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Database: UniProt
Entry: B9PHW6_TOXGV
LinkDB: B9PHW6_TOXGV
Original site: B9PHW6_TOXGV 
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}.
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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
//
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