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Database: UniProt
Entry: A0A1U8BWT1_MESAU
LinkDB: A0A1U8BWT1_MESAU
Original site: A0A1U8BWT1_MESAU 
ID   A0A1U8BWT1_MESAU        Unreviewed;       795 AA.
AC   A0A1U8BWT1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   Name=Aldh18a1 {ECO:0000313|RefSeq:XP_012971712.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_012971712.1};
RN   [1] {ECO:0000313|RefSeq:XP_012971712.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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}.
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DR   RefSeq; XP_012971712.1; XM_013116258.2.
DR   AlphaFoldDB; A0A1U8BWT1; -.
DR   STRING; 10036.ENSMAUP00000023577; -.
DR   GeneID; 101828502; -.
DR   KEGG; maua:101828502; -.
DR   CTD; 5832; -.
DR   OrthoDB; 314297at2759; -.
DR   UniPathway; UPA00098; UER00359.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0019240; P:citrulline biosynthetic process; IEA:Ensembl.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:Ensembl.
DR   GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006592; P:ornithine biosynthetic process; IEA:Ensembl.
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; IPR020593; G-glutamylP_reductase_CS.
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   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   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:UP000189706};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036429}.
FT   DOMAIN          71..329
FT                   /note="Aspartate/glutamate/uridylate kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00696"
FT   DOMAIN          363..625
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
SQ   SEQUENCE   795 AA;  87164 MW;  1FCB1D3DFE3D67E8 CRC64;
     MLRYMHRSGF QPFSQRLLPR VQSVAVPRSH GVQPSAVRHV RSWSNIPFIT VPLSRAHGKP
     FAHRSELKHA KRIVVKLGSA VVTRGDECGL ALGRLASIVE QVSVLQNQGR EMMLVTSGAV
     AFGKQRLRHE ILLSQSVRQA LHSGQNQLKE MAVPVLEARA CAAAGQSGLM ALYEAMFTQY
     SICAAQILVT NLDFHDEQKR RNLNGTLHEL LRMNIVPIVN TNDAVVPPAE PNSDLQGVNV
     ISVKDNDSLA ARLAVEMKTD LLIVLSDVEG LFDSPPGSDD AKLIDIFYPG DQQSVTFGTK
     SRVGLGGMEA KVKAALWALQ GGTSVVIANG THPKVSGHVI TDIVEGKKVG TFFSEVKPAG
     PTVEQQGEMA RSGGRMLATL EPEQRAEIIH HLADLLTDQR EEILLANKKD LEEAEGRLAT
     PLLKRLSLST SKLNSLAIGL RQIAASSQDS VGRVLRRTRI AKNLELEQVT VPIGVLLVIF
     ESRPDCLPQV AALAIASGNG LLLKGGKEAA HSNRILHRLT QEALSIHGVK DAIQLVNTRE
     EVEDLCRLDK IIDLIIPRGS SQLVRDIQKA AKGIPVMGHS EGICHMYVDS EASVDKVTRL
     VRDSKCEYPA ACNALETLLI HRDLLRTPVF DQIIDMLRVE QVKIHAGPKF ASYLTFSPSE
     VKSLRIEYGD LEVCIEVVDS VQEAIDHIHK YGSSHTDVIV TENEKTAEFF LQHVDSACVF
     WNASTRFSDG YRFGLGAEVG ISTSRIHARG PVGLEGLLTT KWLLRGQDHV VSDFSEHGSL
     KYLHENLPVP QRNFS
//
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