UniProt: Q58QF6

Database: UniProt
Entry: Q58QF6_WHEAT

LinkDB:  Q58QF6_WHEAT 
Original site:  Q58QF6_WHEAT

All links

Ontology (6)   
   GO (6)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (15)   
   InterPro (12)   
   Pfam (2)   
   PROSITE (1)   
Literature (2)   
   PubMed (2)   
All databases (27)   

Download RDF

ID   Q58QF6_WHEAT            Unreviewed;       716 AA.
AC   Q58QF6;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 111.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate synthase {ECO:0000256|PIRNR:PIRNR036429};
DE   Includes:
DE     RecName: Full=Glutamate 5-kinase {ECO:0000256|PIRNR:PIRNR036429};
DE              Short=GK {ECO:0000256|PIRNR:PIRNR036429};
DE              EC=2.7.2.11 {ECO:0000256|PIRNR:PIRNR036429};
DE     AltName: Full=Gamma-glutamyl kinase {ECO:0000256|PIRNR:PIRNR036429};
DE   Includes:
DE     RecName: Full=Gamma-glutamyl phosphate reductase {ECO:0000256|PIRNR:PIRNR036429};
DE              Short=GPR {ECO:0000256|PIRNR:PIRNR036429};
DE              EC=1.2.1.41 {ECO:0000256|PIRNR:PIRNR036429};
DE     AltName: Full=Glutamate-5-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036429};
DE     AltName: Full=Glutamyl-gamma-semialdehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036429};
GN   ORFNames=CFC21_007633 {ECO:0000313|EMBL:KAF6990442.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EMBL:AAX35536.1};
RN   [1] {ECO:0000313|EMBL:AAX35536.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Ma L., Jia J.;
RT   "Molecular cloning and overexpression P5CS in wheat.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF6990442.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF6990442.1};
RX   PubMed=29069494;
RA   Zimin A.V., Puiu D., Hall R., Kingan S., Clavijo B.J., Salzberg S.L.;
RT   "The first near-complete assembly of the hexaploid bread wheat genome,
RT   Triticum aestivum.";
RL   Gigascience 6:1-7(2017).
RN   [3] {ECO:0000313|EnsemblPlants:TraesCS1B02G290600.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS1B02G290600.2};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [4] {ECO:0000313|EnsemblPlants:TraesCS1B02G290600.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) to UniProtKB.
RN   [5] {ECO:0000313|EMBL:KAF6990442.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAF6990442.1};
RA   Zimin A.V., Puiu D., Shumante A., Alonge M., Salzberg S.L.;
RT   "The second near-complete assembly of the hexaploid bread wheat (Triticum
RT   aestivum) genome.";
RL   Submitted (MAR-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC       osmoregulation in plants. {ECO:0000256|PIRNR:PIRNR036429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC         Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001844,
CC         ECO:0000256|PIRNR:PIRNR036429};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-
CC         glutamyl 5-phosphate + NADPH; Xref=Rhea:RHEA:19541,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58066, ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41;
CC         Evidence={ECO:0000256|ARBA:ARBA00000979,
CC         ECO:0000256|PIRNR:PIRNR036429};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 1/2.
CC       {ECO:0000256|ARBA:ARBA00005185, ECO:0000256|PIRNR:PIRNR036429}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC       5-semialdehyde from L-glutamate: step 2/2.
CC       {ECO:0000256|ARBA:ARBA00004985, ECO:0000256|PIRNR:PIRNR036429}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl
CC       phosphate reductase family. {ECO:0000256|ARBA:ARBA00006300,
CC       ECO:0000256|PIRNR:PIRNR036429}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC       kinase family. {ECO:0000256|ARBA:ARBA00009302,
CC       ECO:0000256|PIRNR:PIRNR036429}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY888045; AAX35536.1; -; mRNA.
DR   EMBL; CM022212; KAF6990442.1; -; Genomic_DNA.
DR   SMR; Q58QF6; -.
DR   STRING; 4565.Q58QF6; -.
DR   PaxDb; 4565-Traes_1BL_31105367B-1; -.
DR   EnsemblPlants; TraesCS1B02G290600.2; TraesCS1B02G290600.2; TraesCS1B02G290600.
DR   Gramene; TraesCS1B02G290600.2; TraesCS1B02G290600.2; TraesCS1B02G290600.
DR   Gramene; TraesCS1B03G0812300.2; TraesCS1B03G0812300.2.CDS; TraesCS1B03G0812300.
DR   Gramene; TraesKAR1B01G0333040.1; cds.TraesKAR1B01G0333040.1; TraesKAR1B01G0333040.
DR   HOGENOM; CLU_016144_0_0_1; -.
DR   OrthoDB; 314297at2759; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000019116; Chromosome 1B.
DR   Proteomes; UP000815260; Chromosome 1B.
DR   ExpressionAtlas; Q58QF6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd04256; AAK_P5CS_ProBA; 1.
DR   CDD; cd07079; ALDH_F18-19_ProA-GPR; 1.
DR   Gene3D; 3.40.1160.10; Acetylglutamate kinase-like; 1.
DR   HAMAP; MF_00412; ProA; 1.
DR   HAMAP; MF_00456; ProB; 1.
DR   InterPro; IPR036393; AceGlu_kinase-like_sf.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR041744; G5K_ProBA.
DR   InterPro; IPR001057; Glu/AcGlu_kinase.
DR   InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR   InterPro; IPR019797; Glutamate_5-kinase_CS.
DR   InterPro; IPR000965; GPR_dom.
DR   InterPro; IPR005766; P5_carboxy_syn.
DR   NCBIfam; TIGR01092; P5CS; 1.
DR   NCBIfam; TIGR00407; proA; 1.
DR   NCBIfam; TIGR01027; proB; 1.
DR   PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036429; P5C_syn; 1.
DR   PRINTS; PR00474; GLU5KINASE.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   SUPFAM; SSF53633; Carbamate kinase-like; 1.
DR   PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR036429};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR036429};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR036429};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650,
KW   ECO:0000256|PIRNR:PIRNR036429};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036429}.
FT   DOMAIN          15..260
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   DOMAIN          291..556
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   716 AA;  77700 MW;  4911CF3C9FFDC00A CRC64;
     MAGADPNRSF MKDVKRIIIK VGTAVITRND GRLALGRIGA LCEQVKDLNA QGYEVIMVTS
     GAVGVGRQRL RYRKLVNSSF ADLQKPQMEL DGKACAAVGQ SGLMALYDML FTQLDVSSSQ
     LLVTDSDFDN SNFRERLRET VESLLELRVI PIFNENDAIS TRKAPYEDSS GIFWDNDSLA
     GLLALELKAD LLVLLSDVDG LYSGPPSEPS SKLIHTYIKE KHYHEITFGD KSRVGRGGMT
     AKVQAAVWAS TGGVPVVITS GCASQSLVKV LRGEKIGTLF HKNASLWEPS KETSVREMAV
     AARDCSRRLQ NLSSEERKKI LLDVADALEA NEDLIRSENE ADLAAAHEAG YESALVSRLT
     LKPGKIASLA KSVRTLANME DPINEILKRT EVADGLVLEK TSCPLGVLLI IFESRPDALV
     QIASLAIRSG NGLLLKGGKE AMRSNAILHK VITNAIPDNV GEKLIGLITT RDEIADLLKH
     DDVIDLVIPR GSNKLVAQIK SSTKIPVLGH ADGVCHVYID KSADMDMAKR IVMDAKIDYP
     AACNAMETLL VHKDLMKTPE LNDILVALKT AGVNLYCGPV AHKVLGYPKA DSLHLEYSSM
     ACTVEIVDDV QSAIDHIHRY GSAHTDCVVT TDDKVAETFL RQVDSAAVLY NASTRFSDGA
     RFGLGAEVGI STGRIHARGP VGVEGLLTTR WLLRGKGQVV NGDKDVEYTH KSLPLQ
//

DBGET integrated database retrieval system