ID A0A1A0ME35_9MYCO Unreviewed; 543 AA.
AC A0A1A0ME35;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=A9W99_07120 {ECO:0000313|EMBL:OBA83754.1};
OS Mycobacterium sp. 1164966.3.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1856861 {ECO:0000313|EMBL:OBA83754.1, ECO:0000313|Proteomes:UP000092060};
RN [1] {ECO:0000313|Proteomes:UP000092060}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1164966.3 {ECO:0000313|Proteomes:UP000092060};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA Lopez-Varela E., Palencia S.;
RL Submitted (JUN-2016) 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:OBA83754.1}.
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DR EMBL; LZSG01000006; OBA83754.1; -; Genomic_DNA.
DR RefSeq; WP_067373714.1; NZ_LZSG01000006.1.
DR AlphaFoldDB; A0A1A0ME35; -.
DR STRING; 1856861.A9W99_07120; -.
DR OrthoDB; 6882680at2; -.
DR UniPathway; UPA00261; UER00374.
DR Proteomes; UP000092060; 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:UP000092060}.
FT DOMAIN 53..524
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF00171"
SQ SEQUENCE 543 AA; 58949 MW; D8C70B08A2843544 CRC64;
MDAISQVPAP VNEPVHDYAP HSPERARLAT ELAALADHPI DLPHVIGGRH RMGDGERIDV
VQPHRHAAKL GTLTNAVHAD ASAAVEAAMN AKKAWAATPF DERAAVFLRA ADLLAGPWRE
KIAAATMLGQ SKSVYQAEID APCELIDFWR FNVEFARQIL AQQPISGPGE WNRSDYRPLD
GFVYAITPFN FTSIAGNLPT APALMGNTVV WKPSITQTLS AYLLMQLLEA AGLPPGVINM
VTGDGFAVSD VALGDRRLAG IHFTGSTATF QRLWYQVGTN IGRYHCYPRL VGETGGKDFV
LAHTSAHPDV LRTALIRGAF DYQGQKCSAA SRAFIAHSVW QRMGDSFLGA AEELSYGDIT
DLTNYGGALI DRRAFLKNVD AIERAKGAPA VTIAVGGEYD DHEGYFVRPT VFLSDDPTDE
SFATEYFGPL LSVHVYPDDQ FERILDVIDT GSRYALTGAV IADDRRAVLT AQERLRFAAG
NFYVNDKPTG AVVGRQPFGG SRGSGTNDKA GSPLNLLRWT SARTIKETFV PATDHIYPHM
GPD
//
