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Q9UT44 (PROA_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable gamma-glutamyl phosphate reductase

Short name=GPR
EC=1.2.1.41
Alternative name(s):
Glutamate-5-semialdehyde dehydrogenase
Short name=GSA dehydrogenase
Glutamyl-gamma-semialdehyde dehydrogenase
Gene names
Name:pro1
ORF Names:SPAC821.11
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate By similarity.

Catalytic activity

L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH.

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 2/2.

Sequence similarities

Belongs to the gamma-glutamyl phosphate reductase family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processproline biosynthetic process

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamate-5-semialdehyde dehydrogenase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Probable gamma-glutamyl phosphate reductase
PRO_0000189823

Sequences

Sequence LengthMass (Da)Tools
Q9UT44 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 9F823DD58A2B46E0

FASTA45148,707
        10         20         30         40         50         60 
MSLEENVKEA KNAFNILQTL SVEDRDDALD KIVEELRIKK SEVLAANAED MKAAKLLAES 

        70         80         90        100        110        120 
GKLSSSMVKR LDLSSSDKYD SMVQGVLDVK SLPDPLGRVT YARSLDDGLD LYKVSCPVGL 

       130        140        150        160        170        180 
LLVIFEARPE VIINITSLAI KSGNAVVLKG GTESAKSFAA LSNVVRSALG KSKVPQAAVQ 

       190        200        210        220        230        240 
LVQSREEVSQ LLKLDEYIDL VIPRGSTNLV RHIKDNTKIP VLGHAAGLCS MYVHEDADME 

       250        260        270        280        290        300 
LASKLVLDGK TDYPAACNAI ETLLINEAVL SSHLPKIAET LTEAKVTLKC DPASLKVLKD 

       310        320        330        340        350        360 
MPKVSALVEP SVDQDYNTEF SDLILAIKTV PSLQSAMQHI NTHGSKHTDC IITSSEAAAN 

       370        380        390        400        410        420 
RFMAGIDASG VYWNASTRFA DGFRYGYGTE VGISTNKIHA RGPMGLDGLT IYKYQLRGNG 

       430        440        450 
QVASSYGVGP GKRAFKHTPI NIDNISQVSK K 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB57445.1.
PIRT41722.
RefSeqNP_593164.1. NM_001018562.1.

3D structure databases

ProteinModelPortalQ9UT44.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9UT44.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC821.11.1; SPAC821.11.1:pep; SPAC821.11.
GeneID2543410.
GenomeReviewsGene locus pro1 in contig CU329670_GR.
KEGGspo:SPAC821.11.
NMPDRfig|4896.1.peg.3134.

Organism-specific databases

GeneDB_SpombeSPAC821.11.

Phylogenomic databases

eggNOGfuNOG07510.
GeneTreeEFGT00050000004343.
HOGENOMHBG318080.
OMAQYPAACN.
OrthoDBEOG47SWPH.

Gene expression databases

ArrayExpressQ9UT44.

Family and domain databases

InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR000965. G-glutamylP_reductase.
IPR020593. G-glutamylP_reductase_CS.
IPR012134. Glu-5-SA_DH.
[Graphical view]
Gene3DG3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 1 hit.
G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 2 hits.
KOK00147.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF000151. GPR. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMsTIGR00407. ProA. 1 hit.
PROSITEPS01223. PROA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROA_SCHPO
AccessionPrimary (citable) accession number: Q9UT44
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: May 1, 2000
Last modified: December 14, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families