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Protein Overview: PRO2

General Information:
Name(s) found: PRO2 / YOR323C [SGD]
Description(s) found:
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  • gi|940855|emb|CAA62179.1| orf 06155 [Saccharomyces cerevisiae] [NCBI NR]
  • gi|6324899|ref|NP_014968.1| Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis; Pro2p [Saccharomyces cerevisiae] [NCBI NR]
  • gi|51013419|gb|AAT93003.1| YOR323C [Saccharomyces cerevisiae] [NCBI NR]
  • pir||S58334 glutamate-5-semialdehyde dehydrogenase (EC 1.2.1.41) - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|1709784|sp|P54885.1|PROA_YEAST RecName: Full=Gamma-glutamyl phosphate reductase; Short=GPR; AltName: Full=Glutamate-5-semialdehyde dehydrogenase; Short=GSA dehydrogenase; AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase [NCBI NR]
  • gi|1420708|emb|CAA99643.1| PRO2 [Saccharomyces cerevisiae] [NCBI NR]
  • gi|1171206|gb|AAA86261.1| gamma-glutamyl phosphate reductase [NCBI NR]
  • Gamma-glutamyl phosphate reductase OS=Saccharomyces cerevisiae GN=PRO2 PE=1 SV=1 [Swiss-Prot]
  • PRO2 Gamma-glutamyl phosphate reductase [mips]
  • Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis [SGD]
  • (P54885) Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase) (GSA dehydrogenase) [4932.FASTACCERV.txt]
  • Chr XV from 922898-921528, reverse complement [hmr_yeast5_DM3-1_pombe.fasta]
  • Chr XV from 921527-922897, reverse complement [yeastorf3.fasta]
  • Chr XV from 921528-922898, reverse complement [yeastorf4.fasta]
  • PRO2, Chr XV from 921527-922897, reverse complement [yeast_orfs2]
  • PRO2 SGDID:S0005850, Chr XV from 922900-921530, reverse complement, Verified ORF [yeastflysequest.fasta]
  • Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis [Saccharomyces cerevisiae]gi|51013419|gb|AAT93003.1| YOR323C [Saccharomyces cerevisiae]gi|1420708|emb|CAA99643.1| PRO2 [Saccharomyces cerevisiae]gi|940855|emb|CAA6217 [nrdb_11152004_Chlamydomonas]
  • PRO2 SGDID:S000005850, Chr XV from 922900-921530, reverse complement, Verified ORF, "Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis" [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • PRO2 SGDID:S000005850, Chr XV from 922902-921532, reverse complement, Verified ORF, "Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis" [yeast-contam.fasta]
  • YOR323C [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • gamma-glutamyl phosphate reductase [nr-271106-contam.fasta]
  • orf 06155 [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Gamma-glutamyl phosphate reductase (GPR) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase) (GSA dehydrogenase) [nr-271106-contam.fasta]
  • Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis; Pro2p [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • PRO2 [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • [chemostatdb.fasta]
  • Gamma-glutamyl phosphate reductase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PRO2 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • PRO2 SGDID:S000005850, Chr XV from 922905-921535, Genome Release 64-1-1, reverse complement, Verified ORF, "Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis" [yeast-030211-contam.fasta]
  • PRO2 SGDID:S000005850, Chr XV from 922905-921535, Genome Release 64-2-1, reverse complement, Verified ORF, "Gamma-glutamyl phosphate reductase; catalyzes the second step in proline biosynthesis" [20141208_orf_trans.fasta]
  • YOR323C SGDID:S000005850, Chr XV from 922905-921535, Genome Release 64-1-1, reverse complement, Verified ORF, "Gamma-glutamyl phosphate reductase, catalyzes the second step in proline biosynthesis" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 456 amino acids

    Gene Ontology:
    Cellular Component: nucleus [IDALink to PubMed article]
    cytoplasm [IDALink to PubMed articleLink to PubMed article]
    Biological Process: proline biosynthetic process [IDALink to PubMed article][TASLink to PubMed article]
    Molecular Function: glutamate-5-semialdehyde dehydrogenase activity [IDALink to PubMed article][IGILink to PubMed article]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MSSSQQIAKN ARKAGNILKT ISNEGRSDIL YKIHDALKAN AHAIEEANKI DLAVAKETGL  60
   61 ADSLLKRLDL FKGDKFEVML QGIKDVAELE DPVGKVKMAR ELDDGLTLYQ VTAPVGVLLV 120
  121 IFESRPEVIA NITALSIKSG NAAILKGGKE SVNTFREMAK IVNDTIAQFQ SETGVPVGSV 180
  181 QLIETRQDVS DLLDQDEYID LVVPRGSNAL VRKIKDTTKI PVLGHADGIC SIYLDEDADL 240
  241 IKAKRISLDA KTNYPAGCNA METLLINPKF SKWWEVLENL TLEGGVTIHA TKDLKTAYFD 300
  301 KLNELGKLTE AIQCKTVDAD EEQDFDKEFL SLDLAAKFVT STESAIQHIN THSSRHTDAI 360
  361 VTENKANAEK FMKGVDSSGV YWNASTRFAD GFRYGFGAEV GISTSKIHAR GPVGLDGLVS 420
  421 YQYQIRGDGQ VASDYLGAGG NKAFVHKDLD IKTVTL

    Protein Complex Data

      PUBLICATION TOPOLOGY COCOMPLEXED PROTEINS
    View Details Riffle et al. (2010) (Unpublished Data) PRO2 PTC6
    View Details Krogan NJ, et al. (2006) CIT2 PEP3 PRO2 PTC6
    View Details Gavin AC, et al. (2006) HDA1 HDA2 HDA3 PRO2
    View Details Gavin AC, et al. (2002) CMR1 DNA2 HDA1 HDA2 HDA3 HSC82 KAP95 LCD1 MEC1 MGM101 MLH1 MPH1 MSH2 MSH3 MSH6 OLA1 PGK1 PMS1 PRO2 PTC6 RAD16 RAD52 RFA1 RFA2 RFA3 RIM1 RNH1 RSC8 RVB2 SGS1 SHS1 TIF1, TIF2 TOP3 VAS1 VPS1 YHR122W
    View Details Ho Y, et al. (2002) CDC60 DEF1 FAA1 GDE1 HEF3 KGD1 MDH1 PRO2 PTC6 PYC1 RAD1 TIF1, TIF2 TPS1

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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      PROTEIN(S) PUBLICATION
    View Data PRO2 Huh WK, et al. (2003)

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..226]
    [391..456]    		 PSI-BLAST 824.0103 Gamma-glutamyl phosphate reductase
    2 View Details [227..390] PSI-BLAST 824.0103 Gamma-glutamyl phosphate reductase

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • glutamate-5-semialdehyde dehydrogenase activity
    		•  3.27180265380824 bayes_pls_golite062009
  • catalytic activity
    		•  2.80804701752928 bayes_pls_golite062009
  • 1-pyrroline-5-carboxylate dehydrogenase activity
    		•  2.65686856100363 bayes_pls_golite062009
  • oxidoreductase activity
    		•  2.31275077585879 bayes_pls_golite062009
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors
    		•  2.24875477727877 bayes_pls_golite062009
  • oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
    		•  2.22720948878196 bayes_pls_golite062009
  • oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
    		•  1.6559690223037 bayes_pls_golite062009
  • oxidoreductase activity, acting on the CH-NH group of donors
    		•  1.40606039383065 bayes_pls_golite062009
  • binding
    		•  1.06673666884196 bayes_pls_golite062009
  • histidinol dehydrogenase activity
    		•  0.258030369394064 bayes_pls_golite062009
    2 No functions predicted.


    Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.97

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle