Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Pyrroline-5-carboxylate reductase

Gene

proC

Organism
Streptococcus pyogenes serotype M1
Status
Unreviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline.UniRule annotation

Catalytic activityi

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

Pathwayi: L-proline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-proline from L-glutamate 5-semialdehyde.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. Pyrroline-5-carboxylate reductase (proC)
This subpathway is part of the pathway L-proline biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-proline from L-glutamate 5-semialdehyde, the pathway L-proline biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei31 – 311NADPCombined sources
Binding sitei35 – 351NADPCombined sources
Binding sitei51 – 511NADPCombined sources
Binding sitei88 – 881NADP; via amide nitrogenCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi10 – 112NADPCombined sources
Nucleotide bindingi65 – 673NADPCombined sources
Nucleotide bindingi219 – 2213NADPCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

OxidoreductaseUniRule annotationImported

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesisUniRule annotation

Keywords - Ligandi

NADPUniRule annotationCombined sources, Nucleotide-bindingCombined sources

Enzyme and pathway databases

BioCyciSPYO160490:GJ81-129-MONOMER.
SPYO293653:GHFC-146-MONOMER.
UniPathwayiUPA00098; UER00361.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrroline-5-carboxylate reductaseUniRule annotation (EC:1.5.1.2UniRule annotation)
Short name:
P5C reductaseUniRule annotation
Short name:
P5CRUniRule annotation
Alternative name(s):
PCA reductaseUniRule annotation
Gene namesi
Name:proCUniRule annotationImported
Ordered Locus Names:SPy_0112Imported
OrganismiStreptococcus pyogenes serotype M1Imported
Taxonomic identifieri301447 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
Proteomesi
  • UP000000750 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CytoplasmUniRule annotation

PTM / Processingi

Proteomic databases

PaxDbiQ9A1S9.

Interactioni

Protein-protein interaction databases

STRINGi160490.SPy_0112.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AHRX-ray2.15A/B/C/D/E1-256[»]
2AMFX-ray2.20A/B/C/D/E1-256[»]
ProteinModelPortaliQ9A1S9.
SMRiQ9A1S9. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 8988F420_oxidoredInterPro annotationAdd
BLAST
Domaini152 – 256105P5CR_dimerInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the pyrroline-5-carboxylate reductase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105II7. Bacteria.
COG0345. LUCA.
HOGENOMiHOG000230247.
KOiK00286.
OMAiRTFNEHQ.
OrthoDBiEOG6JB16S.

Family and domain databases

Gene3Di1.10.3730.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01925. P5C_reductase.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR029036. P5CR_dimer.
IPR028939. ProC_N.
IPR000304. Pyrroline-COOH_reductase.
[Graphical view]
PANTHERiPTHR11645. PTHR11645. 1 hit.
PfamiPF03807. F420_oxidored. 1 hit.
PF14748. P5CR_dimer. 1 hit.
[Graphical view]
PIRSFiPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00112. proC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9A1S9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKIGIIGVGK MASAIIKGLK QTPHELIISG SSLERSKEIA EQLALPYAMS
60 70 80 90 100
HQDLIDQVDL VILGIKPQLF ETVLKPLHFK QPIISMAAGI SLQRLATFVG
110 120 130 140 150
QDLPLLRIMP NMNAQILQSS TALTGNALVS QELQARVRDL TDSFGSTFDI
160 170 180 190 200
SEKDFDTFTA LAGSSPAYIY LFIEALAKAG VKNGIPKAKA LEIVTQTVLA
210 220 230 240 250
SASNLKTSSQ SPHDFIDAIC SPGGTTIAGL MELERLGLTA TVSSAIDKTI

DKAKSL
Length:256
Mass (Da):27,306
Last modified:June 1, 2001 - v1
Checksum:i9EF15B4BD6021033
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK33229.1.
RefSeqiNP_268508.1. NC_002737.2.

Genome annotation databases

EnsemblBacteriaiAAK33229; AAK33229; SPy_0112.
GeneIDi900451.
KEGGispy:SPy_0112.
PATRICi19714041. VBIStrPyo79812_0096.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004092 Genomic DNA. Translation: AAK33229.1.
RefSeqiNP_268508.1. NC_002737.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AHRX-ray2.15A/B/C/D/E1-256[»]
2AMFX-ray2.20A/B/C/D/E1-256[»]
ProteinModelPortaliQ9A1S9.
SMRiQ9A1S9. Positions 1-256.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi160490.SPy_0112.

Proteomic databases

PaxDbiQ9A1S9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK33229; AAK33229; SPy_0112.
GeneIDi900451.
KEGGispy:SPy_0112.
PATRICi19714041. VBIStrPyo79812_0096.

Phylogenomic databases

eggNOGiENOG4105II7. Bacteria.
COG0345. LUCA.
HOGENOMiHOG000230247.
KOiK00286.
OMAiRTFNEHQ.
OrthoDBiEOG6JB16S.

Enzyme and pathway databases

UniPathwayiUPA00098; UER00361.
BioCyciSPYO160490:GJ81-129-MONOMER.
SPYO293653:GHFC-146-MONOMER.

Family and domain databases

Gene3Di1.10.3730.10. 1 hit.
3.40.50.720. 1 hit.
HAMAPiMF_01925. P5C_reductase.
InterProiIPR008927. 6-PGluconate_DH_C-like.
IPR016040. NAD(P)-bd_dom.
IPR029036. P5CR_dimer.
IPR028939. ProC_N.
IPR000304. Pyrroline-COOH_reductase.
[Graphical view]
PANTHERiPTHR11645. PTHR11645. 1 hit.
PfamiPF03807. F420_oxidored. 1 hit.
PF14748. P5CR_dimer. 1 hit.
[Graphical view]
PIRSFiPIRSF000193. Pyrrol-5-carb_rd. 1 hit.
SUPFAMiSSF48179. SSF48179. 1 hit.
SSF51735. SSF51735. 1 hit.
TIGRFAMsiTIGR00112. proC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700294 / SF370 / Serotype M1Imported.
  2. "Crystal structures of delta1-pyrroline-5-carboxylate reductase from human pathogens Neisseria meningitides and Streptococcus pyogenes."
    Nocek B., Chang C., Li H., Lezondra L., Holzle D., Collart F., Joachimiak A.
    J. Mol. Biol. 354:91-106(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH NADP.

Entry informationi

Entry nameiQ9A1S9_STRP1
AccessioniPrimary (citable) accession number: Q9A1S9
Secondary accession number(s): Q491K3
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.