Escherichia coli K-12 substr. MG1655 Enzyme: pyrroline-5-carboxylate reductase

Gene: proC Accession Numbers: EG10769 (EcoCyc), b0386, ECK0381

Synonyms: pro(3), Pro2, pro3, PCA reductase

Regulation Summary Diagram: ?

Regulation summary diagram for proC

Subunit composition of pyrroline-5-carboxylate reductase = [ProC]10
         pyrroline-5-carboxylate reductase monomer = ProC

The final step in the L-proline biosynthesis I pathway, the reduction of (S)-1-pyrroline-5-carboxylate (PCA) to L-proline, is catalyzed by NADPH-dependent pyrroline- 5-carboxylic acid reductase (PCA reductase) [Deutch82].

Purified PCA reductase mediates the conversion of PCA to proline but not the reverse reaction. The enzyme could use either NADH or NADPH as the reducing agent, but the reaction is 7-fold more active with NADPH [Rossi77]. All KMs listed below were determined using a racemic mixture of D- and L-pyrroline-5-carboxylate and may thus overestimate the KM for ProC, as the enzyme is specific for the L-isomer [Rossi77].

While the enzyme synthesis is not repressed by proline, the enzyme activity is inhibited by the reaction end products, proline and NADP [Rossi77].

Locations: cytosol

Map Position: [404,059 <- 404,868] (8.71 centisomes, 31°)
Length: 810 bp / 269 aa

Molecular Weight of Polypeptide: 28.145 kD (from nucleotide sequence), 26.5 kD (experimental) [Deutch82 ]

Molecular Weight of Multimer: 320 kD (experimental) [Rossi77]

Unification Links: ASAP:ABE-0001338 , CGSC:362 , DIP:DIP-47863N , EchoBASE:EB0762 , EcoGene:EG10769 , EcoliWiki:b0386 , ModBase:P0A9L8 , OU-Microarray:b0386 , PortEco:proC , PR:PRO_000023598 , Pride:P0A9L8 , Protein Model Portal:P0A9L8 , RefSeq:NP_414920 , RegulonDB:EG10769 , SMR:P0A9L8 , String:511145.b0386 , UniProt:P0A9L8

Relationship Links: InterPro:IN-FAMILY:IPR000304 , InterPro:IN-FAMILY:IPR008927 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR028939 , InterPro:IN-FAMILY:IPR029036 , Panther:IN-FAMILY:PTHR11645 , Pfam:IN-FAMILY:PF03807 , Pfam:IN-FAMILY:PF14748 , Prosite:IN-FAMILY:PS00521

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006561 - proline biosynthetic process Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0055129 - L-proline biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004735 - pyrroline-5-carboxylate reductase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Deutch82, Rossi77]
GO:0050661 - NADP binding Inferred from experiment [Deutch82]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids proline

Essentiality data for proC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 2]
M9 medium with 1% glycerol No 37 Aerobic 7.2 0.35 No [Joyce06]
MOPS medium with 0.4% glucose No 37 Aerobic 7.2 0.22 No [Baba06, Comment 1]
No [Feist07, Comment 3]

Last-Curated ? 14-Sep-2006 by Shearer A , SRI International

Enzymatic reaction of: pyrroline-5-carboxylate reductase

Synonyms: P5CR, P5C reductase, δ(1)-pyrroline-5-carboxylate reductase, PCA reductase, L-proline:NADP+ 5-oxidoreductase

EC Number:

(S)-1-pyrroline-5-carboxylate + NAD(P)H + 2 H+ <=> L-proline + NAD(P)+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown. [Rossi77]

Alternative Products for L-proline: L-thiazolidine-4-carboxylate [Deutch01 ] , 3,4-dehydroproline [Deutch01 ]

In Pathways: L-proline biosynthesis I

Cofactors or Prosthetic Groups: NADPH [Deutch82]

Inhibitors (Competitive): NADP+ [Rossi77] , L-proline [Rossi77]

Inhibitors (Unknown Mechanism): p-chloromercuribenzoate [Rossi77]

Primary Physiological Regulators of Enzyme Activity: NADP+ , L-proline

Kinetic Parameters:

Km (μM)

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b0386 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10769; confirmed by SwissProt match.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Deutch01: Deutch CE, Klarstrom JL, Link CL, Ricciardi DL (2001). "Oxidation of L-thiazolidine-4-carboxylate by delta1-pyrroline-5-carboxylate reductase in Escherichia coli." Curr Microbiol 42(6);442-6. PMID: 11381339

Deutch82: Deutch AH, Smith CJ, Rushlow KE, Kretschmer PJ (1982). "Escherichia coli delta 1-pyrroline-5-carboxylate reductase: gene sequence, protein overproduction and purification." Nucleic Acids Res 1982;10(23);7701-14. PMID: 6296787

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

Rossi77: Rossi JJ, Vender J, Berg CM, Coleman WH (1977). "Partial purification and some properties of delta1-pyrroline-5-carboxylate reductase from Escherichia coli." J Bacteriol 1977;129(1);108-14. PMID: 12133

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Other References Related to Gene Regulation

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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