ID B9PHW6_TOXGV Unreviewed; 502 AA.
AC B9PHW6; A0A0F7V3F2; A0A0N5ECQ6; B6KCZ8; B9Q610; S7V513; S8G9K3;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE RecName: Full=glutamate-5-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013002};
DE EC=1.2.1.41 {ECO:0000256|ARBA:ARBA00013002};
GN ORFNames=BN1205_017830 {ECO:0000313|EMBL:CEL75319.1}, TGVEG_270550
GN {ECO:0000313|EMBL:ESS36236.1};
OS Toxoplasma gondii (strain ATCC 50861 / VEG).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=432359 {ECO:0000313|EMBL:ESS36236.1, ECO:0000313|Proteomes:UP000002226};
RN [1] {ECO:0000313|EMBL:ESS36236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS36236.1};
RA Paulsen I.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50861 / VEG {ECO:0000313|Proteomes:UP000002226};
RA Lorenzi H., Inman J., Amedeo P., Brunk B., Roos D., Caler E.;
RT "Annotation of Toxoplasma gondii VEG.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ESS36236.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:ESS36236.1};
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:CEL75319.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VEG {ECO:0000313|EMBL:CEL75319.1};
RX PubMed=25875305; DOI=10.1371/journal.pone.0124473;
RA Ramaprasad A., Mourier T., Naeem R., Malas T.B., Moussa E., Panigrahi A.,
RA Vermont S.J., Otto T.D., Wastling J., Pain A.;
RT "Comprehensive Evaluation of Toxoplasma gondii VEG and Neospora caninum LIV
RT Genomes with Tachyzoite Stage Transcriptome and Proteome Defines Novel
RT Transcript Features.";
RL PLoS ONE 10:e0124473-e0124473(2015).
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 2/2.
CC {ECO:0000256|ARBA:ARBA00004985}.
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; LN714498; CEL75319.1; -; Genomic_DNA.
DR EMBL; AAYL02000011; ESS36236.1; -; Genomic_DNA.
DR AlphaFoldDB; B9PHW6; -.
DR STRING; 432359.B9PHW6; -.
DR PaxDb; 5811-TGME49_070550; -.
DR EnsemblProtists; ESS36236; ESS36236; TGVEG_270550.
DR VEuPathDB; ToxoDB:TGVEG_270550; -.
DR eggNOG; KOG4165; Eukaryota.
DR OMA; PGVCNAM; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000002226; Partially assembled WGS sequence.
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 CDD; cd07079; ALDH_F18-19_ProA-GPR; 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; IPR000965; GPR_dom.
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; 2.
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 NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:ESS36236.1};
KW Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000002226}.
FT DOMAIN 46..326
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT DOMAIN 367..432
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 54410 MW; 1F3A3DAFDEEE36F7 CRC64;
MSLQGMNVVE SGTLAPEEAK KMQNDSEDKI DGPDVSTQNG ESKPGSVRLM AQLARAASRL
LQTSTLEERN AALQAYKDGL VHFREEIEAA NQRELEAAKV AVAAGELSSP VFQRLNCRGQ
KFETLLSGLD SLIAKDDPLG VCDLATELGS HLELFRLSCP IGVIAVIYEA RPEAAVQVAG
LALKTGNALL LKGGKEARET NRAVFKALRW GLEKAASAAI SREVLQLIED RQEVTELLQL
DDEVDLVVPR GSNSLVKYIK ENTRIPVLGH ADGICHIYVD AAADLGKAAK IVADSKLQYV
AACNTVESLL VHREILPTFL PAIISQLALR GVTFKVDSAA LEVLKTQAVH TLEAHAQFVA
VASEHDFHTE WLAPVLAVKT VDSLQEAIAH INSHGSHHTD CIITENKAHA EQFMKGVDSA
GCYCNCSTRF ADGYRYGFGA EVGVSTNKIH ARGPVGLQGL VTYKYCLYGD GHTVGDFEEG
RARYTHRPLA TDKPRSERQL AN
//