ID E3GKL1_9FIRM Unreviewed; 269 AA.
AC E3GKL1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Pyrroline-5-carboxylate reductase {ECO:0000256|HAMAP-Rule:MF_01925, ECO:0000256|RuleBase:RU003903};
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, ECO:0000256|RuleBase:RU003903};
DE AltName: Full=PCA reductase {ECO:0000256|HAMAP-Rule:MF_01925};
GN Name=proC {ECO:0000256|HAMAP-Rule:MF_01925,
GN ECO:0000313|EMBL:NZA39826.1};
GN OrderedLocusNames=ELI_1030 {ECO:0000313|EMBL:ADO36018.1};
GN ORFNames=H0N91_17255 {ECO:0000313|EMBL:NZA39826.1};
OS Eubacterium callanderi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=53442 {ECO:0000313|EMBL:ADO36018.1, ECO:0000313|Proteomes:UP000006873};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KIST612;
RA Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S.,
RA Choi I.-G.;
RL Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO36018.1, ECO:0000313|Proteomes:UP000006873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIST612 {ECO:0000313|EMBL:ADO36018.1,
RC ECO:0000313|Proteomes:UP000006873};
RX PubMed=21036996; DOI=10.1128/JB.01217-10;
RA Roh H., Ko H.J., Kim D., Choi D.G., Park S., Kim S., Chang I.S., Choi I.G.;
RT "Complete genome sequence of a carbon monoxide-utilizing acetogen,
RT Eubacterium limosum KIST612.";
RL J. Bacteriol. 193:307-308(2011).
RN [3] {ECO:0000313|EMBL:NZA39826.1, ECO:0000313|Proteomes:UP000586254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMC0717 {ECO:0000313|EMBL:NZA39826.1,
RC ECO:0000313|Proteomes:UP000586254};
RA Marsh A.J., Azcarate-Peril M.A.;
RT "Organ Donor 1.";
RL Submitted (JUL-2020) 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 ECO:0000256|RuleBase:RU003903};
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, ECO:0000256|RuleBase:RU003903}.
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 ECO:0000256|RuleBase:RU003903}.
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DR EMBL; CP002273; ADO36018.1; -; Genomic_DNA.
DR EMBL; JACCKS010000026; NZA39826.1; -; Genomic_DNA.
DR RefSeq; WP_013379339.1; NZ_JANGDA010000010.1.
DR AlphaFoldDB; E3GKL1; -.
DR GeneID; 68362353; -.
DR KEGG; elm:ELI_1030; -.
DR eggNOG; COG0345; Bacteria.
DR HOGENOM; CLU_042344_3_1_9; -.
DR UniPathway; UPA00098; UER00361.
DR Proteomes; UP000006873; Chromosome.
DR Proteomes; UP000586254; 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 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 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.
DR PROSITE; PS00521; P5CR; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW ECO:0000256|RuleBase:RU003903};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01925};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01925};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925,
KW ECO:0000256|RuleBase:RU003903};
KW Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925,
KW ECO:0000256|RuleBase:RU003903}.
FT DOMAIN 4..98
FT /note="Pyrroline-5-carboxylate reductase catalytic N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF03807"
FT DOMAIN 162..263
FT /note="Pyrroline-5-carboxylate reductase dimerisation"
FT /evidence="ECO:0000259|Pfam:PF14748"
FT BINDING 8..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT BINDING 70..73
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ SEQUENCE 269 AA; 28516 MW; 1E87798A9D7243A0 CRC64;
MKDTIGFIGC GNMAQAMIGG VVSSGLFTGA QIIAYDPSEA QRRKVAEKFG IRTAESNIGV
ASEADYLVLA VKPFVYADVL REIAGHTKKD VIVIVIAVGV EFSDVKDILG KDTKVIRTQP
STPAFVGESD STVCPDDLMT EQDIEAVMTI FKSFGRVEII SEKLMNVVPS IASSAPAYTM
LLIEAMADGG VLHGFPRDQA YRLAAQSVYG AAKLVLETGE HPAVLKDQIC TPGGTTIEAV
RALEASGFRK AVISAVDACA LKSISLLKK
//
