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Database: UniProt
Entry: B4V2Q9_9ACTN
LinkDB: B4V2Q9_9ACTN
Original site: B4V2Q9_9ACTN 
ID   B4V2Q9_9ACTN            Unreviewed;       268 AA.
AC   B4V2Q9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 70.
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=M444_23775 {ECO:0000313|EMBL:AKL70254.1}, SSAG_02037
GN   {ECO:0000313|EMBL:EDX22246.1};
OS   Streptomyces sp. Mg1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX22246.1, ECO:0000313|Proteomes:UP000005764};
RN   [1] {ECO:0000313|EMBL:EDX22246.1, ECO:0000313|Proteomes:UP000005764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:EDX22246.1,
RC   ECO:0000313|Proteomes:UP000005764};
RG   The Broad Institute Genome Sequencing Platform;
RA   Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA   Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., Straight P.,
RA   Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA   Lander E., Galagan J., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces sp. Mg1.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AKL70254.1, ECO:0000313|Proteomes:UP000035653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL70254.1,
RC   ECO:0000313|Proteomes:UP000035653};
RX   PubMed=23908282;
RA   Hoefler B.C., Konganti K., Straight P.D.;
RT   "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT   Single-Molecule Sequencing.";
RL   Genome Announc. 1:e00535-13(2013).
RN   [3] {ECO:0000313|EMBL:AKL70254.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mg1 {ECO:0000313|EMBL:AKL70254.1};
RA   Hoefler B.C., Straight P.D.;
RL   Submitted (JUN-2015) 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; CP011664; AKL70254.1; -; Genomic_DNA.
DR   EMBL; DS570390; EDX22246.1; -; Genomic_DNA.
DR   RefSeq; WP_008738305.1; NZ_DS570390.1.
DR   AlphaFoldDB; B4V2Q9; -.
DR   STRING; 465541.M444_23775; -.
DR   KEGG; strm:M444_23775; -.
DR   PATRIC; fig|465541.12.peg.5039; -.
DR   eggNOG; COG0345; Bacteria.
DR   HOGENOM; CLU_042344_0_0_11; -.
DR   OrthoDB; 9805754at2; -.
DR   UniPathway; UPA00098; UER00361.
DR   Proteomes; UP000005764; Unassembled WGS sequence.
DR   Proteomes; UP000035653; 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; IPR033379; Acid_Pase_AS.
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; PS00616; HIS_ACID_PHOSPHAT_1; 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:UP000035653}.
FT   DOMAIN          5..97
FT                   /note="Pyrroline-5-carboxylate reductase catalytic N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03807"
FT   DOMAIN          160..264
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         35
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         55
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
FT   BINDING         68..71
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000193-1"
SQ   SEQUENCE   268 AA;  27786 MW;  85648EE5E385110A CRC64;
     MTCDVAVLGT GKMGEALLGG LLRSGWPASG LRATSRRKEH AAALEARHGV PVVDNQEAAS
     WADVLVLAVK PQDMGALLAE IAPALTPATL LVSVAAGLTT GFFEERLPAG TPVVRAMPNT
     AVLVDEGMTV LSGGAHASPY HVDRAGAIFR SVGHTLVVPE SQQDAATALS GSGPAYFYFL
     VEAMTDAGVL LGLPRDKAHE LVVRSAVGGA VMLRDTAEHP VRLREAVTSP AGTTVSAMRE
     LERHGVRAAL MAAIEAARDR SRELSASS
//
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