ID A0A2H3PBA7_9BACT Unreviewed; 547 AA.
AC A0A2H3PBA7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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 Name=pruA {ECO:0000313|EMBL:PEN09548.1};
GN ORFNames=CRI93_02110 {ECO:0000313|EMBL:PEN09548.1};
OS Longimonas halophila.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salisaetaceae;
OC Longimonas.
OX NCBI_TaxID=1469170 {ECO:0000313|EMBL:PEN09548.1, ECO:0000313|Proteomes:UP000221024};
RN [1] {ECO:0000313|EMBL:PEN09548.1, ECO:0000313|Proteomes:UP000221024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42399 {ECO:0000313|EMBL:PEN09548.1,
RC ECO:0000313|Proteomes:UP000221024};
RA Goh K.M., Shamsir M.S., Lim S.W.;
RT "Draft genome of Longimonas halophila.";
RL Submitted (OCT-2017) 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}.
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:PEN09548.1}.
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DR EMBL; PDEP01000001; PEN09548.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H3PBA7; -.
DR OrthoDB; 9762913at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000221024; Unassembled WGS sequence.
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 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000221024}.
FT DOMAIN 61..519
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 59933 MW; BAADF98479D681BC CRC64;
MQNALSTPPN PTNEPVLSYA PGSPERSAIR AELERLRDMT VEIPAYIGGD AVYPGSPSSV
RVPHDHQHEL GTVHQSGANE VEQAIKAARE AKAEWAAMDW TDRAAIFLRA ADLIAGPWRH
TLNAATMLGQ GKNVYQAEID AACELIDFLR FNVHYADQIY REQPDNSPGV WNQVQYRPLE
GFVLAITPFN FTAIQGNLPT APALMGNTVL WKPASRSVYS AYFLYQILEE AGMPAGVINM
LPADEGADVG TPAMASPEFA GLHFTGSKAT FDHLWKTVGE NLDTYRTYPT IVGETGGKDF
IVAHPSAHPA QTATAIVRGS FEYQGQKCSA SSRIYLPESL WPTIKEELAE QIESLQVGPP
EDLTNFVNAV IDQRAFDEIT GYIDRAKASD DAEILFGGDY DDSTGYFINP TVILATDPHY
ESMEEEIFGP VTTIYVYDDA DYEATLDLID STSPYALTGA VFAEDRAAIR TTMDHLEHSA
GNFYINDKPT GAVVGQQPFG GARKSGTNDK AGSALNLHRW ISPRSIKETF NPPTHYGYAF
HQPDKDA
//