ID A0A022PWT6_ERYGU Unreviewed; 667 AA.
AC A0A022PWT6;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 13-SEP-2023, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EYU19949.1};
GN ORFNames=MIMGU_mgv1a002084mg {ECO:0000313|EMBL:EYU19949.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU19949.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU19949.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC -!- FUNCTION: P5CS plays a key role in proline biosynthesis, leading to
CC osmoregulation in plants. {ECO:0000256|ARBA:ARBA00003492}.
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 -!- 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 -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005185}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004985}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma-glutamyl
CC phosphate reductase family. {ECO:0000256|ARBA:ARBA00006300}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the glutamate 5-
CC kinase family. {ECO:0000256|ARBA:ARBA00009302}.
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DR EMBL; KI632289; EYU19949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A022PWT6; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000030748; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004350; F:glutamate-5-semialdehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; IPR020593; G-glutamylP_reductase_CS.
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.
DR PROSITE; PS01223; PROA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000030748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..260
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 297..557
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 667 AA; 72206 MW; 8FDCA231A5C2B809 CRC64;
MEALDSARAF VKDVKRVVIK VGTAVVTRAD GRLALGRLGS LCEQIHELNM QGYEVILVTS
GAVGVGRQRL RYRRLVNSSF ADLQKPQVEL DGKACAAVGQ NGLMALYDTL FSQLDMTSAQ
LLVTDNDFRD TEFRKQLNET VVSLLSLKVV PIFNENDAVS TRRAPYEDSS GIFWDNDSLA
ALLALELKAD LLVLLSDVDG LYSGPPSDPH SELIQTYIKE RHEGGITFGD KSRVGRGGMT
AKVKAAVHAA DAGIPVVITS GFAAGNIIKV LNGQLVGTLF HRDAIKWVSQ GQFGARDMAV
AARESSRRLQ AMPSEERSKI LLDVADALEA SEKLIIAENE ADVSEAQLAG YDKSLISRLA
LKPGKVSSLA NSIRVLANME EPVGRVLKRT ELSEGFILEK MSSPLGVLLI IFESRPDALV
QIASLAIRSG NGLLLKGGKE ARRSNAILHK IITSAIPKNI GERLIGLVTS RDEIPELLKL
DDVIDLVIPR GSNKLVSQIK ASTKIPVLGH ADGICHVYVD KSANIDMAKQ IVLDAKTDYP
AACNAMETLL VHKDLAQTGG LNELIVELQI KGVTIFGGPR ASSLLNIPEA RSLHHEYSSL
SCTVEVVDDV NAAIDHIHEH GSGHTDCIIT EDREVADVFL RLVDSAAVFH NASTRFSDGF
RFGLGWH
//
