ID A4S3Y2_OSTLU Unreviewed; 420 AA. AC A4S3Y2; DT 15-MAY-2007, integrated into UniProtKB/TrEMBL. DT 15-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 88. DE RecName: Full=Aldehyde dehydrogenase domain-containing protein {ECO:0000259|Pfam:PF00171}; DE Flags: Fragment; GN ORFNames=OSTLU_1184 {ECO:0000313|EMBL:ABO98293.1}; OS Ostreococcus lucimarinus (strain CCE9901). OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales; OC Bathycoccaceae; Ostreococcus. OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO98293.1, ECO:0000313|Proteomes:UP000001568}; RN [1] {ECO:0000313|EMBL:ABO98293.1, ECO:0000313|Proteomes:UP000001568} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO98293.1, RC ECO:0000313|Proteomes:UP000001568}; RX PubMed=17460045; DOI=10.1073/pnas.0611046104; RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N., RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R., RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K., RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M., RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I., RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D., RA Van de Peer Y., Moreau H., Grigoriev I.V.; RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox RT of plankton speciation."; RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate + ATP = L-glutamyl 5-phosphate + ADP; 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:ARBA00049141}; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-glutamyl CC 5-phosphate + NADPH + H(+); Xref=Rhea:RHEA:19541, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57783, ChEBI:CHEBI:58066, CC ChEBI:CHEBI:58274, ChEBI:CHEBI:58349; EC=1.2.1.41; CC Evidence={ECO:0000256|ARBA:ARBA00049024}; 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}. 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; CP000590; ABO98293.1; -; Genomic_DNA. DR RefSeq; XP_001420000.1; XM_001419963.1. DR AlphaFoldDB; A4S3Y2; -. DR STRING; 436017.A4S3Y2; -. DR GeneID; 5003958; -. DR KEGG; olu:OSTLU_1184; -. DR eggNOG; KOG4165; Eukaryota. DR HOGENOM; CLU_030231_1_0_1; -. DR OMA; KTQRYGT; -. DR OrthoDB; 1934954at2759; -. DR UniPathway; UPA00098; UER00360. DR Proteomes; UP000001568; Chromosome 10. 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:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd07079; ALDH_F18-19_ProA-GPR; 1. DR FunFam; 3.40.309.10:FF:000015; Delta-1-pyrroline-5-carboxylate synthase; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 1. DR HAMAP; MF_00412; ProA; 1. 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; IPR020593; G-glutamylP_reductase_CS. DR InterPro; IPR012134; Glu-5-SA_DH. DR InterPro; IPR000965; GPR_dom. DR NCBIfam; NF001221; PRK00197.1; 1. DR NCBIfam; TIGR00407; proA; 1. DR PANTHER; PTHR11063:SF8; DELTA-1-PYRROLINE-5-CARBOXYLATE SYNTHASE; 1. DR PANTHER; PTHR11063; GLUTAMATE SEMIALDEHYDE DEHYDROGENASE; 1. DR Pfam; PF00171; Aldedh; 1. DR PIRSF; PIRSF000151; GPR; 1. DR SUPFAM; SSF53720; ALDH-like; 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:UP000001568}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 3..262 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:ABO98293.1" FT NON_TER 420 FT /evidence="ECO:0000313|EMBL:ABO98293.1" SQ SEQUENCE 420 AA; 45023 MW; 55FB6BB3067E9160 CRC64; LARKARDASR KLQQLPSRER AALLRAVANA LERRESEIQA ANDEDLRRAE SSDDVEEALL QRLKLKPGKV KQLADGARAI ANMEEPIGKP LSAMELAKGL TLTKVTAPLG VLLIIFESRP DALPQIASLA LRTGNGLLLK GGKEAASSNA KLREVIVDEF EAFGVPKECV CLIEGREAVA DLLKLDDVID LVIPRGSNSL VTYIQNNTKI PVLGHADGVV HVYVDKDANV DMAAKCAIDS KIDYPAACNA LETLLIHDDL VANGGAAELM TALRAAGVEL FGGPRGTKEL NLPAAPALRH EYGGMQCSVE LVSSMDNAID YIHANGSAHT DCIITSNQKT ADEFIARVDS ACVFHNASTR FSDGFRFGLG AEVGISTSRI HARGPVGVEG LLTTRCLLRG KGQICNKDKG VEFTHKRLPL //