ID A0A4C1TDH4_EUMVA Unreviewed; 301 AA.
AC A0A4C1TDH4;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=pyrroline-5-carboxylate reductase {ECO:0000256|ARBA:ARBA00012855};
DE EC=1.5.1.2 {ECO:0000256|ARBA:ARBA00012855};
GN Name=PROC1 {ECO:0000313|EMBL:GBP12165.1};
GN ORFNames=EVAR_6351_1 {ECO:0000313|EMBL:GBP12165.1};
OS Eumeta variegata (Bagworm moth) (Eumeta japonica).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Tineoidea;
OC Psychidae; Oiketicinae; Eumeta.
OX NCBI_TaxID=151549 {ECO:0000313|EMBL:GBP12165.1, ECO:0000313|Proteomes:UP000299102};
RN [1] {ECO:0000313|EMBL:GBP12165.1, ECO:0000313|Proteomes:UP000299102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=31044173; DOI=.1038/s42003-019-0412-8;
RA Kono N., Nakamura H., Ohtoshi R., Tomita M., Numata K., Arakawa K.;
RT "The bagworm genome reveals a unique fibroin gene that provides high
RT tensile strength.";
RL Commun. Biol. 2:148-148(2019).
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 -!- 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:GBP12165.1}.
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DR EMBL; BGZK01000050; GBP12165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4C1TDH4; -.
DR STRING; 151549.A0A4C1TDH4; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000299102; Unassembled WGS sequence.
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; 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; 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.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000299102}.
FT DOMAIN 193..294
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 31534 MW; 94FE14AC9B15952C CRC64;
MSARGAAFSR SKLASEPPES KVVTAVHGQS PLERSHQCSA RLFGRNKISD GKRNADGGGV
LFHVWVLGES DVSSIESGLG AAAFFENKPV VERSEVVIVS VKPDVVGKAL SEVKGLAACS
KKLFISVAMG VNIATIEKNL PLDARVIRVM PNTPALVRQG AAVLSRGSRA TSEDAELTAR
LFRAVGSCDE VPEYQMDAVT ALSGSGPAYV YMMIESLADG GIRCGLPRDL ALKLAAQTAL
GSAAMIREGS HPAQLRDNVT SPAGSTAEGT YHLEQNGFRA AVIGAVSAAT ERCKIVSKEI
N
//
