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Reviewed, UniProtKB/Swiss-Prot P0C1E4 (P5CR_CORGL)

Last modified November 25, 2008. Version 20. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Pyrroline-5-carboxylate reductase
      Short name=P5C reductase
      Short name=P5CR
    EC=1.5.1.2
Gene names
Name: proC
Ordered Locus Names: Cgl0410, cg0490
OrganismCorynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP]
Taxonomic identifier1718 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-proline from L-glutamate 5-semialdehyde: step 1/1.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

Belongs to the pyrroline-5-carboxylate reductase family.

Ontologies

Keywords

   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome

Gene Ontology (GO)

   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

proline biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionbinding

Inferred from electronic annotation. Source: InterPro

pyrroline-5-carboxylate reductase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 270270Pyrroline-5-carboxylate reductase
PRO_0000187288

Sequences

Sequence LengthMass (Da)Tools
P0C1E4-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 85F50E233D94158F

FASTA27028,242
        10         20         30         40         50         60 
MTTIAVIGGG QIGEALVSGL IAANMNPQNI RVTNRSEERG QELRDRYGIL NMTDNSQAAD 

        70         80         90        100        110        120 
EADVVFLCVK PKFIVEVLSE ITGTLDNNSA QSVVVSMAAG ISIAAMEESA SAGLPVVRVM 

       130        140        150        160        170        180 
PNTPMLVGKG MSTVTKGRYV DAEQLEQVKD LLSTVGDVLE VAESDIDAVT AMSGSSPAYL 

       190        200        210        220        230        240 
FLVTEALIEA GVNLGLPRAT AKKLAVASFE GAATMMKETG KEPSELRAGV SSPAGTTVAA 

       250        260        270 
IRELEESGIR GAFYRAAQAC ADRSEELGKR 

« Hide

References

[1]"Complete genomic sequence of Corynebacterium glutamicum ATCC 13032."
Nakagawa S.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.
[2]"The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins."
Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. expand/collapse author list , Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O., Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.
J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025.

Cross-references

Sequence databases

BA000036 Genomic DNA. Translation: BAB97803.1.
BX927149 Genomic DNA. Translation: CAF19126.1.
RefSeqNP_599658.1.
YP_224712.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID1021078.
3343255.
GenomeReviewsGene locus cg0490 in contig BX927147_GR.
Gene locus Cgl0410 in contig BA000036_GR.
KEGGcgb:cg0490.
cgl:NCgl0398.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0C1E4.

Enzyme and pathway databases

BioCycCGLU196627-1:CG0490-MON.

Family and domain databases

InterProIPR016040. NAD(P)-bd.
IPR004455. NADP_OxRdtase_F420.
IPR000304. P5CR.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR11645. P5CR. 1 hit.
PfamPF03807. F420_oxidored. 1 hit.
[Graphical view]
PIRSFPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
TIGRFAMsTIGR00112. proC. 1 hit.
PROSITEPS00521. P5CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameP5CR_CORGL
AccessionPrimary (citable) accession number: P0C1E4
Secondary accession number(s): P46540
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: May 16, 2006
Last modified: November 25, 2008
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents