ID A0A0A2VB36_BEABA Unreviewed; 528 AA.
AC A0A0A2VB36;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=BBAD15_g11458 {ECO:0000313|EMBL:KGQ03295.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ03295.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ03295.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ03295.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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:RU366016}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGQ03295.1}.
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; ANFO01001245; KGQ03295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VB36; -.
DR STRING; 1245745.A0A0A2VB36; -.
DR eggNOG; KOG2455; Eukaryota.
DR HOGENOM; CLU_005391_4_1_1; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000030106; Unassembled WGS sequence.
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 InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU366016};
KW Oxidoreductase {ECO:0000256|RuleBase:RU366016};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062,
KW ECO:0000256|RuleBase:RU366016};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT DOMAIN 50..512
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 528 AA; 58068 MW; 779CE8291215E5A1 CRC64;
MPFRLPDERN EPNFEYRKGS LERQKVQQEL QRLRAALPLR SHVICDGQVQ STSESLDQVL
PGEHGTVFTN YPLASRKQVE HAISSMLAVK KEWEDTPFVD RASVFLKAAE LVAGKYRHQL
IAATMLGQGK NFWQAEIDAA AELADFFRLH CNYAAEIMSR QPQRGSDGMW TRVEVSSFGR
LFSAPALMGN VVLWKPSQYN VYASMLVYQI LLEAGLPPGV IQFVPGDAAK VTETVLSHRD
FAGLNFIGSS DVFRKIYAHI GEGIGNKTYR EFPRVIGETS GKNFHLLHPS ADISSAVNHT
IRGAFEYQGQ KCSATSRVYI PQSRADEFFS ELKAGVAAIT MGSPDGDLSA FMGPVIHKDS
FNKIKSIIDA SKNDSSVELV AGGTYDGSVG YYVHPTVYRV SSPDHNLMNQ EIFGPVLAVY
VYEDSEWSCI LESIDRTGGG LALTGAVFAK SRSAIRQAED ALRYAAGNFY INCKTTAALI
GQQSFGGARS SGTNDKAGSS DVLRRFTSPR TVKEEFAPLT GFTYPSNN
//