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Database: UniProt
Entry: A0A2H3PBA7_9BACT
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Original site: A0A2H3PBA7_9BACT 
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
//
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