Glutamate 5-kinase
     (GK)
     (EC 2.7.2.11)
     (Gamma-glutamyl kinase)
Gamma-glutamyl phosphate reductase
     (GPR)
     (EC 1.2.1.41)
     (Glutamate-5-semialdehyde dehydrogenase)
     (Glutamyl-gamma-semialdehyde dehydrogenase)

Gene name

Name:

P5CS

From

Mesembryanthemum crystallinum (Common ice plant)

[TaxID: 3544]

Taxonomy

Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; Caryophyllales; Aizoaceae; Mesembryanthemum.

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. Michalowski C.B., Quigley-Landreau F., Bohnert H.J.; "Mesembryanthemum crystallinum pyrroline-5-carboxylate synthetase mRNA."; Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.
CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-phosphate.
CATALYTIC ACTIVITY: L-glutamate 5-semialdehyde + phosphate + NADP⁺ = L-glutamyl 5-phosphate + NADPH.
ENZYME REGULATION: Feedback regulated by proline.
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2 .
PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2 .
TISSUE SPECIFICITY: Expressed at high levels in leaves and is inducible in roots subjected to salt stress.
SIMILARITY: In the N-terminal section; belongs to the glutamate 5-kinase family.
SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl phosphate reductase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF067967; AAC18862.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T12258; T12258.

3D structure databases

HSSP

Q9WYC9; 1O20. [HSSP ENTRY / PDB]

ModBase

O65361.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from InterPro).
GO:0004349;	Molecular function: glutamate 5-kinase activity (inferred from electronic annotation from InterPro).
GO:0004350;	Molecular function: glutamate-5-semialdehyde dehydrogenase activity (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006561;	Biological process: proline biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016163; Ald_DHase_C.
IPR016162; Ald_DHase_N.
IPR001048; Asp/Glu/Uridylate_kinase.
IPR000965; Gglut_pp_reduct.
IPR001057; Glu_5kinase.
IPR005766; P5_carboxy_syn.
IPR005715; ProB.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.1160.10; Aa_kinase; 1.
G3DSA:3.40.309.10; Aldehyde_dehydrogenase_C; 1.
G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

Pfam

PF00696; AA_kinase; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF036429; P5C_syn; 1.

PRINTS

PR00474; GLU5KINASE.

TIGRFAMs

TIGR01092; P5CS; 1.
TIGR00407; proA; 1.
TIGR01027; proB; 1.

PROSITE

PS00902; GLUTAMATE_5_KINASE; 1.
PS01223; PROA; 1.

Other

ProtoNet

O65361.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Amino-acid biosynthesis; Kinase; Multifunctional enzyme; NADP; Oxidoreductase; Proline biosynthesis; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 719`	`719`	`Delta-1-pyrroline-5-carboxylate synthetase.`	`PRO_0000109776`
`REGION`	`1 293`	`293`	`Glutamate 5-kinase.`
`REGION`	`294 719`	`426`	`Gamma-glutamyl phosphate reductase.`

Sequence information

Length: 719 AA [This is the length of the unprocessed precursor]

Molecular weight: 77855 Da [This is the MW of the unprocessed precursor]

CRC64: 1510D11AF5559961 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDATRAFVKD VKRVVVKVGT AVVTRSDGRL ALGRLGSLCE QLKELNSDGY EVILVTSGAV 

        70         80         90        100        110        120 
SAGRQRLRFR KLVNSSFADL QKPQVELDGK ACAAVGQNGL MALYDTLFSQ LDLTAAQLLV 

       130        140        150        160        170        180 
TDNDFRDPSF RTQLTETVYQ LLDLKVVPVL NENDAVSTRK APYEDSSGIF WDNDSLAALL 

       190        200        210        220        230        240 
ALELKADLLI LLSDVDGLYN GPPSDPRSKL ISTYVKEKHQ GEITFGDKSR LGRGGMTAKV 

       250        260        270        280        290        300 
KAAVYAAYAG IPVIIASGKA TDNIIKVIDG QCVGTLFHKD AHLWVQVKET GVRDMAVAAR 

       310        320        330        340        350        360 
ESSRRLQAVS SEERKKILLD IADALEANEE KILAENEADV AAAQYAGYDR SLVARLAMNP 

       370        380        390        400        410        420 
DKISSLAKSI RVLADMEEPI GRILKRTEIA DGLILEKTSC PLGVLLIVFE SRPDALVQIA 

       430        440        450        460        470        480 
SLAIRSGNGL LLKGGKEAKR SNAILHKVIT SAIPDKVGEK LIGLVTSRDE IPDLLKLDDV 

       490        500        510        520        530        540 
IDLVIPRGSN KLVSQIKEST RIPVLGHADG ICHVYVDKSA NMDMAKRIVL DAKTDYPAAC 

       550        560        570        580        590        600 
NAMETLLVHK DLAENGGLND LIVDLRTEGV TMFGGPRIDA LQEFNIQATQ TFNREYSSPA 

       610        620        630        640        650        660 
CTVEIVDDVY AAIEHINHHG SAHTDCIIAE DHKVAETFLQ LVDSAAVLHN ASTRFCDGFR 

       670        680        690        700        710 
FGLGAEVGIS TSRIHARGPV GVEGLLTTRW VLKGSGQVVH GDKGVVYTHK DLPLVAQNS

O65361 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools