ID M9LLF9_PSEA3 Unreviewed; 476 AA.
AC M9LLF9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=glutamate-5-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00013002};
DE EC=1.2.1.41 {ECO:0000256|ARBA:ARBA00013002};
GN ORFNames=PANT_7c00054 {ECO:0000313|EMBL:GAC72351.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC72351.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
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; DF196773; GAC72351.1; -; Genomic_DNA.
DR AlphaFoldDB; M9LLF9; -.
DR STRING; 1151754.M9LLF9; -.
DR OrthoDB; 314297at2759; -.
DR UniPathway; UPA00098; UER00360.
DR Proteomes; UP000011976; Unassembled 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; 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; 1.
DR SUPFAM; SSF53720; ALDH-like; 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 Proline biosynthesis {ECO:0000256|ARBA:ARBA00022650};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976}.
FT DOMAIN 127..302
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 476 AA; 50160 MW; BE5BB77369666982 CRC64;
MSASGSAEHV ARQARAAFEA SSHLLSSPSS SASADSVRSS ALLSIRTALE SNRTRIAQAN
ALDMEAATAL VAAGKLSSAL ASRLDLFSKP GKWESLLAGV SDVAALPSPL DHVQWAKRLA
EATDTKGAID LYRVTCPIGV LLCIFEARPE VVVNIASLAI KSGNAAILKG GKESKHTAAV
LSSIIAAALE EAGLPSGLIQ TVETREDIQS LLHLDEYIDL VIPRGSNELV KTIQRDARMP
VMGHADGLCI GYVHEDAELE ATVGTVVDSK TDYPAACNAL ETLLIHDSLV HTSFWPTLAS
ALLSAGVELR CDAATLSALP SSVTSRFEGK IKPAVDVDYS TEFLDLILAV ASVPSLDVAL
SHITTHSSGH TDVLFTSPHS PNAAAAKFTR SINSANVFVN VSSRFADGFR FGLGTEVGIS
TGKTHARGPV GLDGLVIYKY IAKSQPHPTN GPQTAAEFNT KRKWAHTALQ PHYPSF
//
