ID A0A3M9N8Y7_9BACT Unreviewed; 543 AA.
AC A0A3M9N8Y7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
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:RNI33777.1};
GN ORFNames=EFY79_17450 {ECO:0000313|EMBL:RNI33777.1};
OS Hanamia caeni.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Hanamia.
OX NCBI_TaxID=2294116 {ECO:0000313|EMBL:RNI33777.1, ECO:0000313|Proteomes:UP000267223};
RN [1] {ECO:0000313|EMBL:RNI33777.1, ECO:0000313|Proteomes:UP000267223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BO-59 {ECO:0000313|EMBL:RNI33777.1,
RC ECO:0000313|Proteomes:UP000267223};
RA Im W.T.;
RT "Draft genome sequence of Ferruginibacter sp. BO-59.";
RL Submitted (NOV-2018) 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, ECO:0000256|RuleBase:RU003345}.
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:RNI33777.1}.
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DR EMBL; RJJR01000016; RNI33777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M9N8Y7; -.
DR OrthoDB; 629320at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000267223; 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; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003345};
KW Proline metabolism {ECO:0000256|ARBA:ARBA00023062};
KW Reference proteome {ECO:0000313|Proteomes:UP000267223}.
FT DOMAIN 56..512
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
FT ACT_SITE 293
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 543 AA; 60050 MW; B6891463468A1A5A CRC64;
MKIGNFSYPL PANEPVLSYA PGTKERDDLK KALKSLKGKK IDVPMYIGSE EIRTDDKIEI
RPPHEKKFVL GTYNQGTAAD VKKAINAALK AKEKWAALSW GNRANIFLKA ADLIATKYRA
EMCATTMLGQ SKNAFQAEID AACELIDFLR FNVHFLNEIY SQQPVSSAGI HNRMEYRPLE
GFVLAVTPFN FTAIGGNLPT SAAMCGNVVV WKCANTQVFS AQMFMRILKE AGLPDGVVNL
IFVDGPVLGD VCFNHPDFAG IHFTGSTGVF NTMWKHIGEN TKIYKSYPRI VGETGGKDFV
VAHKSADVDV LVTALCRGAF EYQGQKCSAA SRAYIPSNIA AEVKKKLVAE IKTMKMGTVE
DFSNFINAVI DEKSFDKIEE YIKQVKRDKE AKIIVGGKCD KSNGYFIEPT VIEVTNPKYV
TMCNEIFGPV LTIYIYDENK FEETLKLVDT TSPYALTGSI IAQDRNAVEL ATQKLKNSAG
NFYINDKPTG AVVGQQPFGG ARGSGTNDKA GSIINLYRWL SARTIKETFI PATDYRYAFL
KEK
//
