ID M4AJS3_XIPMA Unreviewed; 794 AA.
AC M4AJS3;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 48.
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};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000014717.2, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000014717.2}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000014717.2};
RG Ensembl;
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 AlphaFoldDB; M4AJS3; -.
DR STRING; 8083.ENSXMAP00000014717; -.
DR Ensembl; ENSXMAT00000014737.2; ENSXMAP00000014717.2; ENSXMAG00000014695.2.
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR GeneTree; ENSGT00500000044903; -.
DR HOGENOM; CLU_016144_0_0_1; -.
DR InParanoid; M4AJS3; -.
DR OMA; MGHAEGI; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000002852; Unassembled WGS sequence.
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:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniRule.
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 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; 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; 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 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:UP000002852};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036429}.
FT DOMAIN 79..333
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
SQ SEQUENCE 794 AA; 87440 MW; C055F011E9FDD8A4 CRC64;
MFTPPFLCRI GCVHRCRPCQ CILQMQQVAH FHSHLWIHPA AVKMSRQVSP QLISLLFTEF
SNRVHGSSFA HRGELRKAKR IVVKLGSAVV TRGDECGLAL GRLASIVEQV SLQWKVSVVF
LTAVAFGKQR LRHEILLSQS VRQALHSGNG LHKEMFVPAL EARACAAAGQ SGLMALYEAM
FTQYSTCTAQ VLVTNLDFHD DEKRQNLNST LRELLRMNIV PIINTNDAVV PPPEPNSDLH
GVNVISIKDN DSLAARLAVE MKADLLIALS DVEGLYNSPP GTNDAKLIDI FYSGDQQSIT
YGTKSRVGIG GMEAKVKAAL WALQGGTSVV IANGTNPKIT GQVITDIVEG KKVGTFFSEV
KPAGPSVEEQ TEMARNSGRI LASLHPDQRS EIICHLAELL TERKNEILAA NKMDMKMAVR
RLPSAMLKRL SLSSVKLSSL AVGLRQIAMA AQDSVGRVVR RTRVAPSLEL EQVTVPIGVL
LVIFEARPDC LPQACFWNGG KEAANTNRVL HQLTQEALSL HGVREAVQMV NTHEEVEDLC
RLDKMIDLIV PRGSSQLVRD IQRAAKGIPV LGHSEGICHV YVDADADVDK VIKIVRDSKC
DYPAACNSME TLLIHREILR TPMFDKIIEM LRIEQVKIHS GPRFASYLTF SPSEASSLRT
EYSDLECCLE VVDGVEEAVE HIHKYGSSHT DVIVTENKET AERFLQQLDS ACVFWNASSR
FADGYRFGLG AEVGISTARI HARGPVGLEG LLTTKWVLRG DGHTVADFSE SGSRKYLHEN
IPVEQNLTGH RDSN
//
