ID E4ZLT6_LEPMJ Unreviewed; 584 AA.
AC E4ZLT6;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU366016, ECO:0000256|RuleBase:RU366030};
DE Includes:
DE RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000256|RuleBase:RU366030};
DE Short=P5C dehydrogenase {ECO:0000256|RuleBase:RU366030};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU366030};
DE Includes:
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|RuleBase:RU366016};
DE EC=1.2.1.88 {ECO:0000256|RuleBase:RU366016};
GN ORFNames=LEMA_P054720.1 {ECO:0000313|EMBL:CBX92766.1};
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Plenodomus; Plenodomus lingam/Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895 {ECO:0000313|Proteomes:UP000002668};
RN [1] {ECO:0000313|Proteomes:UP000002668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8
RC {ECO:0000313|Proteomes:UP000002668};
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamate 5-semialdehyde + NAD(+) = 2 H(+) + L-
CC glutamate + NADH; Xref=Rhea:RHEA:30235, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58066; EC=1.2.1.88;
CC Evidence={ECO:0000256|ARBA:ARBA00001468,
CC ECO:0000256|RuleBase:RU366016};
CC -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786, ECO:0000256|RuleBase:RU366016}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|RuleBase:RU003345}.
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DR EMBL; FP929094; CBX92766.1; -; Genomic_DNA.
DR RefSeq; XP_003836131.1; XM_003836083.1.
DR AlphaFoldDB; E4ZLT6; -.
DR STRING; 985895.E4ZLT6; -.
DR EnsemblFungi; CBX92766; CBX92766; LEMA_P054720.1.
DR GeneID; 13287055; -.
DR eggNOG; KOG2455; Eukaryota.
DR HOGENOM; CLU_005391_4_1_1; -.
DR InParanoid; E4ZLT6; -.
DR OMA; FAGIHFT; -.
DR OrthoDB; 4536at2759; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000002668; Genome.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR005931; P5CDH/ALDH4A1.
DR NCBIfam; TIGR01236; D1pyr5carbox1; 1.
DR PANTHER; PTHR42862; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR42862:SF1; DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU366016};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062,
KW ECO:0000256|RuleBase:RU366016};
KW Reference proteome {ECO:0000313|Proteomes:UP000002668}.
FT DOMAIN 94..566
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 332
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 584 AA; 63738 MW; 60FC8D0E1C746ECD CRC64;
MVPSKSLRPL RSATKTLNSL PVAYAGAQVA SRRYAGSIAN FKLPTINNEP NQHYAKGSVD
RQRLQEAIAR LKKQGPVQVP LAVGGEYINN SSILTQHNPS SHADVVAKYS NASKADVKKA
IDSALAAKPA WEALPFAERA AVFLKAADLV STKYRYEIMA ATMVGQGKNA WQAEIDAAAE
LCDFLRFNVK YAEETYGIQP THNSPGVWNR VEYRPLEGFV YAVSPFNFTA IGGNLPAAPA
LMGNVVVWKP SPAAITSNWL LYQILIEAGL PPNVVQWVPG DAVEVTQEVL SHRQFAALHY
TGSTAVFRSL YGKIAGGVAE GKYQSYPRIV GETGGKNFHL IHKDADIHNA AIQTVRGAFE
YQGQKCSACS RLYVPKSVWP EFKEILVKEV EALKIGEPSD FSNFIGPVIH EASFKKLSGV
IDEAKNDSEL KLIVGGKHDS SKGYFIHPTI YETTNPNHPL LSRELFGPIL VAYVYDDAAP
DAFTKIIKQI DETSEYALTG AVFAKDRETI KYASDKLRNT AGNFYINCKS TGAVVGQQPF
GGSRASGTND KAGSANLLAR FVNMRSIKEE FLPTEKVAYP SNEV
//
