ID E1TIM3_BURSG Unreviewed; 537 AA.
AC E1TIM3;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00012884};
DE EC=1.2.1.88 {ECO:0000256|ARBA:ARBA00012884};
DE AltName: Full=L-glutamate gamma-semialdehyde dehydrogenase {ECO:0000256|ARBA:ARBA00032259};
GN OrderedLocusNames=BC1003_6034 {ECO:0000313|EMBL:ADN61932.1};
OS Burkholderia sp. (strain CCGE1003).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=640512 {ECO:0000313|EMBL:ADN61932.1};
RN [1] {ECO:0000313|EMBL:ADN61932.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCGE1003 {ECO:0000313|EMBL:ADN61932.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Daligault H., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G.,
RA Martinez-Romero E., Rogel M.A., Auchtung J., Tiedje J.M., Woyke T.;
RT "Complete sequence of chromosome2 of Burkholderia sp. CCGE1003.";
RL Submitted (SEP-2010) 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 -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC glutamate; L-glutamate from L-proline: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004786}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009986}.
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DR EMBL; CP002218; ADN61932.1; -; Genomic_DNA.
DR AlphaFoldDB; E1TIM3; -.
DR STRING; 640512.BC1003_6034; -.
DR KEGG; bgf:BC1003_6034; -.
DR eggNOG; COG1012; Bacteria.
DR HOGENOM; CLU_005391_4_1_4; -.
DR OrthoDB; 9762913at2; -.
DR UniPathway; UPA00261; UER00374.
DR GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0010133; P:proline catabolic process to glutamate; IEA:UniProtKB-UniPathway.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062}.
FT DOMAIN 54..511
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 537 AA; 57724 MW; 117581FAEB966562 CRC64;
MNSSPNFPLP ANEPEVHFGT GTAAAAQLQQ ALNARDVVEI PTVIGGKRYF SNDVVEVRAP
HDQSRLLARI HRPTEAQINE AIANAKSVSR DWASLPFASR ATIMHRSADI IATRQRMRIN
AATVLGQSKT IDQAEPDAAC ELIDFLRFNA FNAQRVYAEQ SASVSTAVNR TDWRPLEGFV
YAVSPFNFTA IGGNLTTAPA IMGNPVLWKP SEKSALANWI FYEALEEAGL PAGVINFVPG
EAELTTRAVL NSADLAGIHF TGSSAVFQSL WKGVASKVES FRTIPRLVGE TGGKDFVLAH
ASAHPSEVAI ALIRGAFEYC GQKCSAASRA YVPQSLWPAV RDEMVARLAQ LKVGDPADLG
NTFMGAVISQ ASHAKLTAVL NAAKDDSKVK IVSGGKTWSE PGFFVEPTVL EVSDPKHALM
TEELFGPVLS VFVYNDNAWS DTLALIDATS PYALTGSIFC TDRFALHEAE AALVNAAGNL
YLNDKPTGAM IGQQPFGGGR ASGTNDKAGS YLNLLRWASP RVVKETYLPP REWTFGG
//
