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
	OrderedLocusNames:	Os05g0455500, LOC_Os05g38150
	ORFNames:	OJ1651_D06.9

From

Oryza sativa subsp. japonica (Rice)

[TaxID: 39947]

Taxonomy

Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade; Ehrhartoideae; Oryzeae; Oryza.

Protein existence

2: Evidence at transcript level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Akibare; DOI=10.1023/A:1005702408601; PubMed=9106509 [NCBI, ExPASy, EBI, Israel, Japan] Igarashi Y., Yoshiba Y., Sanada Y., Yamaguchi-Shinozaki K., Wada K., Shinozaki K.; "Characterization of the gene for delta1-pyrroline-5-carboxylate synthetase and correlation between the expression of the gene and salt tolerance in Oryza sativa L."; Plant Mol. Biol. 33:857-865(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. Tainung 71; Huang T.-C., Chuang H.-S., Yen T.-Y., Huang Y.-W., Wu M.-L.; "Nucleotide sequence of delta-1-pyrroline-5-carboxylate synthetase."; Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=cv. Nipponbare; DOI=10.1007/s00438-005-0039-y; PubMed=16261349 [NCBI, ExPASy, EBI, Israel, Japan] Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J., Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F., Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.; "A fine physical map of the rice chromosome 5."; Mol. Genet. Genomics 274:337-345(2005).

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

D49714; BAA19916.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY574031; AAS89034.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC111016; AAU90213.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T03695; T03695.

NP_001055723.1; -.

3D structure databases

HSSP

Q9WYC9; 1O20. [HSSP ENTRY / PDB]

ModBase

O04226.

Organism-specific databases

Gramene

O04226; -.

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.

Genome annotation databases

GeneID

4338979; -.

KEGG

osa:4338979; -.

Other

ProtoNet

O04226.

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`	`1 716`	`716`	`Delta-1-pyrroline-5-carboxylate synthetase.`	`PRO_0000109777`
`REGION`	`1 296`	`296`	`Glutamate 5-kinase.`
`REGION`	`297 716`	`420`	`Gamma-glutamyl phosphate reductase.`
`CONFLICT`	`173 173`		`F -> S (in Ref. 2; AAS89034).`
`CONFLICT`	`488 488`		`I -> T (in Ref. 1; BAA19916).`
`CONFLICT`	`500 500`		`K -> E (in Ref. 2; AAS89034).`
`CONFLICT`	`530 530`		`H -> L (in Ref. 1; BAA19916).`
`CONFLICT`	`537 537`		`I -> T (in Ref. 1; BAA19916).`

Sequence information

Length: 716 AA [This is the length of the unprocessed precursor]

Molecular weight: 77745 Da [This is the MW of the unprocessed precursor]

CRC64: F8D3C7D9449CFA64 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASVDPSRSF VRDVKRVIIK VGTAVVSRQD GRLALGRVGA LCEQVKELNS LGYEVILVTS 

        70         80         90        100        110        120 
GAVGVGRQRL RYRKLVNSSF ADLQKPQMEL DGKACAAVGQ SGLMALYDML FNQLDVSSSQ 

       130        140        150        160        170        180 
LLVTDSDFEN PKFREQLTET VESLLDLKVI PIFNENDAIS TRKAPYEDSS GIFWDNDSLA 

       190        200        210        220        230        240 
GLLALELKAD LLILLSDVDG LYSGPPSEPS SKIIHTYIKE KHQQEITFGD KSRVGRGGMT 

       250        260        270        280        290        300 
AKVKAAVLAS NSGTPVVITS GFENRSILKV LHGEKIGTLF HKNANLWESS KDVSTREMAV 

       310        320        330        340        350        360 
AARDCSRHLQ NLSSEERKKI LLDVADALEA NEDLIRSENE ADVAAAQVAG YEKPLVARLT 

       370        380        390        400        410        420 
IKPGKIASLA KSIRTLANME DPINQILKKT EVADDLVLEK TSCPLGVLLI VFESRPDALV 

       430        440        450        460        470        480 
QIASLAIRSG NGLLLKGGKE AIRSNTILHK VITDAIPRNV GEKLIGLVTT RDEIADLLKL 

       490        500        510        520        530        540 
DDVIDLVIPR GSNKLVSQIK ASTKIPVLGH ADGICHVYID KSADMDMAKH IVMDAKIDYP 

       550        560        570        580        590        600 
AACNAMETLL VHKDLMKSPG LDDILVALKT EGVNIYGGPI AHKALGFPKA VSFHHEYSSM 

       610        620        630        640        650        660 
ACTVEFVDDV QSAIDHIHRY GSAHTDCIVT TDDKVAETFL RRVDSAAVFH NASTRFSDGA 

       670        680        690        700        710 
RFGLGAEVGI STGRIHARGP VGVEGLLTTR WILRGRGQVV NGDKDVVYTH KSLPLQ

O04226 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