ID A0A5J5GHM6_9BACL Unreviewed; 283 AA.
AC A0A5J5GHM6;
DT 11-DEC-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE Short=P5C reductase {ECO:0000256|HAMAP-Rule:MF_01925};
DE Short=P5CR {ECO:0000256|HAMAP-Rule:MF_01925};
DE EC=1.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01925};
DE AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000256|HAMAP-Rule:MF_01925};
GN ORFNames=F4V43_04200 {ECO:0000313|EMBL:KAA9007691.1};
OS Paenibacillus spiritus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=2496557 {ECO:0000313|EMBL:KAA9007691.1, ECO:0000313|Proteomes:UP000367750};
RN [1] {ECO:0000313|EMBL:KAA9007691.1, ECO:0000313|Proteomes:UP000367750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MER_111 {ECO:0000313|EMBL:KAA9007691.1,
RC ECO:0000313|Proteomes:UP000367750};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus ochoae sp. nov., Paenibacillus whitsoniae sp. nov., Paenibacillus
RT spiritus sp. nov. Isolated from the Mars Exploration Rover during
RT spacecraft assembly.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to
CC L-proline. {ECO:0000256|HAMAP-Rule:MF_01925}.
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|HAMAP-Rule:MF_01925};
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|HAMAP-Rule:MF_01925};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-proline
CC from L-glutamate 5-semialdehyde: step 1/1. {ECO:0000256|HAMAP-
CC Rule:MF_01925}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925}.
CC -!- SIMILARITY: Belongs to the pyrroline-5-carboxylate reductase family.
CC {ECO:0000256|ARBA:ARBA00005525, ECO:0000256|HAMAP-Rule:MF_01925}.
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:KAA9007691.1}.
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DR EMBL; VYKK01000004; KAA9007691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5J5GHM6; -.
DR OrthoDB; 9805754at2; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000367750; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004735; F:pyrroline-5-carboxylate reductase activity; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR11645:SF51; COME OPERON PROTEIN 4; 1.
DR PANTHER; PTHR11645; PYRROLINE-5-CARBOXYLATE REDUCTASE; 1.
DR Pfam; PF03807; F420_oxidored; 1.
DR Pfam; PF14748; P5CR_dimer; 1.
DR PIRSF; PIRSF000193; Pyrrol-5-carb_rd; 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|HAMAP-Rule:MF_01925};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|PIRSR:PIRSR000193-1};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925};
KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925};
KW Reference proteome {ECO:0000313|Proteomes:UP000367750};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..283
FT /note="Pyrroline-5-carboxylate reductase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039538787"
FT DOMAIN 3..97
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 159..262
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 6..11
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 56
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 283 AA; 30943 MW; 6932F485766D8FBA CRC64;
MKAGFIGTGS MGSLLIDALL SSGALQAADV LASNRSPQKL IRLAQRYPGL SLCSRNSETA
AGSDLLFLCV KPLEFKALID EIGPVLRAEQ IVVSITSPVQ LHHLESVLPC KIAKIIPSIT
HRVFSGASLC IFGSRLGEDD RRLLLKLFSH IGIPAEIHEE HTRIASDFSS CGPAFVSYFL
ERWVEAAVRE TGIDERLAVR LAGEMLLGTG RLLTEGEFSP QELQERVAVP GGITAEALNH
LRRSLDGVFE QLIETTQGKY EEDIAKLDRL FGRDSVIQEP LDR
//