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Database: UniProt
Entry: F7UVE3_EEGSY
LinkDB: F7UVE3_EEGSY
Original site: F7UVE3_EEGSY 
ID   F7UVE3_EEGSY            Unreviewed;       269 AA.
AC   F7UVE3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   24-JAN-2024, entry version 60.
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:0000313|EMBL:BAK45166.1};
GN   Synonyms=proC {ECO:0000256|HAMAP-Rule:MF_01925};
GN   OrderedLocusNames=EGYY_20760 {ECO:0000313|EMBL:BAK45166.1};
OS   Eggerthella sp. (strain YY7918).
OC   Bacteria; Actinomycetota; Coriobacteriia; Eggerthellales; Eggerthellaceae;
OC   Eggerthella.
OX   NCBI_TaxID=502558 {ECO:0000313|EMBL:BAK45166.1, ECO:0000313|Proteomes:UP000008929};
RN   [1] {ECO:0000313|EMBL:BAK45166.1, ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|EMBL:BAK45166.1,
RC   ECO:0000313|Proteomes:UP000008929};
RX   PubMed=21914883;
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete Genomic Sequence of the Equol-Producing Bacterium Eggerthella sp.
RT   Strain YY7918, Isolated from Adult Human Intestine.";
RL   J. Bacteriol. 193:5570-5571(2011).
RN   [2] {ECO:0000313|Proteomes:UP000008929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YY7918 {ECO:0000313|Proteomes:UP000008929};
RA   Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT   "Complete genome sequence of the equol-producing bacterium Eggerthella sp.
RT   strain YY7918 isolated from adult human intestine.";
RL   Submitted (JUN-2011) 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}.
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DR   EMBL; AP012211; BAK45166.1; -; Genomic_DNA.
DR   RefSeq; WP_013980410.1; NC_015738.1.
DR   AlphaFoldDB; F7UVE3; -.
DR   STRING; 502558.EGYY_20760; -.
DR   KEGG; eyy:EGYY_20760; -.
DR   eggNOG; COG0345; Bacteria.
DR   HOGENOM; CLU_042344_3_1_11; -.
DR   OMA; VVRVMTN; -.
DR   OrthoDB; 9805754at2; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000008929; Chromosome.
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 3; 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|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01925};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01925};
KW   Proline biosynthesis {ECO:0000256|HAMAP-Rule:MF_01925};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008929}.
FT   DOMAIN          13..106
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          170..266
FT                   /note="Pyrroline-5-carboxylate reductase dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF14748"
FT   BINDING         16..21
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         78..81
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   269 AA;  27600 MW;  74B529640B5BE1D3 CRC64;
     MSTTDAAHNE AALGFIGFGN MAQAMARGLI ESHTCSGSRI TACAAHFDKL QKNAAALGVQ
     PAQTAAEVVE ASDLVILAVK PYQVAQVVES VRDALANKIV ISVAAGCDFD FYETILASGT
     HHLSTIPNTP IAVGHGVIAC ENRHSLTEDE YALFTGIFGQ IALIEPVDTK LLSTASSVAG
     CGPAFAAMFL EALSDAGVKH GLPRATAYRL ASQMMLGTAA LQLATGEHPG AMKDAVCSPG
     GTTIKGVAAL EKGGFRSSII SAVDATKGE
//
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