ID M3ZY47_XIPMA Unreviewed; 779 AA.
AC M3ZY47;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 60.
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|Ensembl:ENSXMAP00000007141.1};
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:ENSXMAP00000007141.1, 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:ENSXMAP00000007141.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000007141.1};
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 RefSeq; XP_005795198.1; XM_005795141.2.
DR STRING; 8083.ENSXMAP00000041480; -.
DR Ensembl; ENSXMAT00000007149.2; ENSXMAP00000007141.1; ENSXMAG00000007107.2.
DR Ensembl; ENSXMAT00000031726.1; ENSXMAP00000041480.1; ENSXMAG00000007107.2.
DR GeneID; 102235369; -.
DR KEGG; xma:102235369; -.
DR eggNOG; KOG1154; Eukaryota.
DR eggNOG; KOG4165; Eukaryota.
DR GeneTree; ENSGT00500000044903; -.
DR HOGENOM; CLU_016144_0_0_1; -.
DR OMA; CSFHHEY; -.
DR OrthoDB; 314297at2759; -.
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 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 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 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 53..311
FT /note="Aspartate/glutamate/uridylate kinase"
FT /evidence="ECO:0000259|Pfam:PF00696"
FT DOMAIN 344..609
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 779 AA; 84810 MW; E9913D76DBE433E4 CRC64;
MFARLALCSR LPSRIRQTNV GPVSIREFSQ AKFLLPRSHG KSFAHRSELK QAKRIVVKLG
SAVVTRGDEC GLALGRLASI VEQVAMLQNQ GREMMIVTSG AVAFGKQRLR HEILLSQSVR
QALHSGQNQL KDISVPVLEA RACAAAGQSG LMALYEAMFT QYSICTAQIL VTNLDFHDEQ
KRRNLNSTLH ELLRMNIVPI INTNDAVVPP PVPNSDLQGV NVISIKDNDS LAARLAVEMK
ADLLIALSDV QGLYDSPPGT DDAKLIDIFY PGDQQSITYG TKSRVGIGGM EAKVKAALWA
LQGGTSVIIA NGTDPKVTGH VITDIVEGKK IGTFFSEVKP AGPTVEQQTE MARHAGRALA
SLLPEQRGEI ICCLAELLTE KKDEILSANR KDMELATATG RLSQPLINRL SLSTAKLNSL
AIGLRQLAVS SGNSVGRVLR RTRVANNLEL EQITVPIGVL LVIFESRPDC LPQVSALAIA
SGNALLLKGG KEASNTNKIL HQLTQEALSI HGVADAIQLV STREEVEDLC KLDKMIDLII
PRGSSELVRD IQRAAKGVPV LGHSEGVCHV YVDNEASMDK AIDVVRDSKC DYPAACNAME
TLLIHRDLLR TPLFDQIIDM LRTEEVKIHA GPRFASYLTF SPSEVKSLRT EYGDLECCIE
VVDSMQDAVD HIHKYGSSHT DVIVTENEET AEQFLQQVDS ACVFWNSSSR FADGYRFGLG
AEVGISTARI HARGPVGLEG LLTTKWVLRG EGHTVADFSE QGSMKYLHES IPVPQGHIN
//
