313|EMBL:KRZ92467.1};
GN ORFNames=T08_2535 {ECO:0000313|EMBL:KRZ92467.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ92467.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ92467.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ92467.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-proline + NAD(+) = 1-pyrroline-5-carboxylate + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:14105, ChEBI:CHEBI:15378, ChEBI:CHEBI:15893,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:60039; EC=1.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000593};
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|ARBA:ARBA00000723};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005205}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525}.
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:KRZ92467.1}.
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DR EMBL; JYDM01000034; KRZ92467.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1P7Z8; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
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; 6.10.280.10; Mediator complex, subunit Med21; 1.
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; IPR037212; Med7/Med21-like.
DR InterPro; IPR021384; Mediator_Med21.
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; PF11221; Med21; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF140718; Mediator hinge subcomplex-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924}.
FT DOMAIN 173..264
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 327..428
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ92467.1"
SQ SEQUENCE 446 AA; 48320 MW; 1013DAC68DC74DDF CRC64;
LNNSMKSICI HLHLLTMSDR LTQLQDCINE LASQICNSTG VLQQTASASN FENNDQFSTG
AEDNAELFAK LVASTSSDID MLVDLLPNEE PSPDLQNEQF SELNNLNTEA AQSLRLSVER
GQVLLERIKN ILSFIDNTQK IVAEIRSSDP KSVITLTVQK MSVSEDIFFN MNIGFVGAGK
MGQAMIRGKF AAQNITASAP VEDRHYLDEI KSKVNINVTH SNLDLARTSD VVIFAIPPSI
SFRVICEMKT ILNSDKLILS IMNGVSMDTI EQIACKKLRV ARAMPNMAAT VRRSATAYAL
NERCTSRDEA LVSGLLSCIG FAVKLPERLI NSATGLSGCG PAYMFTVLEA MAEGGVKAGL
PRDIAQQLAV NTMLGSAEMV IQTGKHPTIL RESIESPGGS TVVGVHELEK AAFRAALINA
VEAATNHAFK QDNMQIRLGP SATRSN
//
